CA3031858A1 - Alkaline stable fc-binding proteins for affinity chromatography - Google Patents
Alkaline stable fc-binding proteins for affinity chromatography Download PDFInfo
- Publication number
- CA3031858A1 CA3031858A1 CA3031858A CA3031858A CA3031858A1 CA 3031858 A1 CA3031858 A1 CA 3031858A1 CA 3031858 A CA3031858 A CA 3031858A CA 3031858 A CA3031858 A CA 3031858A CA 3031858 A1 CA3031858 A1 CA 3031858A1
- Authority
- CA
- Canada
- Prior art keywords
- protein
- binding
- binding protein
- sequence
- affinity
- 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.)
- Pending
Links
- 108091008324 binding proteins Proteins 0.000 title claims abstract description 151
- 102000014914 Carrier Proteins Human genes 0.000 title claims abstract 25
- 238000001042 affinity chromatography Methods 0.000 title description 9
- 230000027455 binding Effects 0.000 claims abstract description 81
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 55
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 55
- 238000000034 method Methods 0.000 claims abstract description 48
- 238000001261 affinity purification Methods 0.000 claims abstract description 25
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 25
- 108090000623 proteins and genes Proteins 0.000 claims description 113
- 102000004169 proteins and genes Human genes 0.000 claims description 111
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 78
- 239000011159 matrix material Substances 0.000 claims description 63
- 150000001413 amino acids Chemical class 0.000 claims description 27
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 25
- 238000000926 separation method Methods 0.000 claims description 21
- 239000007787 solid Substances 0.000 claims description 18
- 238000011534 incubation Methods 0.000 claims description 17
- 238000010168 coupling process Methods 0.000 claims description 15
- 230000008878 coupling Effects 0.000 claims description 14
- 238000005859 coupling reaction Methods 0.000 claims description 14
- 238000010828 elution Methods 0.000 claims description 14
- 230000009870 specific binding Effects 0.000 claims description 9
- 239000012634 fragment Substances 0.000 claims description 7
- 238000012217 deletion Methods 0.000 claims description 6
- 230000037430 deletion Effects 0.000 claims description 6
- 230000009467 reduction Effects 0.000 claims description 6
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 claims description 4
- 238000005406 washing Methods 0.000 claims description 4
- 229940072221 immunoglobulins Drugs 0.000 abstract description 25
- 102000023732 binding proteins Human genes 0.000 description 126
- 235000018102 proteins Nutrition 0.000 description 94
- 235000001014 amino acid Nutrition 0.000 description 25
- 210000004027 cell Anatomy 0.000 description 19
- 239000003446 ligand Substances 0.000 description 14
- 102000004196 processed proteins & peptides Human genes 0.000 description 13
- 229920001184 polypeptide Polymers 0.000 description 12
- 210000004899 c-terminal region Anatomy 0.000 description 11
- 238000004587 chromatography analysis Methods 0.000 description 11
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 10
- 239000000523 sample Substances 0.000 description 9
- 229920000936 Agarose Polymers 0.000 description 8
- 238000010494 dissociation reaction Methods 0.000 description 8
- 230000005593 dissociations Effects 0.000 description 8
- 102000037865 fusion proteins Human genes 0.000 description 8
- 108020001507 fusion proteins Proteins 0.000 description 8
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 7
- 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 7
- 230000000694 effects Effects 0.000 description 7
- 102000028557 immunoglobulin binding proteins Human genes 0.000 description 7
- 108091009323 immunoglobulin binding proteins Proteins 0.000 description 7
- 108020004707 nucleic acids Proteins 0.000 description 7
- 102000039446 nucleic acids Human genes 0.000 description 7
- 150000007523 nucleic acids Chemical class 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- 230000005526 G1 to G0 transition Effects 0.000 description 6
- 229920002684 Sepharose Polymers 0.000 description 6
- 239000011324 bead Substances 0.000 description 6
- 238000004140 cleaning Methods 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 6
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 6
- -1 cysteine or lysine Chemical class 0.000 description 6
- 239000007788 liquid Substances 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 239000000203 mixture Substances 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000007790 solid phase Substances 0.000 description 6
- 238000004458 analytical method Methods 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 239000000872 buffer Substances 0.000 description 5
- 229960005395 cetuximab Drugs 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 5
- 239000013598 vector Substances 0.000 description 5
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 239000004471 Glycine Substances 0.000 description 4
- 108010058683 Immobilized Proteins Proteins 0.000 description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 4
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 4
- 125000000539 amino acid group Chemical group 0.000 description 4
- 239000007979 citrate buffer Substances 0.000 description 4
- 239000013604 expression vector Substances 0.000 description 4
- 239000011347 resin Substances 0.000 description 4
- 229920005989 resin Polymers 0.000 description 4
- 108020004414 DNA Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 238000012575 bio-layer interferometry Methods 0.000 description 3
- 239000003518 caustics Substances 0.000 description 3
- 239000001913 cellulose Substances 0.000 description 3
- 229920002678 cellulose Polymers 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000000356 contaminant Substances 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 229930027917 kanamycin Natural products 0.000 description 3
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 3
- 229960000318 kanamycin Drugs 0.000 description 3
- 229930182823 kanamycin A Natural products 0.000 description 3
- 239000008101 lactose Substances 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 108020001580 protein domains Proteins 0.000 description 3
- 239000012146 running buffer Substances 0.000 description 3
- 229920006395 saturated elastomer Polymers 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 2
- 101800001415 Bri23 peptide Proteins 0.000 description 2
- 102400000107 C-terminal peptide Human genes 0.000 description 2
- 101800000655 C-terminal peptide Proteins 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 238000001712 DNA sequencing Methods 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 239000004593 Epoxy Substances 0.000 description 2
- 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 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical group [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- MCMNRKCIXSYSNV-UHFFFAOYSA-N Zirconium dioxide Chemical compound O=[Zr]=O MCMNRKCIXSYSNV-UHFFFAOYSA-N 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 239000012670 alkaline solution Substances 0.000 description 2
- 239000002518 antifoaming agent Substances 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 239000004202 carbamide Substances 0.000 description 2
- 239000012504 chromatography matrix Substances 0.000 description 2
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
- 238000001378 electrochemiluminescence detection Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 239000000499 gel Substances 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 239000000017 hydrogel Substances 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000000111 isothermal titration calorimetry Methods 0.000 description 2
- 235000018977 lysine Nutrition 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000008188 pellet Substances 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 102200074807 rs61747482 Human genes 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- DJQYYYCQOZMCRC-UHFFFAOYSA-N 2-aminopropane-1,3-dithiol Chemical compound SCC(N)CS DJQYYYCQOZMCRC-UHFFFAOYSA-N 0.000 description 1
- 108010011170 Ala-Trp-Arg-His-Pro-Gln-Phe-Gly-Gly Proteins 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 229920002307 Dextran Polymers 0.000 description 1
- 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 1
- 102000028555 IgG binding proteins Human genes 0.000 description 1
- 108091009325 IgG binding proteins Proteins 0.000 description 1
- 241000235058 Komagataella pastoris Species 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
- 239000007993 MOPS buffer Substances 0.000 description 1
- PEEHTFAAVSWFBL-UHFFFAOYSA-N Maleimide Chemical compound O=C1NC(=O)C=C1 PEEHTFAAVSWFBL-UHFFFAOYSA-N 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 108010052285 Membrane Proteins Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 229920001218 Pullulan Polymers 0.000 description 1
- 239000004373 Pullulan Substances 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 108010034546 Serratia marcescens nuclease Proteins 0.000 description 1
- 241000191967 Staphylococcus aureus Species 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 239000012505 Superdex™ Substances 0.000 description 1
- GWEVSGVZZGPLCZ-UHFFFAOYSA-N Titan oxide Chemical compound O=[Ti]=O GWEVSGVZZGPLCZ-UHFFFAOYSA-N 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 150000001252 acrylic acid derivatives Chemical class 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 125000002009 alkene group Chemical group 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000013103 analytical ultracentrifugation Methods 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- OWMVSZAMULFTJU-UHFFFAOYSA-N bis-tris Chemical compound OCCN(CCO)C(CO)(CO)CO OWMVSZAMULFTJU-UHFFFAOYSA-N 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 235000010980 cellulose Nutrition 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012412 chemical coupling Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 239000005289 controlled pore glass Substances 0.000 description 1
- 238000011157 data evaluation Methods 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 125000003700 epoxy group Chemical group 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 125000004185 ester group Chemical group 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000011536 extraction buffer Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- 238000000126 in silico method Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 125000003588 lysine group Chemical class [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000012516 mab select resin Substances 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 150000002734 metacrylic acid derivatives Chemical class 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 229960005027 natalizumab Drugs 0.000 description 1
- RVTZCBVAJQQJTK-UHFFFAOYSA-N oxygen(2-);zirconium(4+) Chemical compound [O-2].[O-2].[Zr+4] RVTZCBVAJQQJTK-UHFFFAOYSA-N 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 229920001289 polyvinyl ether Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 235000019423 pullulan Nutrition 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 239000012557 regeneration buffer Substances 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 238000011012 sanitization Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 239000012798 spherical particle Substances 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- OGIDPMRJRNCKJF-UHFFFAOYSA-N titanium oxide Inorganic materials [Ti]=O OGIDPMRJRNCKJF-UHFFFAOYSA-N 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
- 238000013519 translation Methods 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- 229910001928 zirconium oxide Inorganic materials 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/305—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F)
- C07K14/31—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Micrococcaceae (F) from Staphylococcus (G)
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/38—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups B01D15/265 and B01D15/30 - B01D15/36, e.g. affinity, ligand exchange or chiral chromatography
- B01D15/3804—Affinity chromatography
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/26—Selective adsorption, e.g. chromatography characterised by the separation mechanism
- B01D15/38—Selective adsorption, e.g. chromatography characterised by the separation mechanism involving specific interaction not covered by one or more of groups B01D15/265 and B01D15/30 - B01D15/36, e.g. affinity, ligand exchange or chiral chromatography
- B01D15/3804—Affinity chromatography
- B01D15/3809—Affinity chromatography of the antigen-antibody type, e.g. protein A, G or L chromatography
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D15/00—Separating processes involving the treatment of liquids with solid sorbents; Apparatus therefor
- B01D15/08—Selective adsorption, e.g. chromatography
- B01D15/42—Selective adsorption, e.g. chromatography characterised by the development mode, e.g. by displacement or by elution
- B01D15/424—Elution mode
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01J—CHEMICAL OR PHYSICAL PROCESSES, e.g. CATALYSIS OR COLLOID CHEMISTRY; THEIR RELEVANT APPARATUS
- B01J20/00—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof
- B01J20/22—Solid sorbent compositions or filter aid compositions; Sorbents for chromatography; Processes for preparing, regenerating or reactivating thereof comprising organic material
- B01J20/26—Synthetic macromolecular compounds
- B01J20/262—Synthetic macromolecular compounds obtained otherwise than by reactions only involving carbon to carbon unsaturated bonds, e.g. obtained by polycondensation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/22—Affinity chromatography or related techniques based upon selective absorption processes
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/06—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies from serum
- C07K16/065—Purification, fragmentation
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K17/00—Carrier-bound or immobilised peptides; Preparation thereof
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B01—PHYSICAL OR CHEMICAL PROCESSES OR APPARATUS IN GENERAL
- B01D—SEPARATION
- B01D2221/00—Applications of separation devices
- B01D2221/10—Separation devices for use in medical, pharmaceutical or laboratory applications, e.g. separating amalgam from dental treatment residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Analytical Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Solid-Sorbent Or Filter-Aiding Compositions (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP16183710 | 2016-08-11 | ||
| EP16183710.9 | 2016-08-11 | ||
| EP16205707 | 2016-12-21 | ||
| EP16205707.9 | 2016-12-21 | ||
| PCT/EP2017/069979 WO2018029158A1 (en) | 2016-08-11 | 2017-08-07 | Alkaline stable fc—binding proteins for affinity chromatography |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA3031858A1 true CA3031858A1 (en) | 2018-02-15 |
Family
ID=59631752
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA3031858A Pending CA3031858A1 (en) | 2016-08-11 | 2017-08-07 | Alkaline stable fc-binding proteins for affinity chromatography |
| CA3030208A Pending CA3030208A1 (en) | 2016-08-11 | 2017-08-07 | Novel alkaline stable immunoglobulin binding proteins |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA3030208A Pending CA3030208A1 (en) | 2016-08-11 | 2017-08-07 | Novel alkaline stable immunoglobulin binding proteins |
Country Status (11)
| Country | Link |
|---|---|
| US (4) | US11230576B2 (enExample) |
| EP (4) | EP3497118B1 (enExample) |
| JP (3) | JP7181612B2 (enExample) |
| KR (3) | KR102573370B1 (enExample) |
| CN (4) | CN109963864B (enExample) |
| AU (2) | AU2017311541B2 (enExample) |
| CA (2) | CA3031858A1 (enExample) |
| DK (1) | DK3497117T5 (enExample) |
| LT (1) | LT3497117T (enExample) |
| SG (1) | SG11201901066UA (enExample) |
| WO (2) | WO2018029157A1 (enExample) |
Families Citing this family (30)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP6738340B2 (ja) | 2015-02-06 | 2020-08-12 | ナフィゴ プロテインズ ゲゼルシャフト ミット ベシュレンクテル ハフツングＮａｖｉｇｏ Ｐｒｏｔｅｉｎｓ ＧｍｂＨ | 新規なｅｇｆｒ結合タンパク質 |
| CA2991812C (en) | 2015-07-16 | 2024-02-13 | Navigo Proteins Gmbh | Immunoglobulin-binding proteins and their use in affinity purification |
| JP2018520675A (ja) | 2015-07-20 | 2018-08-02 | ナフィゴ プロテインズ ゲゼルシャフト ミット ベシュレンクテル ハフツングＮａｖｉｇｏ Ｐｒｏｔｅｉｎｓ ＧｍｂＨ | ジユビキチン変異タンパク質をベースとした新規結合タンパク質及びその生成方法 |
| CA3022751A1 (en) | 2016-05-04 | 2017-11-09 | Navigo Proteins Gmbh | Targeted compounds for the site-specific coupling of chemical moieties comprising a peptide linker |
| CN109963864B (zh) * | 2016-08-11 | 2024-01-02 | 瑞普利金公司 | 用于亲和色谱的碱性稳定性fc结合蛋白 |
| EP3546476A1 (en) * | 2018-03-26 | 2019-10-02 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
| EP4491268A3 (en) * | 2017-08-07 | 2025-04-09 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
| WO2019091918A1 (en) | 2017-11-07 | 2019-05-16 | Navigo Proteins Gmbh | Fusion proteins with specificity for ed-b and long serum half-life for diagnosis or treatment of cancer |
| EP4249097A3 (en) | 2018-02-01 | 2024-01-10 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
| JP7591284B2 (ja) * | 2018-11-12 | 2024-11-28 | ナフィゴ プロテインズ ゲゼルシャフト ミット ベシュレンクテル ハフツング | 免疫グロブリンＦｃドメインに対する結合親和性を持たない新規三重らせんポリペプチド及び同ポリペプチドの使用 |
| EP3650465A1 (en) | 2018-11-12 | 2020-05-13 | Navigo Proteins Gmbh | Novel populations of polypeptides having a triple-helical structure |
| AU2020213921B2 (en) * | 2019-02-01 | 2022-06-16 | Navigo Proteins Gmbh | Immunoglobulin binding proteins for affinity purification |
| GB201904125D0 (en) | 2019-03-26 | 2019-05-08 | Ge Healthcare Bio Sciences Ab | Method for sanitization of a chromatography column |
| JP7432813B2 (ja) * | 2019-09-10 | 2024-02-19 | 東ソー株式会社 | 免疫グロブリン結合性タンパク質 |
| CA3155432A1 (en) * | 2019-12-17 | 2021-06-24 | Navigo Proteins Gmbh | Binding proteins for the enzyme acid alpha glucosidase (gaa) and uses thereof |
| WO2021165395A1 (en) * | 2020-02-21 | 2021-08-26 | Navigo Proteins Gmbh | Affinity ligand for the soluble part of fibroblast growth factor receptor 3 (sfgfr3) |
| EP3875472A1 (en) * | 2020-03-06 | 2021-09-08 | Navigo Proteins Gmbh | Novel immunoglobulin binding polypeptides |
| CA3183655A1 (en) * | 2020-06-23 | 2021-12-30 | Mathias KAHL | Binding protein specific for the spike protein of severe acute respiratory syndrome corona virus 2 (sars-cov-2) |
| EP4132943B1 (en) * | 2020-07-15 | 2024-05-29 | Navigo Proteins Gmbh | Immunoglobulin binding proteins for affinity purification |
| JP2023547340A (ja) * | 2020-11-09 | 2023-11-10 | ナフィゴ プロテインズ ゲゼルシャフト ミット ベシュレンクテル ハフツング | 新規ｉｉ型コラーゲン結合タンパク質 |
| EP4001301A1 (en) * | 2020-11-13 | 2022-05-25 | Navigo Proteins Gmbh | Binding protein for complement factor h (cfh) |
| EP4380955A1 (en) * | 2021-08-06 | 2024-06-12 | Roche Diagnostics GmbH | Chimeric igg-fc-binding ligand polypeptide and uses thereof for igg affinity purification |
| GB202113626D0 (en) | 2021-09-24 | 2021-11-10 | Cytiva Bioprocess R & D Ab | FC binding polypeptides |
| CN116675729A (zh) * | 2021-12-21 | 2023-09-01 | 百林科(兰州)新材料有限公司 | 耐碱蛋白A变体去除样品中IgG抗体的应用 |
| CN113999294B (zh) * | 2021-12-30 | 2022-03-29 | 苏州纳微科技股份有限公司 | 免疫球蛋白结合蛋白及其应用 |
| CN114409748A (zh) * | 2022-01-28 | 2022-04-29 | 博格隆(浙江)生物技术有限公司 | 蛋白a的b结构域和z结构域突变体及其应用 |
| GB202203478D0 (en) | 2022-03-14 | 2022-04-27 | Cytiva Bioprocess R & D Ab | Vh3 binding polypeptides |
| KR20250112269A (ko) * | 2022-12-16 | 2025-07-23 | 나피고 프로타인스 게엠베하 | 친화성 크로마토그래피를 위한 신규한 리간드 |
| WO2025059162A1 (en) | 2023-09-11 | 2025-03-20 | Dana-Farber Cancer Institute, Inc. | Car-engager containing il-2 variants to enhance the functionality of car t cells |
| EP4541444A1 (en) * | 2023-10-20 | 2025-04-23 | Cytiva BioProcess R&D AB | Fusion protein for affinity capture |
Family Cites Families (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4873192A (en) | 1987-02-17 | 1989-10-10 | The United States Of America As Represented By The Department Of Health And Human Services | Process for site specific mutagenesis without phenotypic selection |
| SE9103701D0 (sv) | 1991-12-13 | 1991-12-13 | Kabi Pharmacia Ab | Apolipoprotein |
| US5629167A (en) * | 1994-04-19 | 1997-05-13 | Biocine S.P.A. | Detection of antibodies against Chlamydia trachomatis pgp3 antigen in patient sera by enzyme-linked immunosorbent assay |
| DE69533102T2 (de) * | 1994-07-21 | 2005-06-02 | Aventis Pasteur Ltd., Toronto | Analog von haemophilus hin47 mit verminderter protease aktivität |
| AU7142796A (en) | 1995-10-02 | 1997-04-28 | Erasmus University Rotterdam | Diagnosis method and reagents |
| WO1997016556A1 (en) | 1995-10-30 | 1997-05-09 | Massachusetts Institute Of Technology | Rationally designed polysaccharide lyases derived from heparinase i |
| US5789166A (en) | 1995-12-08 | 1998-08-04 | Stratagene | Circular site-directed mutagenesis |
| GB9610967D0 (en) | 1996-05-24 | 1996-07-31 | Cambridge Antibody Tech | Specific binding members,materials and methods |
| FR2761689B1 (fr) | 1997-04-02 | 1999-06-25 | Transgene Sa | Fibre adenovirale modifiee et adenovirus cibles |
| EP0985032B2 (en) | 1997-05-28 | 2009-06-03 | Discerna Limited | Ribosome complexes as selection particles for in vitro display and evolution of proteins |
| CA2293632C (en) | 1997-06-12 | 2011-11-29 | Research Corporation Technologies, Inc. | Artificial antibody polypeptides |
| DE19742706B4 (de) | 1997-09-26 | 2013-07-25 | Pieris Proteolab Ag | Lipocalinmuteine |
| TWI259837B (en) | 1998-05-11 | 2006-08-11 | Eidgenossische Tech Hochscule | Specific binding molecules for scintigraphy, conjugates containing them and therapeutic method for treatment of angiogenesis |
| US20030045681A1 (en) | 1998-05-11 | 2003-03-06 | Anthony J. Zelano | Specific binding molecules for scintigraphy, conjugates containing them and therapeutic method for treatment of angiogenesis |
| DE19932688B4 (de) | 1999-07-13 | 2009-10-08 | Scil Proteins Gmbh | Design von Beta-Faltblatt-Proteinen des gamma-II-kristallins antikörperähnlichen |
| AU4243201A (en) | 2000-02-24 | 2001-09-03 | Eidgenoess Tech Hochschule | Antibody specific for the ed-b domain of fibronectin, conjugates comprising saidantibody, and their use for the detection and treatment of angiogenesis |
| DK1719528T3 (da) | 2000-02-24 | 2012-01-09 | Philogen Spa | Sammensætninger og fremgangsmåder til behandling af angiogenese i patologiske læsioner |
| US6799121B2 (en) | 2000-03-30 | 2004-09-28 | York University | Sequencing of peptides by mass spectrometry |
| US20110179531A1 (en) | 2000-05-09 | 2011-07-21 | Kovalic David K | Nucleic acid molecules and other molecules associated with plants and uses thereof for plant improvement |
| US20030073623A1 (en) | 2001-07-30 | 2003-04-17 | Drmanac Radoje T. | Novel nucleic acid sequences obtained from various cDNA libraries |
| AU2003210802B2 (en) | 2002-02-05 | 2009-09-10 | Genentech Inc. | Protein purification |
| SE0200943D0 (sv) * | 2002-03-25 | 2002-03-25 | Amersham Biosciences Ab | Mutant protein |
| US20040043386A1 (en) | 2002-08-30 | 2004-03-04 | Todd Pray | Methods and compositions for functional ubiquitin assays |
| EP1591527B1 (en) | 2003-01-23 | 2015-08-26 | Ono Pharmaceutical Co., Ltd. | Substance specific to human pd-1 |
| DE10324447A1 (de) | 2003-05-28 | 2004-12-30 | Scil Proteins Gmbh | Generierung künstlicher Bindungsproteine auf der Grundlage von Ubiquitin |
| WO2005044845A2 (en) | 2003-11-04 | 2005-05-19 | Yale University | Protein binding miniature proteins |
| WO2005059131A2 (en) | 2003-12-11 | 2005-06-30 | Yale University | Protein binding miniature proteins and uses thereof |
| DE10360483B4 (de) | 2003-12-22 | 2007-11-15 | Scil Proteins Gmbh | Expressionsvektor und dessen Verwendung |
| DE102004014983A1 (de) | 2004-03-26 | 2005-10-20 | Univ Stuttgart | Rekombinante Polypeptide der Mitglieder der TNF Ligandenfamilie und deren Verwendung |
| DE102004049479A1 (de) | 2004-10-11 | 2006-04-13 | Scil Proteins Gmbh | Proteinkonjugate zur Verwendung in Therapie, Diagnose und Chromatographie |
| JP2006304633A (ja) | 2005-04-26 | 2006-11-09 | Apro Life Science Institute Inc | イムノグロブリン結合タンパク質 |
| JP2008543278A (ja) | 2005-05-11 | 2008-12-04 | フィロゲン エスピーエー | フィブロネクチンｅｄ−ｂに対する抗体ｌ１９とインターロイキン１２との融合タンパク質 |
| MY185597A (en) * | 2005-09-20 | 2021-05-24 | Avantor Performance Mat Inc | Vegetarian protein a preparation and methods thereof |
| EP1945767B1 (de) | 2005-11-09 | 2010-04-07 | MorphoSys AG | Identifizierung und charakterisierung von funktionsblockierenden anti-ed-b-fibronektin antikörpern |
| EP1842553A1 (en) | 2006-04-07 | 2007-10-10 | Bayer Schering Pharma Aktiengesellschaft | Combination of an anti-EDb fibronectin domain antibody/IL2 fusion protein and a further small molecule |
| ES2606490T3 (es) | 2006-05-08 | 2017-03-24 | Philogen S.P.A. | Citocinas dirigidas por anticuerpos para terapia |
| EP1892248A1 (en) | 2006-08-21 | 2008-02-27 | Eidgenössische Technische Hochschule Zürich | Specific and high affinity binding proteins comprising modified SH3 domains of FYN kinase |
| CN101522278B (zh) * | 2006-09-29 | 2016-08-10 | 通用电气健康护理生物科学股份公司 | 用于抗体分离的包含来自金黄色葡萄球菌a蛋白的结构域c的层析配体 |
| EP1925664A1 (en) | 2006-11-15 | 2008-05-28 | Scil proteins GmbH | Artificial binding proteins based on a modified alpha helical region of ubiquitin |
| EP1955712A1 (en) | 2007-02-09 | 2008-08-13 | Scil proteins GmbH | Multimeric conjugate |
| CA2731388C (en) | 2008-07-21 | 2018-05-01 | Apogenix Gmbh | Tnfsf single chain molecules |
| US8592555B2 (en) * | 2008-08-11 | 2013-11-26 | Emd Millipore Corporation | Immunoglobulin-binding proteins with improved specificity |
| CN102753568B (zh) | 2009-12-14 | 2014-08-20 | 塞尔蛋白质股份有限公司 | 用于识别具有结合配体能力的异源多聚体修饰的泛素蛋白质的方法 |
| KR101893225B1 (ko) * | 2010-03-24 | 2018-08-29 | 가부시키가이샤 가네카 | 면역 글로불린에 특이적으로 결합하는 단백질 및 면역 글로불린 결합성의 친화성 리간드 |
| WO2012133349A1 (ja) * | 2011-03-25 | 2012-10-04 | 株式会社カネカ | アフィニティー分離マトリックス用タンパク質 |
| SG10201604559TA (en) * | 2011-06-08 | 2016-07-28 | Emd Millipore Corp | Chromatography matrices including novel staphylococcus aureus protein a based ligands |
| US9492572B2 (en) | 2011-06-15 | 2016-11-15 | Scil Proteins Gmbh | Dimeric binding proteins based on modified ubiquitins |
| WO2012171541A1 (en) | 2011-06-15 | 2012-12-20 | Scil Proteins Gmbh | Human fusion proteins comprising interferons and hetero-dimeric modified ubiquitin proteins |
| WO2013186329A1 (en) | 2012-06-13 | 2013-12-19 | Scil Proteins Gmbh | Human fusion proteins comprising single chain tnfalpha and targeting domains |
| AU2013318928A1 (en) | 2012-09-21 | 2015-04-09 | Kaneka Corporation | Protein ligand for affinity isolation matrix |
| EP2727942A1 (en) | 2012-11-05 | 2014-05-07 | MAB Discovery GmbH | Bispecific antibodies against human EGFR, HER2, and HER3 |
| EP2738180A1 (en) | 2012-11-30 | 2014-06-04 | Molecular Partners AG | Binding proteins comprising at least two binding domains against HER2. |
| WO2014094799A1 (en) | 2012-12-19 | 2014-06-26 | Scil-Proteins-Gmbh | Ubiquitin moieties as a means for prolonging serum half-life |
| US9896486B2 (en) * | 2013-07-10 | 2018-02-20 | Ge Healthcare Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| KR102236367B1 (ko) | 2013-07-26 | 2021-04-05 | 삼성전자주식회사 | DARPin을 포함하는 이중 특이 키메라 단백질 |
| US11566082B2 (en) * | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| US20180030140A1 (en) | 2015-02-06 | 2018-02-01 | Navigo Proteins Gmbh | Novel binding proteins comprising a ubiquitin mutein and antibodies or antibody fragments |
| JP6738340B2 (ja) | 2015-02-06 | 2020-08-12 | ナフィゴ プロテインズ ゲゼルシャフト ミット ベシュレンクテル ハフツングＮａｖｉｇｏ Ｐｒｏｔｅｉｎｓ ＧｍｂＨ | 新規なｅｇｆｒ結合タンパク質 |
| CA2991812C (en) | 2015-07-16 | 2024-02-13 | Navigo Proteins Gmbh | Immunoglobulin-binding proteins and their use in affinity purification |
| JP2018520675A (ja) | 2015-07-20 | 2018-08-02 | ナフィゴ プロテインズ ゲゼルシャフト ミット ベシュレンクテル ハフツングＮａｖｉｇｏ Ｐｒｏｔｅｉｎｓ ＧｍｂＨ | ジユビキチン変異タンパク質をベースとした新規結合タンパク質及びその生成方法 |
| CA2991814A1 (en) | 2015-07-20 | 2017-01-26 | Navigo Proteins Gmbh | Her2 binding proteins based on di-ubiquitin muteins |
| CA3022751A1 (en) | 2016-05-04 | 2017-11-09 | Navigo Proteins Gmbh | Targeted compounds for the site-specific coupling of chemical moieties comprising a peptide linker |
| CN109963864B (zh) | 2016-08-11 | 2024-01-02 | 瑞普利金公司 | 用于亲和色谱的碱性稳定性fc结合蛋白 |
| EP4491268A3 (en) | 2017-08-07 | 2025-04-09 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
| WO2019091918A1 (en) | 2017-11-07 | 2019-05-16 | Navigo Proteins Gmbh | Fusion proteins with specificity for ed-b and long serum half-life for diagnosis or treatment of cancer |
| EP4249097A3 (en) | 2018-02-01 | 2024-01-10 | Repligen Corporation | Fc binding proteins with cysteine in the c-terminal helical region |
-
2017
- 2017-08-07 CN CN201780050413.2A patent/CN109963864B/zh active Active
- 2017-08-07 JP JP2019505354A patent/JP7181612B2/ja active Active
- 2017-08-07 WO PCT/EP2017/069976 patent/WO2018029157A1/en not_active Ceased
- 2017-08-07 CN CN202210871980.7A patent/CN116333065A/zh active Pending
- 2017-08-07 WO PCT/EP2017/069979 patent/WO2018029158A1/en not_active Ceased
- 2017-08-07 CN CN202311795884.XA patent/CN117736281A/zh active Pending
- 2017-08-07 KR KR1020197003966A patent/KR102573370B1/ko active Active
- 2017-08-07 EP EP17752350.3A patent/EP3497118B1/en active Active
- 2017-08-07 EP EP23218805.2A patent/EP4324840A3/en active Pending
- 2017-08-07 US US16/324,651 patent/US11230576B2/en active Active
- 2017-08-07 KR KR1020237030862A patent/KR20230133943A/ko not_active Ceased
- 2017-08-07 KR KR1020197003790A patent/KR102578256B1/ko active Active
- 2017-08-07 LT LTEPPCT/EP2017/069976T patent/LT3497117T/lt unknown
- 2017-08-07 CA CA3031858A patent/CA3031858A1/en active Pending
- 2017-08-07 CN CN201780044905.0A patent/CN109476712B/zh active Active
- 2017-08-07 CA CA3030208A patent/CA3030208A1/en active Pending
- 2017-08-07 DK DK17752349.5T patent/DK3497117T5/da active
- 2017-08-07 JP JP2019507171A patent/JP6951417B2/ja active Active
- 2017-08-07 EP EP17752349.5A patent/EP3497117B1/en active Active
- 2017-08-07 SG SG11201901066UA patent/SG11201901066UA/en unknown
- 2017-08-07 AU AU2017311541A patent/AU2017311541B2/en active Active
- 2017-08-07 US US16/324,842 patent/US11014967B2/en active Active
- 2017-08-07 EP EP22193930.9A patent/EP4177260A1/en active Pending
- 2017-08-07 AU AU2017311542A patent/AU2017311542B2/en active Active
-
2021
- 2021-03-23 US US17/209,455 patent/US20210206815A1/en not_active Abandoned
-
2022
- 2022-07-13 JP JP2022112299A patent/JP2022160444A/ja active Pending
-
2024
- 2024-09-03 US US18/822,867 patent/US20250051400A1/en active Pending
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20250051400A1 (en) | Alkaline stable fc-binding proteins for affinity chromatography | |
| US12257530B2 (en) | Fc binding proteins with cysteine in the c-terminal helical region | |
| US20230340069A1 (en) | Fc binding proteins with cysteine in the c-terminal helical region | |
| AU2020213921B2 (en) | Immunoglobulin binding proteins for affinity purification | |
| EP3546476A1 (en) | Fc binding proteins with cysteine in the c-terminal helical region |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20220330 |
|
| EEER | Examination request |
Effective date: 20220330 |
|
| EEER | Examination request |
Effective date: 20220330 |
|
| EEER | Examination request |
Effective date: 20220330 |
|
| EEER | Examination request |
Effective date: 20220330 |