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Lampalizumab (anti-Complement Factor D) (Ab175571) - SEC
The purity of Lampalizumab (anti-Complement Factor D) (Ab175571) is more than 95% verified by HPLC.
SKU | Size | Availability | Price | Qty |
---|---|---|---|---|
Ab175571-100μg | 100μg | In stock | $109.90 | |
Ab175571-1mg | 1mg | In stock | $519.90 | |
Ab175571-5mg | 5mg | In stock | $1,399.90 | |
Ab175571-10mg | 10mg | Available within 8-12 weeks(?) Production requires sourcing of materials. We appreciate your patience and understanding. | $2,239.90 |
Purity>95% (SDS-PAGE&SEC); Endotoxin Level<1.0EU/mg; Human IgG1; CHO; ELISA, FACS, Functional assay, Animal Model; Unconjugated
Product Name | Lampalizumab (anti-Complement Factor D) - Primary antibody, specific to CFD, >95%, high purity, Human IgG1 |
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Synonyms | Adipsin antibody | Adipsin/complement factor D antibody | Adn antibody | C3 convertase activator antibody | CFAD_HUMAN antibody | CFD antibody | Complement factor D antibody | complement factor D preproprotein antibody | D component of complement antibody |
Specifications & Purity | Carrier Free, Recombinant, ExactAb™, Low Endotoxin, Azide Free, Validated, ≥95%(SDS-PAGE&SEC-HPLC), See COA |
Host species | Human |
Specificity | CFD |
Conjugation | Unconjugated |
Grade | Azide Free, Carrier Free, ExactAb™, Low Endotoxin, Recombinant, Validated |
Action Type | INHIBITOR |
Mechanism of action | Antibody of complement factor D |
Product Description | Lampalizumab (anti-Complement Factor D) is a humanised monoclonal antibody targeting complement Factor D in the alternative complement pathway. Lampalizumab (anti-Complement Factor D) binds an exosite and sterically blocks Factor B access to the active site. Lampalizumab (anti-Complement Factor D) can be used for age-related macular degeneration (AMD) research. |
Isotype | Human IgG1 |
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Light Chain Type | kappa |
SDS-PAGE | 25.7 kDa (Light Chain) & 50.8 kDa (Heavy Chain), under reducing conditions; 180.0 kDa, under non-reducing conditions. |
Purification Method | Protein A purified |
Purity | >95% |
Form | Liquid |
Concentration | See COA |
Storage Temp | Store at -80°C,Avoid repeated freezing and thawing |
Shipped In | Ice chest + Ice pads |
Stability And Storage | Store at -80℃ for 24 months. Upon delivery aliquot. Avoid freeze/thaw cycle. |
CAS | 1278466-20-8 |
Lampalizumab (anti-Complement Factor D) (Ab175571) - SEC
The purity of Lampalizumab (anti-Complement Factor D) (Ab175571) is more than 95% verified by HPLC.
Activity Type | Activity Value -log(M) | Mechanism of Action | Activity Reference | Publications (PubMed IDs) |
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Mechanism of Action | Action Type | target ID | Target Name | Target Type | Target Organism | Binding Site Name | References |
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Complement factor D inhibitor | INHIBITOR | ALA2176771 | Complement factor D | SINGLE PROTEIN | Homo sapiens | ||
Complement factor D inhibitor | INHIBITOR | ALA2176771 | Complement factor D | SINGLE PROTEIN | Homo sapiens |
Find and download the COA for your product by matching the lot number on the packaging.
3 results found
Lot Number | Certificate Type | Date | Item |
---|---|---|---|
ZJ24F0405069 | Certificate of Analysis | Apr 30, 2024 | Ab175571 |
ZJ24F0405068 | Certificate of Analysis | Apr 30, 2024 | Ab175571 |
ZJ24F0405067 | Certificate of Analysis | Apr 30, 2024 | Ab175571 |
1. Tanhehco EJ, Kilgore KS, Liff DA, Murphy KL, Fung MS, Sun WN, Sun C, Lucchesi BR. (1999) The anti-factor D antibody, MAb 166-32, inhibits the alternative pathway of the human complement system.. Transplant Proc, 31 (5): (2168-71). [PMID:10456004] [10.1021/op500134e] |
2. Fung M, Loubser PG, Undar A, Mueller M, Sun C, Sun WN, Vaughn WK, Fraser Jr CD. (2001) Inhibition of complement, neutrophil, and platelet activation by an anti-factor D monoclonal antibody in simulated cardiopulmonary bypass circuits.. J Thorac Cardiovasc Surg, 122 (1): (113-22). [PMID:11436043] [10.1021/op500134e] |
3. Charbel Issa P, Chong NV, Scholl HP. (2011) The significance of the complement system for the pathogenesis of age-related macular degeneration - current evidence and translation into clinical application.. Graefes Arch Clin Exp Ophthalmol, 249 (2): (163-74). [PMID:21127893] [10.1021/op500134e] |
4. Do DV, Pieramici DJ, van Lookeren Campagne M, Beres T, Friesenhahn M, Zhang Y, Strauss EC, Phase Ia Investigators. (2014) A phase ia dose-escalation study of the anti-factor D monoclonal antibody fragment FCFD4514S in patients with geographic atrophy.. Retina (Philadelphia, PA), 34 (2): (313-20). [PMID:23842100] [10.1021/op500134e] |
5. Yang CY, Phillips JG, Stuckey JA, Bai L, Sun H, Delproposto J, Brown WC, Chinnaswamy K.. (2016) Buried Hydrogen Bond Interactions Contribute to the High Potency of Complement Factor D Inhibitors.. ACS Med Chem Lett, 7 (12): (1092-1096). [PMID:27994744] [10.1021/acsmedchemlett.6b00299] |
6. Vulpetti A, Randl S, Rüdisser S, Ostermann N, Erbel P, Mac Sweeney A, Zoller T, Salem B, Gerhartz B, Cumin F, Hommel U, Dalvit C, Lorthiois E, Maibaum J.. (2017) Structure-Based Library Design and Fragment Screening for the Identification of Reversible Complement Factor D Protease Inhibitors.. J Med Chem, 60 (5): (1946-1958). [PMID:28157311] [10.1021/acs.jmedchem.6b01684] |
7. Velcicky J,Wilcken R,Cotesta S,Janser P,Schlapbach A,Wagner T,Piechon P,Villard F,Bouhelal R,Piller F,Harlfinger S,Stringer R,Fehlmann D,Kaupmann K,Littlewood-Evans A,Haffke M,Gommermann N. (2020) Discovery and Optimization of Novel SUCNR1 Inhibitors: Design of Zwitterionic Derivatives with a Salt Bridge for the Improvement of Oral Exposure.. J Med Chem, 63 (17): (9856-9875). [PMID:32856916] [10.1021/acs.jmedchem.0c01020] |
8. White, R T RT and 7 more authors.. (1992) Human adipsin is identical to complement factor D and is expressed at high levels in adipose tissue.. The Journal of biological chemistry, (5): [PMID:1374388] |
9. Johnson, D M DM, Gagnon, J J and Reid, K B KB.. (1984) Amino acid sequence of human factor D of the complement system. Similarity in sequence between factor D and proteases of non-plasma origin.. FEBS letters, (30): [PMID:6363133] |
10. Niemann, M A MA, Bhown, A S AS, Bennett, J C JC and Volanakis, J E JE.. (1984) Amino acid sequence of human D of the alternative complement pathway.. Biochemistry, (22): [PMID:6383466] |
11. and Davis, A E AE.. (1980) Active site amino acid sequence of human factor D.. Proceedings of the National Academy of Sciences of the United States of America, [PMID:6776531] |
12. Johnson, D M DM, Gagnon, J J and Reid, K B KB.. (1980) Factor D of the alternative pathway of human complement. Purification, alignment and N-terminal amino acid sequences of the major cyanogen bromide fragments, and localization of the serine residue at the active site.. The Biochemical journal, (1): [PMID:6821372] |
13. Volanakis, J E JE, Bhown, A A, Bennett, J C JC and Mole, J E JE.. (1980) Partial amino acid sequence of human factor D:homology with serine proteases.. Proceedings of the National Academy of Sciences of the United States of America, [PMID:6987665] |
14. Kim, S S, Narayana, S V SV and Volanakis, J E JE.. (1995) Crystal structure of a complement factor D mutant expressing enhanced catalytic activity.. The Journal of biological chemistry, (13): [PMID:7592653] |
15. Narayana, S V SV and 8 more authors.. (1994) Structure of human factor D. A complement system protein at 2.0 A resolution.. Journal of molecular biology, (14): [PMID:8289289] |
16. Sprong, Tom T and 6 more authors.. (2006) Deficient alternative complement pathway activation due to factor D deficiency by 2 novel mutations in the complement factor D gene in a family with meningococcal infections.. Blood, (15): [PMID:16527897] |
17. Maibaum, Jürgen J and 28 more authors.. (2016) Small-molecule factor D inhibitors targeting the alternative complement pathway.. Nature chemical biology, [PMID:27775713] |