MX2011001363A - Anticuerpos selectivos de anti-hepcidina-25 y usos de los mismos. - Google Patents
Anticuerpos selectivos de anti-hepcidina-25 y usos de los mismos.Info
- Publication number
- MX2011001363A MX2011001363A MX2011001363A MX2011001363A MX2011001363A MX 2011001363 A MX2011001363 A MX 2011001363A MX 2011001363 A MX2011001363 A MX 2011001363A MX 2011001363 A MX2011001363 A MX 2011001363A MX 2011001363 A MX2011001363 A MX 2011001363A
- Authority
- MX
- Mexico
- Prior art keywords
- hepcidin
- antibody
- seq
- nos
- amino acid
- Prior art date
Links
- 108700022871 human hepcidin 25 Proteins 0.000 claims abstract description 63
- 102000009052 human hepcidin 25 Human genes 0.000 claims abstract description 63
- 210000002966 serum Anatomy 0.000 claims abstract description 52
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 claims abstract description 51
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 48
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 42
- 229920001184 polypeptide Polymers 0.000 claims abstract description 39
- 208000007502 anemia Diseases 0.000 claims abstract description 23
- 229910052742 iron Inorganic materials 0.000 claims abstract description 23
- 238000011282 treatment Methods 0.000 claims abstract description 22
- 102000001554 Hemoglobins Human genes 0.000 claims abstract description 16
- 108010054147 Hemoglobins Proteins 0.000 claims abstract description 16
- 238000005534 hematocrit Methods 0.000 claims abstract description 16
- 210000001995 reticulocyte Anatomy 0.000 claims abstract description 16
- 210000003743 erythrocyte Anatomy 0.000 claims abstract description 9
- XJOTXKZIRSHZQV-RXHOOSIZSA-N (3S)-3-amino-4-[[(2S,3R)-1-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S,3S)-1-[[(1R,6R,12R,17R,20S,23S,26R,31R,34R,39R,42S,45S,48S,51S,59S)-51-(4-aminobutyl)-31-[[(2S)-6-amino-1-[[(1S,2R)-1-carboxy-2-hydroxypropyl]amino]-1-oxohexan-2-yl]carbamoyl]-20-benzyl-23-[(2S)-butan-2-yl]-45-(3-carbamimidamidopropyl)-48-(hydroxymethyl)-42-(1H-imidazol-4-ylmethyl)-59-(2-methylsulfanylethyl)-7,10,19,22,25,33,40,43,46,49,52,54,57,60,63,64-hexadecaoxo-3,4,14,15,28,29,36,37-octathia-8,11,18,21,24,32,41,44,47,50,53,55,58,61,62,65-hexadecazatetracyclo[32.19.8.26,17.212,39]pentahexacontan-26-yl]amino]-3-methyl-1-oxopentan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxo-3-phenylpropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-3-hydroxy-1-oxobutan-2-yl]amino]-4-oxobutanoic acid Chemical compound CC[C@H](C)[C@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1cnc[nH]1)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(O)=O)[C@@H](C)O)C(=O)N[C@H]1CSSC[C@H](NC(=O)[C@@H]2CSSC[C@@H]3NC(=O)[C@@H]4CSSC[C@H](NC(=O)[C@H](Cc5ccccc5)NC(=O)[C@@H](NC1=O)[C@@H](C)CC)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](Cc1cnc[nH]1)NC3=O)C(=O)NCC(=O)N[C@@H](CCSC)C(=O)N2)C(=O)NCC(=O)N4)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O XJOTXKZIRSHZQV-RXHOOSIZSA-N 0.000 claims description 220
- 101800003310 Hepcidin-25 Proteins 0.000 claims description 174
- 102400001151 Hepcidin-25 Human genes 0.000 claims description 173
- 108060003558 hepcidin Proteins 0.000 claims description 84
- 102000018511 hepcidin Human genes 0.000 claims description 83
- 150000001413 amino acids Chemical group 0.000 claims description 78
- 238000000034 method Methods 0.000 claims description 78
- 210000004027 cell Anatomy 0.000 claims description 50
- 238000003018 immunoassay Methods 0.000 claims description 42
- 108090000623 proteins and genes Proteins 0.000 claims description 26
- 102000004169 proteins and genes Human genes 0.000 claims description 24
- 238000002965 ELISA Methods 0.000 claims description 23
- 239000012634 fragment Substances 0.000 claims description 18
- 239000013060 biological fluid Substances 0.000 claims description 16
- 210000001519 tissue Anatomy 0.000 claims description 16
- 102000022413 human hepcidin (6-25) Human genes 0.000 claims description 15
- 108091004639 human hepcidin (6-25) Proteins 0.000 claims description 15
- 239000008194 pharmaceutical composition Substances 0.000 claims description 15
- 238000001514 detection method Methods 0.000 claims description 13
- 239000007787 solid Substances 0.000 claims description 12
- 238000002560 therapeutic procedure Methods 0.000 claims description 7
- 239000003814 drug Substances 0.000 claims description 6
- 238000004519 manufacturing process Methods 0.000 claims description 6
- 239000003085 diluting agent Substances 0.000 claims description 5
- 239000003937 drug carrier Substances 0.000 claims description 5
- 238000003127 radioimmunoassay Methods 0.000 claims description 4
- 238000012286 ELISA Assay Methods 0.000 claims description 3
- 102000004190 Enzymes Human genes 0.000 claims description 3
- 108090000790 Enzymes Proteins 0.000 claims description 3
- 210000004369 blood Anatomy 0.000 claims description 3
- 239000008280 blood Substances 0.000 claims description 3
- 238000006243 chemical reaction Methods 0.000 claims description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 2
- 239000011248 coating agent Substances 0.000 claims description 2
- 238000000576 coating method Methods 0.000 claims description 2
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 2
- 238000001556 precipitation Methods 0.000 claims description 2
- 210000001175 cerebrospinal fluid Anatomy 0.000 claims 2
- 239000012530 fluid Substances 0.000 claims 2
- 206010003445 Ascites Diseases 0.000 claims 1
- 210000004381 amniotic fluid Anatomy 0.000 claims 1
- 210000002726 cyst fluid Anatomy 0.000 claims 1
- 210000004251 human milk Anatomy 0.000 claims 1
- 235000020256 human milk Nutrition 0.000 claims 1
- 210000002381 plasma Anatomy 0.000 claims 1
- 210000003296 saliva Anatomy 0.000 claims 1
- 210000004243 sweat Anatomy 0.000 claims 1
- 210000002700 urine Anatomy 0.000 claims 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 abstract description 46
- 238000004820 blood count Methods 0.000 abstract description 7
- 238000003118 sandwich ELISA Methods 0.000 abstract 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 60
- 229940066919 hepcidin Drugs 0.000 description 58
- 235000001014 amino acid Nutrition 0.000 description 34
- 201000010099 disease Diseases 0.000 description 30
- 239000000523 sample Substances 0.000 description 30
- 241000699666 Mus <mouse, genus> Species 0.000 description 28
- 230000027455 binding Effects 0.000 description 26
- 238000003556 assay Methods 0.000 description 23
- 235000018102 proteins Nutrition 0.000 description 23
- 238000009830 intercalation Methods 0.000 description 22
- 230000002687 intercalation Effects 0.000 description 22
- 208000035475 disorder Diseases 0.000 description 15
- 101001021253 Homo sapiens Hepcidin Proteins 0.000 description 14
- 241000894007 species Species 0.000 description 14
- 238000012360 testing method Methods 0.000 description 13
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- 230000001225 therapeutic effect Effects 0.000 description 12
- 239000013598 vector Substances 0.000 description 12
- 239000012472 biological sample Substances 0.000 description 11
- 150000007523 nucleic acids Chemical class 0.000 description 11
- 241000282693 Cercopithecidae Species 0.000 description 10
- 241000124008 Mammalia Species 0.000 description 10
- 206010028980 Neoplasm Diseases 0.000 description 10
- 239000006180 TBST buffer Substances 0.000 description 10
- 239000000427 antigen Substances 0.000 description 10
- 239000000872 buffer Substances 0.000 description 10
- 201000011510 cancer Diseases 0.000 description 10
- 239000003153 chemical reaction reagent Substances 0.000 description 10
- 238000005259 measurement Methods 0.000 description 10
- 101800003308 Hepcidin-20 Proteins 0.000 description 9
- 102400001150 Hepcidin-20 Human genes 0.000 description 9
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 9
- 239000007983 Tris buffer Substances 0.000 description 9
- 102000036639 antigens Human genes 0.000 description 9
- 108091007433 antigens Proteins 0.000 description 9
- 108020001507 fusion proteins Proteins 0.000 description 9
- 102000037865 fusion proteins Human genes 0.000 description 9
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 8
- 230000000694 effects Effects 0.000 description 8
- 239000011159 matrix material Substances 0.000 description 8
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 8
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 7
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 7
- 241000283707 Capra Species 0.000 description 7
- 206010061218 Inflammation Diseases 0.000 description 7
- 230000008901 benefit Effects 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 230000004054 inflammatory process Effects 0.000 description 7
- 108020004707 nucleic acids Proteins 0.000 description 7
- 102000039446 nucleic acids Human genes 0.000 description 7
- 239000002243 precursor Substances 0.000 description 7
- 208000017667 Chronic Disease Diseases 0.000 description 6
- 241000282412 Homo Species 0.000 description 6
- 238000005516 engineering process Methods 0.000 description 6
- 210000004602 germ cell Anatomy 0.000 description 6
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- 208000015181 infectious disease Diseases 0.000 description 6
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 6
- 239000011780 sodium chloride Substances 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 5
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 5
- 108060003951 Immunoglobulin Proteins 0.000 description 5
- 229920001213 Polysorbate 20 Polymers 0.000 description 5
- 108091006976 SLC40A1 Proteins 0.000 description 5
- 238000002835 absorbance Methods 0.000 description 5
- 239000005018 casein Substances 0.000 description 5
- 238000010494 dissociation reaction Methods 0.000 description 5
- 230000005593 dissociations Effects 0.000 description 5
- 102000018358 immunoglobulin Human genes 0.000 description 5
- 239000000463 material Substances 0.000 description 5
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 5
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 5
- 230000035945 sensitivity Effects 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 239000000758 substrate Substances 0.000 description 5
- 229910052717 sulfur Inorganic materials 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 241001529936 Murinae Species 0.000 description 4
- 239000012131 assay buffer Substances 0.000 description 4
- 238000011088 calibration curve Methods 0.000 description 4
- 239000004202 carbamide Substances 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 4
- 235000021240 caseins Nutrition 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- -1 hepcidin-20 (e.g. Chemical compound 0.000 description 4
- 238000001819 mass spectrum Methods 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 4
- 108091033319 polynucleotide Proteins 0.000 description 4
- 102000040430 polynucleotide Human genes 0.000 description 4
- 239000002157 polynucleotide Substances 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 239000007995 HEPES buffer Substances 0.000 description 3
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 3
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 3
- 101001021252 Mus musculus Hepcidin Proteins 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 101001021296 Rattus norvegicus Hepcidin Proteins 0.000 description 3
- 150000001412 amines Chemical class 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 230000000903 blocking effect Effects 0.000 description 3
- 230000002596 correlated effect Effects 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 229910052731 fluorine Inorganic materials 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 230000003993 interaction Effects 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 239000006193 liquid solution Substances 0.000 description 3
- 229910052757 nitrogen Inorganic materials 0.000 description 3
- 239000013641 positive control Substances 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 230000002265 prevention Effects 0.000 description 3
- 238000003259 recombinant expression Methods 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 238000010186 staining Methods 0.000 description 3
- 239000004094 surface-active agent Substances 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
- 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 description 2
- 208000030760 Anaemia of chronic disease Diseases 0.000 description 2
- 108090001008 Avidin Proteins 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 2
- 102000008857 Ferritin Human genes 0.000 description 2
- 108050000784 Ferritin Proteins 0.000 description 2
- 238000008416 Ferritin Methods 0.000 description 2
- 101150043052 Hamp gene Proteins 0.000 description 2
- 208000002250 Hematologic Neoplasms Diseases 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 208000026350 Inborn Genetic disease Diseases 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 241000283984 Rodentia Species 0.000 description 2
- KJTLSVCANCCWHF-UHFFFAOYSA-N Ruthenium Chemical compound [Ru] KJTLSVCANCCWHF-UHFFFAOYSA-N 0.000 description 2
- PXIPVTKHYLBLMZ-UHFFFAOYSA-N Sodium azide Chemical compound [Na+].[N-]=[N+]=[N-] PXIPVTKHYLBLMZ-UHFFFAOYSA-N 0.000 description 2
- 208000022400 anemia due to chronic disease Diseases 0.000 description 2
- 230000009286 beneficial effect Effects 0.000 description 2
- 230000000975 bioactive effect Effects 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 239000012501 chromatography medium Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000002380 cytological effect Effects 0.000 description 2
- 238000003745 diagnosis Methods 0.000 description 2
- 238000007865 diluting Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000013604 expression vector Substances 0.000 description 2
- 208000016361 genetic disease Diseases 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 229910052739 hydrogen Inorganic materials 0.000 description 2
- 238000001597 immobilized metal affinity chromatography Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000003119 immunoblot Methods 0.000 description 2
- 238000010166 immunofluorescence Methods 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 230000002055 immunohistochemical effect Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 238000004949 mass spectrometry Methods 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 239000013642 negative control Substances 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- 230000009871 nonspecific binding Effects 0.000 description 2
- 239000005022 packaging material Substances 0.000 description 2
- 230000001575 pathological effect Effects 0.000 description 2
- 238000002823 phage display Methods 0.000 description 2
- 229910052698 phosphorus Inorganic materials 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 229910052707 ruthenium Inorganic materials 0.000 description 2
- 238000004611 spectroscopical analysis Methods 0.000 description 2
- 238000010254 subcutaneous injection Methods 0.000 description 2
- 239000007929 subcutaneous injection Substances 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 208000024891 symptom Diseases 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 229910052720 vanadium Inorganic materials 0.000 description 2
- 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 2
- ANAZDOWEOOFEET-UHFFFAOYSA-N (4-hydroxyphenyl) [4-(3-oxo-1h-2-benzofuran-1-yl)phenyl] hydrogen phosphate Chemical compound C1=CC(O)=CC=C1OP(O)(=O)OC1=CC=C(C2C3=CC=CC=C3C(=O)O2)C=C1 ANAZDOWEOOFEET-UHFFFAOYSA-N 0.000 description 1
- KPYXMALABCDPGN-HYOZMBHHSA-N (4s)-5-[[(2s)-6-amino-1-[[(2s,3s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2r)-1-[[2-[[2-[[(1s)-3-amino-1-carboxy-3-oxopropyl]amino]-2-oxoethyl]amino]-2-oxoethyl]amino]-1-oxo-3-sulfanylpropan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]a Chemical compound NC(=O)C[C@@H](C(O)=O)NC(=O)CNC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN)CC1=CC=C(O)C=C1 KPYXMALABCDPGN-HYOZMBHHSA-N 0.000 description 1
- 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 1
- 229940058020 2-amino-2-methyl-1-propanol Drugs 0.000 description 1
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 1
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 108010032595 Antibody Binding Sites Proteins 0.000 description 1
- 240000003291 Armoracia rusticana Species 0.000 description 1
- 235000011330 Armoracia rusticana Nutrition 0.000 description 1
- 101800001415 Bri23 peptide Proteins 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 101800000655 C-terminal peptide Proteins 0.000 description 1
- 102400000107 C-terminal peptide Human genes 0.000 description 1
- 101100454807 Caenorhabditis elegans lgg-1 gene Proteins 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 102000004961 Furin Human genes 0.000 description 1
- 108090001126 Furin Proteins 0.000 description 1
- 101710160303 Hepcidin-2 Proteins 0.000 description 1
- 101000956778 Homo sapiens LETM1 domain-containing protein 1 Proteins 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- 206010065973 Iron Overload Diseases 0.000 description 1
- 102000018434 Iron-Regulatory Proteins Human genes 0.000 description 1
- 108010066420 Iron-Regulatory Proteins Proteins 0.000 description 1
- 102100038448 LETM1 domain-containing protein 1 Human genes 0.000 description 1
- 241000446313 Lamella Species 0.000 description 1
- 101100273674 Mus musculus Ccrl2 gene Proteins 0.000 description 1
- 101100338774 Mus musculus Hamp gene Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 230000001594 aberrant effect Effects 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- DGUFGVRBHSFJGU-UHFFFAOYSA-N acetic acid ethane-1,2-diol Chemical compound CC(O)=O.CC(O)=O.CC(O)=O.CC(O)=O.OCCO DGUFGVRBHSFJGU-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- CBTVGIZVANVGBH-UHFFFAOYSA-N aminomethyl propanol Chemical compound CC(C)(N)CO CBTVGIZVANVGBH-UHFFFAOYSA-N 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 230000000845 anti-microbial effect Effects 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 230000005875 antibody response Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 230000033228 biological regulation Effects 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
- 230000037396 body weight Effects 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 239000011545 carbonate/bicarbonate buffer Substances 0.000 description 1
- HFNQLYDPNAZRCH-UHFFFAOYSA-N carbonic acid Chemical compound OC(O)=O.OC(O)=O HFNQLYDPNAZRCH-UHFFFAOYSA-N 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000003759 clinical diagnosis Methods 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 230000000875 corresponding effect Effects 0.000 description 1
- 238000012258 culturing Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 230000005292 diamagnetic effect Effects 0.000 description 1
- 239000002270 dispersing agent Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 231100000673 dose–response relationship Toxicity 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 230000008482 dysregulation Effects 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 230000005294 ferromagnetic effect Effects 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229960001269 glycine hydrochloride Drugs 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000000951 immunodiffusion Effects 0.000 description 1
- 230000005847 immunogenicity Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000031891 intestinal absorption Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 125000001449 isopropyl group Chemical group [H]C([H])([H])C([H])(*)C([H])([H])[H] 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 239000006101 laboratory sample Substances 0.000 description 1
- 238000001698 laser desorption ionisation Methods 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 230000005291 magnetic effect Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 238000001254 matrix assisted laser desorption--ionisation time-of-flight mass spectrum Methods 0.000 description 1
- 238000002493 microarray Methods 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 108010087904 neutravidin Proteins 0.000 description 1
- JPMIIZHYYWMHDT-UHFFFAOYSA-N octhilinone Chemical compound CCCCCCCCN1SC=CC1=O JPMIIZHYYWMHDT-UHFFFAOYSA-N 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 239000002907 paramagnetic material Substances 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000007310 pathophysiology Effects 0.000 description 1
- 239000013610 patient sample Substances 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 210000001322 periplasm Anatomy 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 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 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000010791 quenching Methods 0.000 description 1
- 230000000171 quenching effect Effects 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000004064 recycling Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 238000002821 scintillation proximity assay Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000011285 therapeutic regimen Methods 0.000 description 1
- 230000004797 therapeutic response Effects 0.000 description 1
- 238000001196 time-of-flight mass spectrum Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 239000003656 tris buffered saline Substances 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
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
-
- 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
- C07K16/26—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against hormones ; against hormone releasing or inhibiting factors
-
- 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
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/06—Antianaemics
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/577—Immunoassay; Biospecific binding assay; Materials therefor involving monoclonal antibodies binding reaction mechanisms characterised by the use of monoclonal antibodies; monoclonal antibodies per se are classified with their corresponding antigens
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/74—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving hormones or other non-cytokine intercellular protein regulatory factors such as growth factors, including receptors to hormones and growth factors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/567—Framework region [FR]
-
- 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)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Hematology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Urology & Nephrology (AREA)
- Endocrinology (AREA)
- Microbiology (AREA)
- Biophysics (AREA)
- Biotechnology (AREA)
- Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Analytical Chemistry (AREA)
- Pathology (AREA)
- Genetics & Genomics (AREA)
- General Physics & Mathematics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Pharmacology & Pharmacy (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Veterinary Medicine (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- General Chemical & Material Sciences (AREA)
- Diabetes (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US8655708P | 2008-08-06 | 2008-08-06 | |
| PCT/US2009/052044 WO2010017070A1 (en) | 2008-08-06 | 2009-07-29 | Anti-hepcidin-25 selective antibodies and uses thereof |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2011001363A true MX2011001363A (es) | 2011-04-26 |
Family
ID=41165490
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2011001363A MX2011001363A (es) | 2008-08-06 | 2009-07-29 | Anticuerpos selectivos de anti-hepcidina-25 y usos de los mismos. |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US8609817B2 (enExample) |
| EP (1) | EP2328931B1 (enExample) |
| JP (1) | JP5730200B2 (enExample) |
| KR (1) | KR101462307B1 (enExample) |
| CN (1) | CN102112489B (enExample) |
| AU (1) | AU2009279865B2 (enExample) |
| BR (1) | BRPI0916624A2 (enExample) |
| CA (1) | CA2733497C (enExample) |
| DK (1) | DK2328931T3 (enExample) |
| EA (1) | EA201170312A1 (enExample) |
| ES (1) | ES2432018T3 (enExample) |
| IL (1) | IL210643A (enExample) |
| MX (1) | MX2011001363A (enExample) |
| NZ (1) | NZ590863A (enExample) |
| PL (1) | PL2328931T3 (enExample) |
| PT (1) | PT2328931E (enExample) |
| UA (1) | UA103032C2 (enExample) |
| WO (1) | WO2010017070A1 (enExample) |
| ZA (1) | ZA201100261B (enExample) |
Families Citing this family (20)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102584947B (zh) * | 2003-04-01 | 2014-03-12 | 国家健康医学研究所 | 针对丙型肝炎病毒e1e2 复合体的抗体、hcv 颗粒的组合物和药物组合物 |
| AR069062A1 (es) * | 2007-11-02 | 2009-12-23 | Lilly Co Eli | Anticuerpo anti-hepcidina |
| DK2606061T3 (da) | 2010-08-16 | 2017-11-06 | Pieris Pharmaceuticals Gmbh | Bindingsproteiner til hepcidin |
| AU2012350654C1 (en) | 2011-12-12 | 2018-05-10 | Pieris Ag | Methods for preventing or treating disorders by increasing bioavailability of iron and related pharmaceutical formulation |
| US10316103B1 (en) | 2012-03-30 | 2019-06-11 | Biocare Medical, Llc | Systems and methods for anti-Uroplakin III antibodies |
| US20140120560A1 (en) * | 2012-10-26 | 2014-05-01 | Claresa Levetan | Generation of new pancreatic beta cells |
| US10429390B2 (en) | 2012-12-18 | 2019-10-01 | Biocare Medical, Llc | Antibody cocktail systems and methods for classification of histologic subtypes in lung cancer |
| JP6463331B2 (ja) * | 2013-03-15 | 2019-01-30 | イントリンシック ライフサイエンシズ リミテッド ライアビリティ カンパニー | 抗ヘプシジン抗体およびその使用 |
| US9816997B2 (en) * | 2013-10-03 | 2017-11-14 | Biocare Medical, Llc | Anti-SOX10 antibody systems and methods |
| JPWO2016027469A1 (ja) * | 2014-08-21 | 2017-06-01 | 国立大学法人旭川医科大学 | ヘプシジンのスプライシングバリアント並びに該バリアントを指標とした癌の診断方法 |
| AU2015321462B2 (en) * | 2014-09-22 | 2020-04-30 | Intrinsic Lifesciences Llc | Humanized anti-hepcidin antibodies and uses thereof |
| WO2016146587A1 (en) | 2015-03-13 | 2016-09-22 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Hepcidin antagonists for use in the treatment of inflammation |
| US11692027B2 (en) | 2016-09-28 | 2023-07-04 | Board Of Regents, The University Of Texas System | Antibody and protein therapeutic formulations and uses thereof |
| EP3559039A1 (en) | 2016-12-22 | 2019-10-30 | Università Degli Studi Magna Graecia Catanzaro | A monoclonal antibody targeting a unique sialoglycosilated cancer-associated epitope of cd43 |
| WO2018234538A1 (en) | 2017-06-23 | 2018-12-27 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Hepcidin antagonist or agonist for use in the treatment of dysregulation of mo and/or mn metabolism |
| CN109948371B (zh) * | 2019-03-07 | 2021-06-25 | 深圳市智税链科技有限公司 | 为区块链节点发放身份证书的方法及相关装置 |
| JP2022549506A (ja) | 2019-09-27 | 2022-11-25 | ディスク・メディシン・インコーポレイテッド | 骨髄線維症および関連状態を処置するための方法 |
| EP4149548A4 (en) | 2020-05-13 | 2024-05-08 | Disc Medicine, Inc. | ANTI-HEMOJUVELIN ANTIBODIES (HJV) FOR THE TREATMENT OF MYELOFIBROSIS |
| WO2022098812A1 (en) | 2020-11-04 | 2022-05-12 | Keros Therapeutics, Inc. | Methods of treating iron overload |
| JPWO2022154121A1 (enExample) * | 2021-01-18 | 2022-07-21 |
Family Cites Families (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1210418B1 (en) | 1999-06-02 | 2010-08-18 | Genentech, Inc. | Secreted and transmembrane polypeptides and nucleic acids encoding the same |
| US6262247B1 (en) | 1999-08-30 | 2001-07-17 | Incyte Genomics, Inc. | Polycyclic aromatic hydrocarbon induced molecules |
| JP4944360B2 (ja) * | 2001-05-25 | 2012-05-30 | アンスティテュ ナシオナル ド ラ サント エ ド ラ ルシュルシェ メディカル（アンセルム） | 鉄ホメオスタシスの障害を治療するための医薬品を製造するためのヘプシジンの使用 |
| CN1173737C (zh) | 2002-10-21 | 2004-11-03 | 钱忠明 | Hepcidin(海魄喜定)在制药中的应用 |
| US7411048B2 (en) * | 2002-11-19 | 2008-08-12 | Drg International, Inc. | Diagnostic method for diseases by screening for hepcidin in human or animal tissues, blood or body fluids |
| EP1578254B1 (en) | 2002-11-19 | 2013-03-06 | DRG International, Inc. | Diagnostic method for diseases by screening for hepcidin in human or animal tissues, blood or body fluids and therapeutic uses therefor |
| US8017737B2 (en) | 2002-11-19 | 2011-09-13 | Hasan Kulaksiz | Diagnostic methods for diseases by screening for hepcidin in human or animal tissues, blood or body fluids; monoclonal antibodies specific to human hepcidin and associated uses therefor |
| US20050033029A1 (en) | 2003-06-30 | 2005-02-10 | Jin Lu | Engineered anti-target immunoglobulin derived proteins, compositions, methods and uses |
| CA2537668A1 (en) | 2003-09-29 | 2005-04-14 | Biosite Incorporated | Methods and compositions for the diagnosis of sepsis |
| AU2003271174A1 (en) * | 2003-10-10 | 2005-04-27 | Chugai Seiyaku Kabushiki Kaisha | Double specific antibodies substituting for functional protein |
| US7723063B2 (en) * | 2004-04-28 | 2010-05-25 | Intrinsic Lifesciences | Methods for measuring levels of bioactive human hepcidin |
| NZ560976A (en) | 2005-03-11 | 2011-06-30 | Univ Johns Hopkins | Biomarkers for ovarian cancer and endometrial cancer: hepcidin |
| MX2009008104A (es) | 2007-02-02 | 2009-08-07 | Amgen Inc | Hepcidina, antagonistas de hepcidina y metodos de uso. |
| GR1006896B (el) * | 2007-08-24 | 2010-07-20 | Ελληνικο Ινστιτουτο Παστερ, | Μεθοδος παραγωγης μιας πεπτιδικης ορμονης |
| CN101903044A (zh) | 2007-10-02 | 2010-12-01 | 国家健康与医学研究院 | 对人铁调素具有特异性的抗原结合蛋白 |
| AR069062A1 (es) * | 2007-11-02 | 2009-12-23 | Lilly Co Eli | Anticuerpo anti-hepcidina |
| EP2620448A1 (en) | 2008-05-01 | 2013-07-31 | Amgen Inc. | Anti-hepcidin antibodies and methods of use |
-
2009
- 2009-07-29 KR KR1020117002748A patent/KR101462307B1/ko not_active Expired - Fee Related
- 2009-07-29 CA CA2733497A patent/CA2733497C/en active Active
- 2009-07-29 PL PL09790908T patent/PL2328931T3/pl unknown
- 2009-07-29 EA EA201170312A patent/EA201170312A1/ru unknown
- 2009-07-29 UA UAA201101111A patent/UA103032C2/uk unknown
- 2009-07-29 BR BRPI0916624A patent/BRPI0916624A2/pt not_active IP Right Cessation
- 2009-07-29 NZ NZ590863A patent/NZ590863A/xx not_active IP Right Cessation
- 2009-07-29 ES ES09790908T patent/ES2432018T3/es active Active
- 2009-07-29 PT PT97909089T patent/PT2328931E/pt unknown
- 2009-07-29 US US13/055,201 patent/US8609817B2/en not_active Expired - Fee Related
- 2009-07-29 DK DK09790908.9T patent/DK2328931T3/da active
- 2009-07-29 WO PCT/US2009/052044 patent/WO2010017070A1/en not_active Ceased
- 2009-07-29 AU AU2009279865A patent/AU2009279865B2/en not_active Ceased
- 2009-07-29 JP JP2011522119A patent/JP5730200B2/ja not_active Expired - Fee Related
- 2009-07-29 MX MX2011001363A patent/MX2011001363A/es active IP Right Grant
- 2009-07-29 CN CN200980129864.0A patent/CN102112489B/zh not_active Expired - Fee Related
- 2009-07-29 EP EP09790908.9A patent/EP2328931B1/en active Active
-
2011
- 2011-01-10 ZA ZA2011/00261A patent/ZA201100261B/en unknown
- 2011-01-13 IL IL210643A patent/IL210643A/en not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| AU2009279865B2 (en) | 2013-10-10 |
| EP2328931B1 (en) | 2013-08-14 |
| HK1156326A1 (en) | 2012-06-08 |
| PL2328931T3 (pl) | 2014-01-31 |
| UA103032C2 (uk) | 2013-09-10 |
| CA2733497A1 (en) | 2010-02-11 |
| EP2328931A1 (en) | 2011-06-08 |
| PT2328931E (pt) | 2013-11-07 |
| US20110189190A1 (en) | 2011-08-04 |
| KR101462307B1 (ko) | 2014-11-17 |
| IL210643A0 (en) | 2011-03-31 |
| ES2432018T3 (es) | 2013-11-29 |
| IL210643A (en) | 2015-09-24 |
| JP2011530514A (ja) | 2011-12-22 |
| CN102112489A (zh) | 2011-06-29 |
| NZ590863A (en) | 2012-10-26 |
| BRPI0916624A2 (pt) | 2015-12-01 |
| JP5730200B2 (ja) | 2015-06-03 |
| CN102112489B (zh) | 2014-05-14 |
| AU2009279865A1 (en) | 2010-02-11 |
| KR20110031963A (ko) | 2011-03-29 |
| CA2733497C (en) | 2015-06-02 |
| US8609817B2 (en) | 2013-12-17 |
| EA201170312A1 (ru) | 2012-03-30 |
| DK2328931T3 (da) | 2013-09-30 |
| WO2010017070A1 (en) | 2010-02-11 |
| ZA201100261B (en) | 2012-06-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU2009279865B2 (en) | Anti-hepcidin-25 selective antibodies and uses thereof | |
| CN112250763B (zh) | 靶向SARS-CoV-2冠状病毒的抗体及其诊断和检测用途 | |
| CN110464842B (zh) | 包含抗pcsk9抗体的制剂及其用途 | |
| KR102748987B1 (ko) | 사스-코로나바이러스-2에 특이적으로 결합하는 항체 및 그의 용도 | |
| JP2025020209A (ja) | インターロイキン－１９を標的とする化合物および方法 | |
| AU2019395325A1 (en) | Anti-Alpha-Synuclein Antibodies and Uses Thereof | |
| CN110423278B (zh) | 一种抗凝血因子XI活化形式因子XIa的抗体及其制备方法和应用 | |
| US20150355199A1 (en) | Agents, kits and methods for complement factor h-related protein 1 detection | |
| KR102421918B1 (ko) | 호산구 유래 신경독과 특이적으로 결합하는 단일클론항체 및 이의 용도 | |
| HK1156326B (en) | Anti-hepcidin-25 selective antibodies and uses thereof | |
| US20240044920A1 (en) | Anti-ceruloplasmin antibodies and uses thereof | |
| CA3188429A1 (en) | Compounds and methods targeting human and mouse insl5 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG | Grant or registration |