| Form | Liquid |
|---|---|
| Host Species | Human |
| Clonality | Monoclonal |
| Isotype | IgG3, kappa |
| Purity | >95% as determined by SDS-PAGE. |
| Purification | Protein A/G purified from cell culture supernatant. |
| Endotoxin Level | Please contact with the lab for this information. |
| Applications | ELISA, IF, Bioactivity: FACS, Functional assay, Research in vivo |
| Species Reactivity | Homo sapiens (Human) |
| Target | CFH, Complement factor H, H factor 1, HF, HF1, HF2 |
| Storage Buffer | 0.01M PBS pH 7.4 |
| Stability and Storage | Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at -20 to -80°C for twelve months from the date of receipt. |
| Reconstitution | Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details. |
| Shipping Condition | In general, proteins are provided as lyophilized powder/frozen liquid. They are shipped out with dry ice/blue ice unless customers require otherwise. |
| Accession Number | P08603 |
| Background | Complement factor H (CFH) is a ~139 kDa protein. Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces. Accelerates the decay of the complement alternative pathway (AP) C3 convertase C3bBb, thus preventing local formation of more C3b, the central player of the complement amplification loop. As a cofactor of the serine protease factor I, CFH also regulates proteolytic degradation of already-deposited C3b. In addition, mediates several cellular responses through interaction with specific receptors. 1. Kajander, T. et al. (2011) Proceedings of the National Academy of Sciences of the United States of America 108, 2897-902. PMID: 21285368 2. Morgan, HP. et al. (2011) Nature structural & molecular biology 18, 463-70. PMID: 21317894 3. Blaum, BS. et al. (2015) Nature chemical biology 11, 77-82. PMID: 25402769 4. Wu, J. et al. (2009) Nature immunology 10, 728-33. PMID: 19503104 5. Kennedy, AT. et al. (2016) Journal of immunology (Baltimore, Md. : 1950) 196, 1239-48. PMID: 26700768 6. Hocking, HG. et al. (2008) The Journal of biological chemistry 283, 9475-87. PMID: 18252712 7. Simon, N. et al. (2013) Cell host & microbe 13, 29-41. PMID: 23332154 8. Xue, X. et al. (2017) Nature structural & molecular biology 24, 643-651. PMID: 28671664 9. Losse, J. et al. (2010) Journal of immunology (Baltimore, Md. : 1950) 184, 912-21. PMID: 20008295 10. DiScipio, RG. et al. (1998) Journal of immunology (Baltimore, Md. : 1950) 160, 4057-66. PMID: 9558116 |
| Note | For research use only |