JP5583591B2 - Ｗｉｓｅ結合抗体及びエピトープ - Google Patents
Ｗｉｓｅ結合抗体及びエピトープ Download PDFInfo
- Publication number
- JP5583591B2 JP5583591B2 JP2010534969A JP2010534969A JP5583591B2 JP 5583591 B2 JP5583591 B2 JP 5583591B2 JP 2010534969 A JP2010534969 A JP 2010534969A JP 2010534969 A JP2010534969 A JP 2010534969A JP 5583591 B2 JP5583591 B2 JP 5583591B2
- Authority
- JP
- Japan
- Prior art keywords
- seq
- wise
- antibody
- antigen
- binding
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 102100022432 Sclerostin domain-containing protein 1 Human genes 0.000 title claims description 259
- 101100366217 Gallus gallus SOSTDC1 gene Proteins 0.000 title claims description 251
- 230000027455 binding Effects 0.000 title claims description 136
- 238000009739 binding Methods 0.000 title claims description 134
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 129
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 113
- 101000825071 Homo sapiens Sclerostin domain-containing protein 1 Proteins 0.000 claims description 109
- 229920001184 polypeptide Polymers 0.000 claims description 106
- 102000057897 human SOSTDC1 Human genes 0.000 claims description 95
- 238000000034 method Methods 0.000 claims description 74
- 239000012634 fragment Substances 0.000 claims description 69
- 239000002773 nucleotide Substances 0.000 claims description 64
- 125000003729 nucleotide group Chemical group 0.000 claims description 64
- 229940024606 amino acid Drugs 0.000 claims description 62
- 150000001413 amino acids Chemical class 0.000 claims description 62
- 230000000694 effects Effects 0.000 claims description 43
- 239000000427 antigen Substances 0.000 claims description 42
- 108091007433 antigens Proteins 0.000 claims description 42
- 102000036639 antigens Human genes 0.000 claims description 42
- 108010047041 Complementarity Determining Regions Proteins 0.000 claims description 40
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 37
- 230000014509 gene expression Effects 0.000 claims description 35
- 206010016654 Fibrosis Diseases 0.000 claims description 31
- 230000004761 fibrosis Effects 0.000 claims description 31
- 238000011282 treatment Methods 0.000 claims description 30
- 230000002829 reductive effect Effects 0.000 claims description 22
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 21
- 238000000423 cell based assay Methods 0.000 claims description 20
- 125000000539 amino acid group Chemical group 0.000 claims description 19
- 210000003734 kidney Anatomy 0.000 claims description 19
- 201000001474 proteinuria Diseases 0.000 claims description 18
- 102000004264 Osteopontin Human genes 0.000 claims description 17
- 108010081689 Osteopontin Proteins 0.000 claims description 17
- 201000010099 disease Diseases 0.000 claims description 14
- 230000002401 inhibitory effect Effects 0.000 claims description 14
- 208000004852 Lung Injury Diseases 0.000 claims description 13
- 206010069363 Traumatic lung injury Diseases 0.000 claims description 13
- 230000002163 immunogen Effects 0.000 claims description 12
- 231100000515 lung injury Toxicity 0.000 claims description 12
- 206010028980 Neoplasm Diseases 0.000 claims description 11
- 208000017169 kidney disease Diseases 0.000 claims description 8
- 239000003550 marker Substances 0.000 claims description 8
- 239000008194 pharmaceutical composition Substances 0.000 claims description 8
- 238000003776 cleavage reaction Methods 0.000 claims description 7
- 238000004519 manufacturing process Methods 0.000 claims description 6
- 210000000651 myofibroblast Anatomy 0.000 claims description 6
- 230000007017 scission Effects 0.000 claims description 6
- 206010061481 Renal injury Diseases 0.000 claims description 5
- 239000003085 diluting agent Substances 0.000 claims description 5
- 208000037806 kidney injury Diseases 0.000 claims description 5
- 230000007170 pathology Effects 0.000 claims description 5
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 4
- 239000004473 Threonine Substances 0.000 claims description 4
- 238000013424 sirius red staining Methods 0.000 claims description 4
- 208000037816 tissue injury Diseases 0.000 claims description 4
- 108010088751 Albumins Proteins 0.000 claims description 3
- 102000009027 Albumins Human genes 0.000 claims description 3
- 208000019693 Lung disease Diseases 0.000 claims description 3
- 230000037319 collagen production Effects 0.000 claims description 3
- 239000003937 drug carrier Substances 0.000 claims description 3
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 3
- 102000004338 Transferrin Human genes 0.000 claims description 2
- 108090000901 Transferrin Proteins 0.000 claims description 2
- 239000012581 transferrin Substances 0.000 claims description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims 2
- 229960000310 isoleucine Drugs 0.000 claims 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims 2
- 102100029880 Glycodelin Human genes 0.000 claims 1
- 101000585553 Homo sapiens Glycodelin Proteins 0.000 claims 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 claims 1
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 121
- 239000011230 binding agent Substances 0.000 description 110
- 210000004027 cell Anatomy 0.000 description 92
- 235000001014 amino acid Nutrition 0.000 description 66
- 108090000623 proteins and genes Proteins 0.000 description 63
- 241000282414 Homo sapiens Species 0.000 description 60
- 102000004169 proteins and genes Human genes 0.000 description 57
- 235000018102 proteins Nutrition 0.000 description 54
- 239000000203 mixture Substances 0.000 description 50
- 238000003556 assay Methods 0.000 description 40
- 239000000243 solution Substances 0.000 description 39
- 241000699666 Mus <mouse, genus> Species 0.000 description 36
- 241000699670 Mus sp. Species 0.000 description 32
- 238000012360 testing method Methods 0.000 description 30
- 238000002965 ELISA Methods 0.000 description 26
- 210000004408 hybridoma Anatomy 0.000 description 25
- 125000003275 alpha amino acid group Chemical group 0.000 description 22
- 241001465754 Metazoa Species 0.000 description 20
- 238000006467 substitution reaction Methods 0.000 description 20
- 108020004414 DNA Proteins 0.000 description 19
- 241000700159 Rattus Species 0.000 description 19
- 210000004072 lung Anatomy 0.000 description 19
- 210000003719 b-lymphocyte Anatomy 0.000 description 18
- 239000001963 growth medium Substances 0.000 description 15
- 108010006654 Bleomycin Proteins 0.000 description 14
- 229960001561 bleomycin Drugs 0.000 description 14
- OYVAGSVQBOHSSS-UAPAGMARSA-O bleomycin A2 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC=C(N=1)C=1SC=C(N=1)C(=O)NCCC[S+](C)C)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C OYVAGSVQBOHSSS-UAPAGMARSA-O 0.000 description 14
- 238000003752 polymerase chain reaction Methods 0.000 description 14
- 238000000746 purification Methods 0.000 description 14
- 230000001225 therapeutic effect Effects 0.000 description 14
- 239000013598 vector Substances 0.000 description 14
- 102000008186 Collagen Human genes 0.000 description 13
- 108010035532 Collagen Proteins 0.000 description 13
- 229920001436 collagen Polymers 0.000 description 13
- 230000004069 differentiation Effects 0.000 description 13
- 239000002609 medium Substances 0.000 description 13
- LEVWYRKDKASIDU-IMJSIDKUSA-N L-cystine Chemical compound [O-]C(=O)[C@@H]([NH3+])CSSC[C@H]([NH3+])C([O-])=O LEVWYRKDKASIDU-IMJSIDKUSA-N 0.000 description 12
- 229960003067 cystine Drugs 0.000 description 12
- 210000002966 serum Anatomy 0.000 description 12
- 239000006228 supernatant Substances 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 11
- 102000004142 Trypsin Human genes 0.000 description 11
- 108090000631 Trypsin Proteins 0.000 description 11
- 102000013814 Wnt Human genes 0.000 description 11
- 108050003627 Wnt Proteins 0.000 description 11
- 238000000576 coating method Methods 0.000 description 11
- 210000004602 germ cell Anatomy 0.000 description 11
- 238000000159 protein binding assay Methods 0.000 description 11
- 239000012588 trypsin Substances 0.000 description 11
- 239000005089 Luciferase Substances 0.000 description 10
- 101100366219 Mus musculus Sostdc1 gene Proteins 0.000 description 10
- 239000003153 chemical reaction reagent Substances 0.000 description 10
- 239000011248 coating agent Substances 0.000 description 10
- 230000008021 deposition Effects 0.000 description 10
- 230000029087 digestion Effects 0.000 description 10
- 229940027941 immunoglobulin g Drugs 0.000 description 10
- 229920001223 polyethylene glycol Polymers 0.000 description 10
- 230000011664 signaling Effects 0.000 description 10
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 9
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 9
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 9
- 239000002202 Polyethylene glycol Substances 0.000 description 9
- 230000008859 change Effects 0.000 description 9
- 238000012875 competitive assay Methods 0.000 description 9
- 230000004927 fusion Effects 0.000 description 9
- 239000012071 phase Substances 0.000 description 9
- 230000004952 protein activity Effects 0.000 description 9
- 241000588724 Escherichia coli Species 0.000 description 8
- 108060001084 Luciferase Proteins 0.000 description 8
- 241000282567 Macaca fascicularis Species 0.000 description 8
- 238000002835 absorbance Methods 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 230000004071 biological effect Effects 0.000 description 8
- 230000000903 blocking effect Effects 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 230000003053 immunization Effects 0.000 description 8
- 238000001727 in vivo Methods 0.000 description 8
- 230000035772 mutation Effects 0.000 description 8
- 230000003472 neutralizing effect Effects 0.000 description 8
- 239000002904 solvent Substances 0.000 description 8
- 239000003981 vehicle Substances 0.000 description 8
- 102000014914 Carrier Proteins Human genes 0.000 description 7
- 241000124008 Mammalia Species 0.000 description 7
- 229920001213 Polysorbate 20 Polymers 0.000 description 7
- 108091008324 binding proteins Proteins 0.000 description 7
- 230000002860 competitive effect Effects 0.000 description 7
- 208000035475 disorder Diseases 0.000 description 7
- 239000013604 expression vector Substances 0.000 description 7
- 238000009472 formulation Methods 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- 238000002347 injection Methods 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 7
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 7
- 230000000069 prophylactic effect Effects 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- 239000011780 sodium chloride Substances 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 6
- 108060003951 Immunoglobulin Proteins 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 206010035226 Plasma cell myeloma Diseases 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 239000012930 cell culture fluid Substances 0.000 description 6
- 239000003795 chemical substances by application Substances 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 239000003814 drug Substances 0.000 description 6
- 230000003176 fibrotic effect Effects 0.000 description 6
- 239000012530 fluid Substances 0.000 description 6
- 229960002897 heparin Drugs 0.000 description 6
- 229920000669 heparin Polymers 0.000 description 6
- 102000018358 immunoglobulin Human genes 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- 229940090044 injection Drugs 0.000 description 6
- 210000004962 mammalian cell Anatomy 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 239000008188 pellet Substances 0.000 description 6
- 108091033319 polynucleotide Proteins 0.000 description 6
- 102000040430 polynucleotide Human genes 0.000 description 6
- 239000002157 polynucleotide Substances 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 230000001603 reducing effect Effects 0.000 description 6
- 230000009467 reduction Effects 0.000 description 6
- 238000012216 screening Methods 0.000 description 6
- -1 such as the CDR-H1 Proteins 0.000 description 6
- 210000002700 urine Anatomy 0.000 description 6
- 241000699660 Mus musculus Species 0.000 description 5
- 102100023087 Protein S100-A4 Human genes 0.000 description 5
- 101710120037 Toxin CcdB Proteins 0.000 description 5
- 208000004608 Ureteral Obstruction Diseases 0.000 description 5
- 201000011510 cancer Diseases 0.000 description 5
- 208000020832 chronic kidney disease Diseases 0.000 description 5
- 235000018417 cysteine Nutrition 0.000 description 5
- 230000003247 decreasing effect Effects 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 238000000502 dialysis Methods 0.000 description 5
- 229940079593 drug Drugs 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 238000004128 high performance liquid chromatography Methods 0.000 description 5
- 238000002649 immunization Methods 0.000 description 5
- 210000003000 inclusion body Anatomy 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- 239000003446 ligand Substances 0.000 description 5
- 239000002502 liposome Substances 0.000 description 5
- 238000003670 luciferase enzyme activity assay Methods 0.000 description 5
- 201000000050 myeloid neoplasm Diseases 0.000 description 5
- 238000004091 panning Methods 0.000 description 5
- 239000002245 particle Substances 0.000 description 5
- 229920000642 polymer Polymers 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 238000011321 prophylaxis Methods 0.000 description 5
- 208000005069 pulmonary fibrosis Diseases 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 210000000952 spleen Anatomy 0.000 description 5
- 208000024891 symptom Diseases 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 238000001890 transfection Methods 0.000 description 5
- 238000011830 transgenic mouse model Methods 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- 241000283707 Capra Species 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 4
- 101710204931 Ferroptosis suppressor protein 1 Proteins 0.000 description 4
- 102000016359 Fibronectins Human genes 0.000 description 4
- 108010067306 Fibronectins Proteins 0.000 description 4
- 206010018364 Glomerulonephritis Diseases 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 201000009794 Idiopathic Pulmonary Fibrosis Diseases 0.000 description 4
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 4
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 4
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 4
- 206010027476 Metastases Diseases 0.000 description 4
- MUBZPKHOEPUJKR-UHFFFAOYSA-N Oxalic acid Chemical compound OC(=O)C(O)=O MUBZPKHOEPUJKR-UHFFFAOYSA-N 0.000 description 4
- 239000004365 Protease Substances 0.000 description 4
- 101710169324 Sclerostin domain-containing protein 1 Proteins 0.000 description 4
- 239000011324 bead Substances 0.000 description 4
- 239000012472 biological sample Substances 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 150000001720 carbohydrates Chemical class 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 239000006285 cell suspension Substances 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000012512 characterization method Methods 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 4
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 4
- 230000006378 damage Effects 0.000 description 4
- 238000011161 development Methods 0.000 description 4
- 230000018109 developmental process Effects 0.000 description 4
- 239000006185 dispersion Substances 0.000 description 4
- 238000002955 isolation Methods 0.000 description 4
- 230000003907 kidney function Effects 0.000 description 4
- 238000011813 knockout mouse model Methods 0.000 description 4
- 150000002632 lipids Chemical class 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 230000009401 metastasis Effects 0.000 description 4
- 238000010172 mouse model Methods 0.000 description 4
- 230000000717 retained effect Effects 0.000 description 4
- 238000004007 reversed phase HPLC Methods 0.000 description 4
- 238000002741 site-directed mutagenesis Methods 0.000 description 4
- 230000009466 transformation Effects 0.000 description 4
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
- 102000007469 Actins Human genes 0.000 description 3
- 108010085238 Actins Proteins 0.000 description 3
- 239000004475 Arginine Substances 0.000 description 3
- 208000007342 Diabetic Nephropathies Diseases 0.000 description 3
- 238000012286 ELISA Assay Methods 0.000 description 3
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 3
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 3
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 3
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 3
- 230000004988 N-glycosylation Effects 0.000 description 3
- 108090000526 Papain Proteins 0.000 description 3
- 102000057297 Pepsin A Human genes 0.000 description 3
- 108090000284 Pepsin A Proteins 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- 101100366221 Rattus norvegicus Sostdc1 gene Proteins 0.000 description 3
- 241000283984 Rodentia Species 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 3
- 206010039710 Scleroderma Diseases 0.000 description 3
- 208000034189 Sclerosis Diseases 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 239000003242 anti bacterial agent Substances 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 238000013329 compounding Methods 0.000 description 3
- 208000033679 diabetic kidney disease Diseases 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 208000028208 end stage renal disease Diseases 0.000 description 3
- 201000000523 end stage renal failure Diseases 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 238000005194 fractionation Methods 0.000 description 3
- 238000010353 genetic engineering Methods 0.000 description 3
- 210000000585 glomerular basement membrane Anatomy 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 230000016784 immunoglobulin production Effects 0.000 description 3
- 238000005462 in vivo assay Methods 0.000 description 3
- 208000036971 interstitial lung disease 2 Diseases 0.000 description 3
- 201000006370 kidney failure Diseases 0.000 description 3
- 210000004698 lymphocyte Anatomy 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 239000002088 nanocapsule Substances 0.000 description 3
- 238000006386 neutralization reaction Methods 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 210000000056 organ Anatomy 0.000 description 3
- 229940055729 papain Drugs 0.000 description 3
- 235000019834 papain Nutrition 0.000 description 3
- 229940111202 pepsin Drugs 0.000 description 3
- 238000002823 phage display Methods 0.000 description 3
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 201000002793 renal fibrosis Diseases 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 238000013207 serial dilution Methods 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 238000007920 subcutaneous administration Methods 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 3
- 238000002054 transplantation Methods 0.000 description 3
- 239000004474 valine Substances 0.000 description 3
- 229920003169 water-soluble polymer Polymers 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- 229920001817 Agar Polymers 0.000 description 2
- 108010032595 Antibody Binding Sites Proteins 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 208000028006 Corneal injury Diseases 0.000 description 2
- 206010011044 Corneal scar Diseases 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 239000004971 Cross linker Substances 0.000 description 2
- 201000003883 Cystic fibrosis Diseases 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 206010058314 Dysplasia Diseases 0.000 description 2
- 241000283086 Equidae Species 0.000 description 2
- 102000003951 Erythropoietin Human genes 0.000 description 2
- 108090000394 Erythropoietin Proteins 0.000 description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- 208000010412 Glaucoma Diseases 0.000 description 2
- 208000022461 Glomerular disease Diseases 0.000 description 2
- 206010018372 Glomerulonephritis membranous Diseases 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 2
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- 206010058031 Joint adhesion Diseases 0.000 description 2
- 208000008839 Kidney Neoplasms Diseases 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 208000001647 Renal Insufficiency Diseases 0.000 description 2
- 208000019802 Sexually transmitted disease Diseases 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 2
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 230000001154 acute effect Effects 0.000 description 2
- 238000011374 additional therapy Methods 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 150000001412 amines Chemical class 0.000 description 2
- 239000002333 angiotensin II receptor antagonist Substances 0.000 description 2
- 229940125364 angiotensin receptor blocker Drugs 0.000 description 2
- 210000004102 animal cell Anatomy 0.000 description 2
- 230000000844 anti-bacterial effect Effects 0.000 description 2
- 239000003429 antifungal agent Substances 0.000 description 2
- 229940121375 antifungal agent Drugs 0.000 description 2
- 239000012736 aqueous medium Substances 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 229940046731 calcineurin inhibitors Drugs 0.000 description 2
- 230000007910 cell fusion Effects 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 2
- 229960004316 cisplatin Drugs 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 239000003636 conditioned culture medium Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 239000002612 dispersion medium Substances 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 210000002919 epithelial cell Anatomy 0.000 description 2
- 229940105423 erythropoietin Drugs 0.000 description 2
- 230000029142 excretion Effects 0.000 description 2
- 239000000835 fiber Substances 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 231100000852 glomerular disease Toxicity 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 229960000789 guanidine hydrochloride Drugs 0.000 description 2
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 238000012151 immunohistochemical method Methods 0.000 description 2
- 238000003364 immunohistochemistry Methods 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000007918 intramuscular administration Methods 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 239000007951 isotonicity adjuster Substances 0.000 description 2
- 238000012004 kinetic exclusion assay Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 210000005265 lung cell Anatomy 0.000 description 2
- 210000001165 lymph node Anatomy 0.000 description 2
- 239000012139 lysis buffer Substances 0.000 description 2
- 238000012423 maintenance Methods 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- 238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 201000008350 membranous glomerulonephritis Diseases 0.000 description 2
- 231100000855 membranous nephropathy Toxicity 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 230000003589 nefrotoxic effect Effects 0.000 description 2
- 231100000381 nephrotoxic Toxicity 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 208000002154 non-small cell lung carcinoma Diseases 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 210000005259 peripheral blood Anatomy 0.000 description 2
- 239000011886 peripheral blood Substances 0.000 description 2
- 210000004976 peripheral blood cell Anatomy 0.000 description 2
- 229920001451 polypropylene glycol Polymers 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- XOJVVFBFDXDTEG-UHFFFAOYSA-N pristane Chemical compound CC(C)CCCC(C)CCCC(C)CCCC(C)C XOJVVFBFDXDTEG-UHFFFAOYSA-N 0.000 description 2
- 238000004393 prognosis Methods 0.000 description 2
- 230000013777 protein digestion Effects 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 231100000241 scar Toxicity 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 239000002002 slurry Substances 0.000 description 2
- 210000002460 smooth muscle Anatomy 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 238000001356 surgical procedure Methods 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 230000008685 targeting Effects 0.000 description 2
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 2
- 238000011269 treatment regimen Methods 0.000 description 2
- GETQZCLCWQTVFV-UHFFFAOYSA-N trimethylamine Chemical compound CN(C)C GETQZCLCWQTVFV-UHFFFAOYSA-N 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 208000029729 tumor suppressor gene on chromosome 11 Diseases 0.000 description 2
- QBYIENPQHBMVBV-HFEGYEGKSA-N (2R)-2-hydroxy-2-phenylacetic acid Chemical compound O[C@@H](C(O)=O)c1ccccc1.O[C@@H](C(O)=O)c1ccccc1 QBYIENPQHBMVBV-HFEGYEGKSA-N 0.000 description 1
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- IEJPPSMHUUQABK-UHFFFAOYSA-N 2,4-diphenyl-4h-1,3-oxazol-5-one Chemical compound O=C1OC(C=2C=CC=CC=2)=NC1C1=CC=CC=C1 IEJPPSMHUUQABK-UHFFFAOYSA-N 0.000 description 1
- TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 1
- 239000005541 ACE inhibitor Substances 0.000 description 1
- 206010001052 Acute respiratory distress syndrome Diseases 0.000 description 1
- 206010067484 Adverse reaction Diseases 0.000 description 1
- 208000024985 Alport syndrome Diseases 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 102000008102 Ankyrins Human genes 0.000 description 1
- 108010049777 Ankyrins Proteins 0.000 description 1
- 241001156002 Anthonomus pomorum Species 0.000 description 1
- 101000725156 Aplysia californica Cerebral peptide 1 Proteins 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 102220549033 B-cell linker protein_Y91F_mutation Human genes 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 208000008439 Biliary Liver Cirrhosis Diseases 0.000 description 1
- 206010004659 Biliary cirrhosis Diseases 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 102100021786 CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase Human genes 0.000 description 1
- 102000000905 Cadherin Human genes 0.000 description 1
- 108050007957 Cadherin Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000282832 Camelidae Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 101710132601 Capsid protein Proteins 0.000 description 1
- 102000005367 Carboxypeptidases Human genes 0.000 description 1
- 108010006303 Carboxypeptidases Proteins 0.000 description 1
- 208000031229 Cardiomyopathies Diseases 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 206010009208 Cirrhosis alcoholic Diseases 0.000 description 1
- 101710094648 Coat protein Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 208000026372 Congenital cystic kidney disease Diseases 0.000 description 1
- 208000016998 Conn syndrome Diseases 0.000 description 1
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
- 108010036949 Cyclosporine Proteins 0.000 description 1
- 102100025287 Cytochrome b Human genes 0.000 description 1
- 108010075028 Cytochromes b Proteins 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 108010019673 Darbepoetin alfa Proteins 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- FEWJPZIEWOKRBE-JCYAYHJZSA-N Dextrotartaric acid Chemical compound OC(=O)[C@H](O)[C@@H](O)C(O)=O FEWJPZIEWOKRBE-JCYAYHJZSA-N 0.000 description 1
- 238000009007 Diagnostic Kit Methods 0.000 description 1
- 206010061818 Disease progression Diseases 0.000 description 1
- SNRUBQQJIBEYMU-UHFFFAOYSA-N Dodecane Natural products CCCCCCCCCCCC SNRUBQQJIBEYMU-UHFFFAOYSA-N 0.000 description 1
- 208000001708 Dupuytren contracture Diseases 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 206010071309 Epidural fibrosis Diseases 0.000 description 1
- 108010074604 Epoetin Alfa Proteins 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 208000007217 Esophageal Stenosis Diseases 0.000 description 1
- 108010008177 Fd immunoglobulins Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 102100024802 Fibroblast growth factor 23 Human genes 0.000 description 1
- 241000724791 Filamentous phage Species 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 201000006004 Gitelman syndrome Diseases 0.000 description 1
- 206010018367 Glomerulonephritis chronic Diseases 0.000 description 1
- 206010051920 Glomerulonephropathy Diseases 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 102100033808 Glycoprotein hormone alpha-2 Human genes 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 1
- 208000009329 Graft vs Host Disease Diseases 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- 101000616698 Homo sapiens CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase Proteins 0.000 description 1
- 101001051973 Homo sapiens Fibroblast growth factor 23 Proteins 0.000 description 1
- 101001069261 Homo sapiens Glycoprotein hormone alpha-2 Proteins 0.000 description 1
- 101001018100 Homo sapiens Lysozyme C Proteins 0.000 description 1
- 101000990902 Homo sapiens Matrix metalloproteinase-9 Proteins 0.000 description 1
- 229920002153 Hydroxypropyl cellulose Polymers 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 206010020772 Hypertension Diseases 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- 201000003838 Idiopathic interstitial pneumonia Diseases 0.000 description 1
- 208000010159 IgA glomerulonephritis Diseases 0.000 description 1
- 206010021263 IgA nephropathy Diseases 0.000 description 1
- 235000003332 Ilex aquifolium Nutrition 0.000 description 1
- 241000209027 Ilex aquifolium Species 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- 208000029523 Interstitial Lung disease Diseases 0.000 description 1
- 208000002260 Keloid Diseases 0.000 description 1
- 206010023330 Keloid scar Diseases 0.000 description 1
- 206010023421 Kidney fibrosis Diseases 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- 239000012741 Laemmli sample buffer Substances 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102000019298 Lipocalin Human genes 0.000 description 1
- 108050006654 Lipocalin Proteins 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 102100033468 Lysozyme C Human genes 0.000 description 1
- 101710125418 Major capsid protein Proteins 0.000 description 1
- 102100030412 Matrix metalloproteinase-9 Human genes 0.000 description 1
- 101710151805 Mitochondrial intermediate peptidase 1 Proteins 0.000 description 1
- 101710151803 Mitochondrial intermediate peptidase 2 Proteins 0.000 description 1
- 208000034578 Multiple myelomas Diseases 0.000 description 1
- 102000007474 Multiprotein Complexes Human genes 0.000 description 1
- 108010085220 Multiprotein Complexes Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000238367 Mya arenaria Species 0.000 description 1
- 101710204212 Neocarzinostatin Proteins 0.000 description 1
- 206010029148 Nephrolithiasis Diseases 0.000 description 1
- 244000061176 Nicotiana tabacum Species 0.000 description 1
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 102220558706 Nuclear protein 1_T68Q_mutation Human genes 0.000 description 1
- 101710141454 Nucleoprotein Proteins 0.000 description 1
- 206010030194 Oesophageal stenosis Diseases 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 206010053159 Organ failure Diseases 0.000 description 1
- 240000007594 Oryza sativa Species 0.000 description 1
- 235000007164 Oryza sativa Nutrition 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 206010034238 Pelvic adhesions Diseases 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 101710083689 Probable capsid protein Proteins 0.000 description 1
- 102220468699 Protein arginine N-methyltransferase 3_Y87F_mutation Human genes 0.000 description 1
- 238000012181 QIAquick gel extraction kit Methods 0.000 description 1
- IWYDHOAUDWTVEP-UHFFFAOYSA-N R-2-phenyl-2-hydroxyacetic acid Natural products OC(=O)C(O)C1=CC=CC=C1 IWYDHOAUDWTVEP-UHFFFAOYSA-N 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 206010038357 Renal amyloidosis Diseases 0.000 description 1
- 206010038389 Renal cancer Diseases 0.000 description 1
- 208000006265 Renal cell carcinoma Diseases 0.000 description 1
- 208000013616 Respiratory Distress Syndrome Diseases 0.000 description 1
- 206010038848 Retinal detachment Diseases 0.000 description 1
- 108010085149 S100 Calcium-Binding Protein A4 Proteins 0.000 description 1
- 241000235347 Schizosaccharomyces pombe Species 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 1
- 108091005735 TGF-beta receptors Proteins 0.000 description 1
- FEWJPZIEWOKRBE-UHFFFAOYSA-N Tartaric acid Natural products [H+].[H+].[O-]C(=O)C(O)C(O)C([O-])=O FEWJPZIEWOKRBE-UHFFFAOYSA-N 0.000 description 1
- 102000016715 Transforming Growth Factor beta Receptors Human genes 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 206010048302 Tubulointerstitial nephritis Diseases 0.000 description 1
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 1
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 1
- 208000024248 Vascular System injury Diseases 0.000 description 1
- 208000012339 Vascular injury Diseases 0.000 description 1
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 1
- 239000003070 absorption delaying agent Substances 0.000 description 1
- PMZXXNPJQYDFJX-UHFFFAOYSA-N acetonitrile;2,2,2-trifluoroacetic acid Chemical compound CC#N.OC(=O)C(F)(F)F PMZXXNPJQYDFJX-UHFFFAOYSA-N 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 201000000028 adult respiratory distress syndrome Diseases 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000006838 adverse reaction Effects 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 238000012867 alanine scanning Methods 0.000 description 1
- 208000010002 alcoholic liver cirrhosis Diseases 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 238000005804 alkylation reaction Methods 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 230000006229 amino acid addition Effects 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 229960003896 aminopterin Drugs 0.000 description 1
- 229940035676 analgesics Drugs 0.000 description 1
- 229940044094 angiotensin-converting-enzyme inhibitor Drugs 0.000 description 1
- 239000000730 antalgic agent Substances 0.000 description 1
- 230000003302 anti-idiotype Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 239000001961 anticonvulsive agent Substances 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 229940115115 aranesp Drugs 0.000 description 1
- 206010003246 arthritis Diseases 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 238000011190 asparagine deamidation Methods 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 239000002585 base Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 239000002876 beta blocker Substances 0.000 description 1
- 229940097320 beta blocking agent Drugs 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 239000003124 biologic agent Substances 0.000 description 1
- 239000000090 biomarker Substances 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 229940040609 bleomycin injection Drugs 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 102220346089 c.113G>A Human genes 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 229940087373 calcium oxide Drugs 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000009787 cardiac fibrosis Effects 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 239000002771 cell marker Substances 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 229940096384 chicken egg white lysozyme Drugs 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 239000012501 chromatography medium Substances 0.000 description 1
- 230000001684 chronic effect Effects 0.000 description 1
- 229960001265 ciclosporin Drugs 0.000 description 1
- 238000013377 clone selection method Methods 0.000 description 1
- 238000012411 cloning technique Methods 0.000 description 1
- 239000000084 colloidal system Substances 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000013270 controlled release Methods 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 238000012937 correction Methods 0.000 description 1
- 230000001054 cortical effect Effects 0.000 description 1
- 238000002316 cosmetic surgery Methods 0.000 description 1
- 229930182912 cyclosporin Natural products 0.000 description 1
- 208000031513 cyst Diseases 0.000 description 1
- 150000001945 cysteines Chemical class 0.000 description 1
- 210000000805 cytoplasm Anatomy 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- UGMCXQCYOVCMTB-UHFFFAOYSA-K dihydroxy(stearato)aluminium Chemical compound CCCCCCCCCCCCCCCCCC(=O)O[Al](O)O UGMCXQCYOVCMTB-UHFFFAOYSA-K 0.000 description 1
- 230000005750 disease progression Effects 0.000 description 1
- 208000037765 diseases and disorders Diseases 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 230000002500 effect on skin Effects 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 210000001671 embryonic stem cell Anatomy 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- YQGOJNYOYNNSMM-UHFFFAOYSA-N eosin Chemical compound [Na+].OC(=O)C1=CC=CC=C1C1=C2C=C(Br)C(=O)C(Br)=C2OC2=C(Br)C(O)=C(Br)C=C21 YQGOJNYOYNNSMM-UHFFFAOYSA-N 0.000 description 1
- 229940089118 epogen Drugs 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- BEFDCLMNVWHSGT-UHFFFAOYSA-N ethenylcyclopentane Chemical compound C=CC1CCCC1 BEFDCLMNVWHSGT-UHFFFAOYSA-N 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 210000001508 eye Anatomy 0.000 description 1
- 201000007891 familial visceral amyloidosis Diseases 0.000 description 1
- 229960004887 ferric hydroxide Drugs 0.000 description 1
- 206010016629 fibroma Diseases 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 239000012458 free base Substances 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000007903 gelatin capsule Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000001434 glomerular Effects 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 208000024908 graft versus host disease Diseases 0.000 description 1
- 230000035876 healing Effects 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 239000004009 herbicide Substances 0.000 description 1
- 208000003215 hereditary nephritis Diseases 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000036732 histological change Effects 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 1
- 239000001863 hydroxypropyl cellulose Substances 0.000 description 1
- 235000010977 hydroxypropyl cellulose Nutrition 0.000 description 1
- 230000001969 hypertrophic effect Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 229960003444 immunosuppressant agent Drugs 0.000 description 1
- 239000003018 immunosuppressive agent Substances 0.000 description 1
- 231100000268 induced nephrotoxicity Toxicity 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 239000003701 inert diluent Substances 0.000 description 1
- 208000000509 infertility Diseases 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 231100000535 infertility Toxicity 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000003978 infusion fluid Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 239000002054 inoculum Substances 0.000 description 1
- 150000007529 inorganic bases Chemical class 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 102000006495 integrins Human genes 0.000 description 1
- 108010044426 integrins Proteins 0.000 description 1
- 201000006334 interstitial nephritis Diseases 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- IEECXTSVVFWGSE-UHFFFAOYSA-M iron(3+);oxygen(2-);hydroxide Chemical compound [OH-].[O-2].[Fe+3] IEECXTSVVFWGSE-UHFFFAOYSA-M 0.000 description 1
- 238000006317 isomerization reaction Methods 0.000 description 1
- JJWLVOIRVHMVIS-UHFFFAOYSA-N isopropylamine Chemical compound CC(C)N JJWLVOIRVHMVIS-UHFFFAOYSA-N 0.000 description 1
- 210000001117 keloid Anatomy 0.000 description 1
- 201000010982 kidney cancer Diseases 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 201000010260 leiomyoma Diseases 0.000 description 1
- 210000003644 lens cell Anatomy 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000012417 linear regression Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 231100000516 lung damage Toxicity 0.000 description 1
- 206010025135 lupus erythematosus Diseases 0.000 description 1
- 210000003563 lymphoid tissue Anatomy 0.000 description 1
- 101150035025 lysC gene Proteins 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 230000036244 malformation Effects 0.000 description 1
- 229960002510 mandelic acid Drugs 0.000 description 1
- 230000000873 masking effect Effects 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 230000034217 membrane fusion Effects 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 230000001394 metastastic effect Effects 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 150000007522 mineralic acids Chemical class 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000004660 morphological change Effects 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 201000006938 muscular dystrophy Diseases 0.000 description 1
- 206010028537 myelofibrosis Diseases 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 239000002077 nanosphere Substances 0.000 description 1
- QZGIWPZCWHMVQL-UIYAJPBUSA-N neocarzinostatin chromophore Chemical compound O1[C@H](C)[C@H](O)[C@H](O)[C@@H](NC)[C@H]1O[C@@H]1C/2=C/C#C[C@H]3O[C@@]3([C@@H]3OC(=O)OC3)C#CC\2=C[C@H]1OC(=O)C1=C(O)C=CC2=C(C)C=C(OC)C=C12 QZGIWPZCWHMVQL-UIYAJPBUSA-N 0.000 description 1
- 201000002648 nephronophthisis Diseases 0.000 description 1
- 210000005036 nerve Anatomy 0.000 description 1
- 108010087904 neutravidin Proteins 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 238000002515 oligonucleotide synthesis Methods 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 150000007530 organic bases Chemical class 0.000 description 1
- 235000006408 oxalic acid Nutrition 0.000 description 1
- 239000005022 packaging material Substances 0.000 description 1
- 208000030346 palmar fibromatosis Diseases 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 239000000816 peptidomimetic Substances 0.000 description 1
- 210000003200 peritoneal cavity Anatomy 0.000 description 1
- 239000000575 pesticide Substances 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 229960003742 phenol Drugs 0.000 description 1
- 238000002205 phenol-chloroform extraction Methods 0.000 description 1
- 239000002953 phosphate buffered saline Substances 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 230000007505 plaque formation Effects 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920000191 poly(N-vinyl pyrrolidone) Polymers 0.000 description 1
- 229920001583 poly(oxyethylated polyols) Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 208000030761 polycystic kidney disease Diseases 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 210000004896 polypeptide structure Anatomy 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 238000011176 pooling Methods 0.000 description 1
- 238000010837 poor prognosis Methods 0.000 description 1
- 235000020004 porter Nutrition 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 208000013846 primary aldosteronism Diseases 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- MFDFERRIHVXMIY-UHFFFAOYSA-N procaine Chemical compound CCN(CC)CCOC(=O)C1=CC=C(N)C=C1 MFDFERRIHVXMIY-UHFFFAOYSA-N 0.000 description 1
- 229960004919 procaine Drugs 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 230000012846 protein folding Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 238000012207 quantitative assay Methods 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000008085 renal dysfunction Effects 0.000 description 1
- 206010038433 renal dysplasia Diseases 0.000 description 1
- 230000008663 renal system process Effects 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 208000037803 restenosis Diseases 0.000 description 1
- 230000004264 retinal detachment Effects 0.000 description 1
- 235000009566 rice Nutrition 0.000 description 1
- 102200156936 rs28934878 Human genes 0.000 description 1
- 102200082919 rs35857380 Human genes 0.000 description 1
- 102200087445 rs566961335 Human genes 0.000 description 1
- 102220047535 rs587783040 Human genes 0.000 description 1
- 102220244406 rs761122171 Human genes 0.000 description 1
- 102220323800 rs774193307 Human genes 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 230000037390 scarring Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 230000001568 sexual effect Effects 0.000 description 1
- 238000001542 size-exclusion chromatography Methods 0.000 description 1
- 210000003491 skin Anatomy 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000004334 sorbic acid Substances 0.000 description 1
- 235000010199 sorbic acid Nutrition 0.000 description 1
- 229940075582 sorbic acid Drugs 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 238000009987 spinning Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012385 systemic delivery Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 235000002906 tartaric acid Nutrition 0.000 description 1
- 239000011975 tartaric acid Substances 0.000 description 1
- 210000002435 tendon Anatomy 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 150000003573 thiols Chemical class 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 238000012384 transportation and delivery Methods 0.000 description 1
- YFDSDPIBEUFTMI-UHFFFAOYSA-N tribromoethanol Chemical compound OCC(Br)(Br)Br YFDSDPIBEUFTMI-UHFFFAOYSA-N 0.000 description 1
- 229950004616 tribromoethanol Drugs 0.000 description 1
- 239000012137 tryptone Substances 0.000 description 1
- 210000005239 tubule Anatomy 0.000 description 1
- 229910052721 tungsten Inorganic materials 0.000 description 1
- 239000011882 ultra-fine particle Substances 0.000 description 1
- 231100000402 unacceptable toxicity Toxicity 0.000 description 1
- 230000002485 urinary effect Effects 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 229910052725 zinc Inorganic materials 0.000 description 1
- 239000011701 zinc Substances 0.000 description 1
- 229950009268 zinostatin Drugs 0.000 description 1
- AFVLVVWMAFSXCK-UHFFFAOYSA-N α-cyano-4-hydroxycinnamic acid Chemical compound OC(=O)C(C#N)=CC1=CC=C(O)C=C1 AFVLVVWMAFSXCK-UHFFFAOYSA-N 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P13/00—Drugs for disorders of the urinary system
- A61P13/12—Drugs for disorders of the urinary system of the kidneys
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Veterinary Medicine (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Urology & Nephrology (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Pulmonology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US403707P | 2007-11-21 | 2007-11-21 | |
| US61/004,037 | 2007-11-21 | ||
| PCT/US2008/012987 WO2009070243A2 (en) | 2007-11-21 | 2008-11-21 | Wise binding agents and epitopes |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014061293A Division JP2014167002A (ja) | 2007-11-21 | 2014-03-25 | Ｗｉｓｅ結合抗体及びエピトープ |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2011504501A JP2011504501A (ja) | 2011-02-10 |
| JP2011504501A5 JP2011504501A5 (cg-RX-API-DMAC7.html) | 2012-01-12 |
| JP5583591B2 true JP5583591B2 (ja) | 2014-09-03 |
Family
ID=40524859
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2010534969A Expired - Fee Related JP5583591B2 (ja) | 2007-11-21 | 2008-11-21 | Ｗｉｓｅ結合抗体及びエピトープ |
| JP2014061293A Withdrawn JP2014167002A (ja) | 2007-11-21 | 2014-03-25 | Ｗｉｓｅ結合抗体及びエピトープ |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2014061293A Withdrawn JP2014167002A (ja) | 2007-11-21 | 2014-03-25 | Ｗｉｓｅ結合抗体及びエピトープ |
Country Status (17)
| Country | Link |
|---|---|
| US (2) | US8043620B2 (cg-RX-API-DMAC7.html) |
| EP (1) | EP2220118A2 (cg-RX-API-DMAC7.html) |
| JP (2) | JP5583591B2 (cg-RX-API-DMAC7.html) |
| KR (1) | KR20100099193A (cg-RX-API-DMAC7.html) |
| CN (1) | CN101925611A (cg-RX-API-DMAC7.html) |
| AU (1) | AU2008330125B2 (cg-RX-API-DMAC7.html) |
| BR (1) | BRPI0820387A2 (cg-RX-API-DMAC7.html) |
| CA (1) | CA2705879A1 (cg-RX-API-DMAC7.html) |
| CO (1) | CO6311002A2 (cg-RX-API-DMAC7.html) |
| CR (1) | CR11523A (cg-RX-API-DMAC7.html) |
| EA (1) | EA201000844A1 (cg-RX-API-DMAC7.html) |
| IL (1) | IL205569A0 (cg-RX-API-DMAC7.html) |
| MA (1) | MA31918B1 (cg-RX-API-DMAC7.html) |
| MX (1) | MX2010005656A (cg-RX-API-DMAC7.html) |
| TN (1) | TN2010000213A1 (cg-RX-API-DMAC7.html) |
| WO (1) | WO2009070243A2 (cg-RX-API-DMAC7.html) |
| ZA (1) | ZA201003578B (cg-RX-API-DMAC7.html) |
Families Citing this family (45)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2005266875B2 (en) | 2004-07-23 | 2012-07-26 | Acceleron Pharma Inc. | ActRII receptor polypeptides, methods and compositions |
| CN105001320A (zh) | 2005-11-23 | 2015-10-28 | 阿塞勒隆制药公司 | Activin-ActRIIa拮抗剂及其促进骨骼生长的应用 |
| US8128933B2 (en) | 2005-11-23 | 2012-03-06 | Acceleron Pharma, Inc. | Method of promoting bone growth by an anti-activin B antibody |
| US8895016B2 (en) | 2006-12-18 | 2014-11-25 | Acceleron Pharma, Inc. | Antagonists of activin-actriia and uses for increasing red blood cell levels |
| CN101835485B (zh) | 2007-02-01 | 2016-10-26 | 阿塞勒隆制药公司 | 活化素-actriia拮抗剂及在治疗或预防乳腺癌中的用途 |
| TW201940502A (zh) | 2007-02-02 | 2019-10-16 | 美商艾瑟勒朗法瑪公司 | 衍生自ＡｃｔＲＩＩＢ的變體與其用途 |
| JP5574711B2 (ja) | 2007-02-09 | 2014-08-20 | アクセルロン ファーマ， インコーポレイテッド | 癌患者における骨成長を促進するためのアクチビン−ａｃｔｒｉｉａアンタゴニストおよびその使用 |
| EP3243524A1 (en) | 2007-09-18 | 2017-11-15 | Acceleron Pharma Inc. | Activin-actriia antagonists and uses for decreasing or inhibiting fsh secretion |
| US8216997B2 (en) | 2008-08-14 | 2012-07-10 | Acceleron Pharma, Inc. | Methods for increasing red blood cell levels and treating anemia using a combination of GDF traps and erythropoietin receptor activators |
| WO2010019261A1 (en) | 2008-08-14 | 2010-02-18 | Acceleron Pharma Inc. | Use of gdf traps to increase red blood cell levels |
| WO2011063127A1 (en) | 2009-11-18 | 2011-05-26 | University Of Medicine And Dentistry Of New Jersey | Targeting tumor cells with chemotherapeutic agents conjugated to matriptase antibodies |
| EP2387412A4 (en) | 2009-01-13 | 2013-04-03 | Acceleron Pharma Inc | PROCESS FOR INCREASING THE ADIPONECTIN MIRROR |
| US8178488B2 (en) | 2009-06-08 | 2012-05-15 | Acceleron Pharma, Inc. | Methods for increasing thermogenic adipocytes |
| BRPI1010704B1 (pt) | 2009-06-12 | 2021-12-14 | Acceleron Pharma Inc | Polipeptídeo recombinante, proteína de fusão recombinante, preparação farmacêutica e uso da mesma |
| WO2011025964A2 (en) | 2009-08-29 | 2011-03-03 | Abbott Laboratories | Therapeutic dll4 binding proteins |
| JP6267425B2 (ja) | 2009-11-17 | 2018-01-24 | アクセルロン ファーマ， インコーポレイテッド | 筋ジストロフィー治療のためのユートロフィン誘導に関するａｃｔｒｉｉｂタンパク質およびその改変体およびその使用 |
| US9849192B2 (en) | 2009-11-18 | 2017-12-26 | Rutgers, The State University Of New Jersey | Targeting tumor cells with chemotherapeutic agents conjugated to matriptase antibodies |
| EP2507381A4 (en) * | 2009-12-04 | 2016-07-20 | Hoffmann La Roche | MULTISPECIFIC ANTIBODIES, ANTIBODY ANALOGS, COMPOSITIONS AND METHODS |
| WO2011075636A2 (en) | 2009-12-18 | 2011-06-23 | Amgen Inc. | Wise binding agents and epitopes |
| BR112012021941A2 (pt) * | 2010-03-02 | 2022-02-01 | Abbvie Inc | Proteínas terapêuticas de ligação a dll4 |
| AU2011326586A1 (en) | 2010-11-08 | 2013-05-30 | Acceleron Pharma, Inc. | ActRIIA binding agents and uses thereof |
| AU2012327223A1 (en) | 2011-11-30 | 2013-06-20 | Wellstat Diagnostics, Llc. | Assays, antibodies, immunogens and compositions related to 5-FU |
| WO2013103800A1 (en) * | 2012-01-06 | 2013-07-11 | Bioalliance C.V. | Anti-transferrin receptor antibodies and methods using same |
| FR2987293B1 (fr) * | 2012-02-27 | 2014-03-07 | Michelin & Cie | Procede et appareil pour realiser des objets tridimensionnels a proprietes ameliorees |
| EP2904015A4 (en) | 2012-10-02 | 2016-10-05 | Univ Rutgers | TARGETED RELEASE OF ANTIBODIES TO ACTIVATED MATRIPTASE-CONJUGATED TOXINS |
| NZ707477A (en) | 2012-11-02 | 2019-09-27 | Celgene Corp | Activin-actrii antagonists and uses for treating bone and other disorders |
| BR112015010360A8 (pt) | 2012-11-08 | 2018-01-16 | Eleven Biotherapeutics Inc | antagonistas de il-6 e utilização dos mesmos. |
| US20140171356A1 (en) * | 2012-12-12 | 2014-06-19 | The Board Of Trustees Of The Leland Stanford Junior University | Chemically immobilized wnt protein and methods of use |
| AU2014315081A1 (en) | 2013-09-05 | 2016-03-24 | Duke University | Nav1.7 antibodies and methods of using the same |
| US10035847B2 (en) | 2013-10-02 | 2018-07-31 | The Rockefeller University | Amyloid protofibril antibodies and methods of use thereof |
| AP2017009674A0 (en) | 2014-06-13 | 2017-01-31 | Acceleron Pharma Inc | Methods and compositions for treating ulcers |
| MA41052A (fr) | 2014-10-09 | 2017-08-15 | Celgene Corp | Traitement d'une maladie cardiovasculaire à l'aide de pièges de ligands d'actrii |
| UA122673C2 (uk) | 2014-11-07 | 2020-12-28 | Елевен Байотерапьютікс, Інк. | Антитіло, що специфічно зв'язується з людським il-6 |
| JP2018501307A (ja) | 2014-12-03 | 2018-01-18 | セルジーン コーポレイション | アクチビン−ＡｃｔＲＩＩアンタゴニスト及び貧血を治療するための使用 |
| JP2019510078A (ja) | 2016-02-23 | 2019-04-11 | セセン バイオ， インコーポレイテッド | Ｉｌ−６アンタゴニスト製剤およびその使用 |
| CA3017958C (en) | 2016-03-18 | 2024-03-12 | Rutgers, The State University Of New Jersey | Targeting tumor cells with chemotherapeutic agents conjugated to anti-matriptase antibodies by in vivo cleavable linking moieties |
| EP3448875A4 (en) * | 2016-04-29 | 2020-04-08 | Voyager Therapeutics, Inc. | Compositions for the treatment of disease |
| WO2018129248A1 (en) * | 2017-01-06 | 2018-07-12 | The Regents Of The University Of California | Therapeutic anti-ige antibodies and methods and compositions thereof |
| US11021540B2 (en) * | 2017-09-07 | 2021-06-01 | Augusta University Research Institute, Inc. | Antibodies to programmed cell death protein 1 |
| KR20220034176A (ko) * | 2019-07-12 | 2022-03-17 | 고쿠리츠 다이가쿠 호진 교토 다이가쿠 | 치아의 재생 치료를 위한 usag-1을 표적 분자로 한 중화 항체 |
| CN112180099B (zh) * | 2020-09-15 | 2022-07-29 | 江南大学附属医院 | 子宫内膜异位症血清标志物的应用 |
| IL314524A (en) | 2022-01-28 | 2024-09-01 | Georgiamune Inc | Antibodies to programmed cell death protein 1 that are agonists for PD-1 |
| CN115322258B (zh) * | 2022-05-31 | 2024-08-13 | 武汉真福医药股份有限公司 | 一种单克隆抗体qkma-1g41及其应用 |
| CN115304677B (zh) * | 2022-06-19 | 2024-08-16 | 湖北真福医药有限公司 | 一种抗枯草芽孢杆菌纤溶酶的单克隆抗体qkma-9a10及应用 |
| CN116712533B (zh) * | 2023-07-03 | 2024-02-02 | 广东暨安特博生物科技有限公司 | 一种sostdc1蛋白在制备治疗皮肤病产品中的应用 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CA2220912A1 (en) * | 1995-06-05 | 1996-12-12 | Gregg A. Hastings | Human ccn-like growth factor |
| WO2002008284A2 (en) | 2000-07-20 | 2002-01-31 | Genentech, Inc. | Compositions and methods for the diagnosis and treatment of disorders involving angiogenesis |
| AU2003276430A1 (en) * | 2002-06-14 | 2003-12-31 | Stowers Institute For Medical Research | Wise/sost nucleic acid sequences and amino acid sequences |
| MXPA06010887A (es) * | 2004-03-23 | 2007-03-08 | Amgen Inc | Anticuerpos monoclonales especificos para ox4ol (cd 134l) humano. |
| PL3345607T3 (pl) * | 2006-12-29 | 2023-01-09 | Ossifi-Mab Llc | Sposoby modyfikowania wzrostu kości poprzez podanie antagonisty lub agonisty sost lub wise |
| WO2008156712A1 (en) * | 2007-06-18 | 2008-12-24 | N. V. Organon | Antibodies to human programmed death receptor pd-1 |
| JO3382B1 (ar) * | 2008-12-23 | 2019-03-13 | Amgen Inc | أجسام مضادة ترتبط مع مستقبل cgrp بشري |
| WO2010131185A1 (en) * | 2009-05-12 | 2010-11-18 | Pfizer Inc. | Blocking anti-dkk-1 antibodies and their uses |
-
2008
- 2008-11-21 EA EA201000844A patent/EA201000844A1/ru unknown
- 2008-11-21 KR KR1020107013609A patent/KR20100099193A/ko not_active Withdrawn
- 2008-11-21 EP EP08855691A patent/EP2220118A2/en not_active Withdrawn
- 2008-11-21 CN CN2008801252375A patent/CN101925611A/zh active Pending
- 2008-11-21 WO PCT/US2008/012987 patent/WO2009070243A2/en not_active Ceased
- 2008-11-21 CA CA2705879A patent/CA2705879A1/en not_active Abandoned
- 2008-11-21 AU AU2008330125A patent/AU2008330125B2/en not_active Ceased
- 2008-11-21 JP JP2010534969A patent/JP5583591B2/ja not_active Expired - Fee Related
- 2008-11-21 MX MX2010005656A patent/MX2010005656A/es active IP Right Grant
- 2008-11-21 US US12/275,850 patent/US8043620B2/en not_active Expired - Fee Related
- 2008-11-21 BR BRPI0820387-3A patent/BRPI0820387A2/pt not_active IP Right Cessation
-
2010
- 2010-05-05 IL IL205569A patent/IL205569A0/en unknown
- 2010-05-14 TN TN2010000213A patent/TN2010000213A1/fr unknown
- 2010-05-20 ZA ZA2010/03578A patent/ZA201003578B/en unknown
- 2010-06-15 MA MA32918A patent/MA31918B1/fr unknown
- 2010-06-21 CR CR11523A patent/CR11523A/es not_active Application Discontinuation
- 2010-06-23 CO CO10075718A patent/CO6311002A2/es not_active Application Discontinuation
-
2011
- 2011-09-15 US US13/233,983 patent/US8309092B2/en active Active
-
2014
- 2014-03-25 JP JP2014061293A patent/JP2014167002A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| WO2009070243A3 (en) | 2009-10-29 |
| ZA201003578B (en) | 2011-04-28 |
| CA2705879A1 (en) | 2009-06-04 |
| IL205569A0 (en) | 2010-12-30 |
| TN2010000213A1 (en) | 2011-11-11 |
| WO2009070243A2 (en) | 2009-06-04 |
| JP2011504501A (ja) | 2011-02-10 |
| BRPI0820387A2 (pt) | 2015-05-26 |
| MA31918B1 (fr) | 2010-12-01 |
| JP2014167002A (ja) | 2014-09-11 |
| CN101925611A (zh) | 2010-12-22 |
| EA201000844A1 (ru) | 2011-10-31 |
| MX2010005656A (es) | 2010-11-12 |
| US20090130114A1 (en) | 2009-05-21 |
| US20120003237A1 (en) | 2012-01-05 |
| AU2008330125B2 (en) | 2012-11-22 |
| US8043620B2 (en) | 2011-10-25 |
| US8309092B2 (en) | 2012-11-13 |
| KR20100099193A (ko) | 2010-09-10 |
| CO6311002A2 (es) | 2011-08-22 |
| EP2220118A2 (en) | 2010-08-25 |
| AU2008330125A1 (en) | 2009-06-04 |
| CR11523A (es) | 2010-12-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP5583591B2 (ja) | Ｗｉｓｅ結合抗体及びエピトープ | |
| US11542325B2 (en) | Anti-activin A antibodies and uses thereof | |
| US20120288507A1 (en) | Wise binding agents and epitopes | |
| JP2023065375A (ja) | 胸腺間質性リンパ球性新生因子に結合することができる抗原結合タンパク質 | |
| TWI494320B (zh) | 結合劑 | |
| EP2423226A2 (en) | Antibody-based diagnostics and therapeutics | |
| EP2460828A2 (en) | Antibodies and diagnostics | |
| JP2010502740A5 (cg-RX-API-DMAC7.html) |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20111118 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20111118 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20130730 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20131030 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20131126 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20140325 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20140326 |
|
| A911 | Transfer to examiner for re-examination before appeal (zenchi) |
Free format text: JAPANESE INTERMEDIATE CODE: A911 Effective date: 20140520 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20140701 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20140716 |
|
| R150 | Certificate of patent or registration of utility model |
Ref document number: 5583591 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| LAPS | Cancellation because of no payment of annual fees |