Recombinant Mouse Complement Factor H Protein, CF
Recombinant Mouse Complement Factor H Protein, CF Summary
The ED50 for this effect is 3-18 μg/mL in the presence of 50 ng/mL of rhTNF-alpha.
Ser875-Val1252, with a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.|
|Reconstitution||Reconstitute at 400 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: Complement Factor H
Factor H is a 155 kDa glycoprotein that provides critical negative regulation of the alternative pathway complement cascade. It is secreted by Kupffer cells, hepatocytes, vascular endothelial cells, and platelets and circulates in the serum at high concentration (1). Factor H is composed of 20 SCR (short consensus repeats), each of which consists of approximately 60 amino acids with four invariant Cys residues (2). Factor H interacts with cell surface polyanions including heparin and sialoglycoproteins (3 - 6), and immobilized Factor H supports the CD11b/CD18 integrin-dependent adhesion of neutrophils (7). It prevents local complement activation by sequestering complement component C3b, accelerating the decay of C3 and C5 convertases, and functioning as a cofactor for the C3b inactivator, Factor I (1, 3, 6, 8). This recombinant protein corresponds to SCR15-20 which encompass the primary binding sites for heparin and C3b as well as for the peptide hormone adrenomedullin (4, 9 - 11). Within SCR15-20, mouse Factor H shares 60% and 80% amino acid sequence identity with human and rat Factor H, respectively. Dozens of mutations clustered in SCR15-20 are associated with atypical hemolytic uremic syndrome, a disorder characterized by anemia, thrombocytopenia, and renal failure (12). Binding of Factor H to tumor cell-associated dentin matrix protein 1, bone sialoprotein, or osteopontin results in the protection of that cell from complement mediated lysis (13, 14). A variety of pathogenic microbes also express Factor H binding molecules that interfere with immune clearance of the infection (15).
- Schmidt, C.Q. et al. (2008) Clin. Exp. Immunol. 151:14.
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