IMP-1521

CFH

Recombinant C-terminal segment of CFH isoform a (NP_000177.2), corresponding to amino acid (Ser 860-Arg 1231) was expressed, fused with a polyhistidine tag at the C-terminus and a signal peptide at the N-terminus.

Complement factor H, also known as H factor 1, and CFH, is a sialic acid containing glycoprotein that plays an integral role in the regulation of the complement-mediated immune system that is involved in microbial defense, immune complex processing, and programmed cell death. Factor H protects host cells from injury resulting from unrestrained complement activation. CFH regulates complement activation on self cells by possessing both cofactor activity for the Factor I mediated C3b cleavage, and decay accelerating activity against the alternative pathway C3 convertase, C3bBb. CFH protects self cells from complement activation but not bacteria/viruses. Due to the central role that CFH plays in the regulation of complement, there are many clinical implications arrising from aberrant CFH activity. Mutations in the Factor H gene are associated with severe and diverse diseases including the rare renal disorders hemolytic uremic syndrome (HUS) and membranoproliferative glomerulonephritis (MPGN) also termed dense deposit disease (DDD), membranoproliferative glomuleronephritis type II or dense deposit disease, as well as the more frequent retinal disease age related macular degeneration (AMD). In addition to its complement regulatory activities, factor H has multiple physiological activities and 1) acts as an extracellular matrix component, 2) binds to cellular receptors of the integrin type, and 3) interacts with a wide selection of ligands, such as the C-reactive protein, thrombospondin, bone sialoprotein, osteopontin, and heparin.

HEK293

Human

C-His

Ser 860

Lyophilized from sterile PBS, pH 7.4, 5 % trehalose, 5% mannitol and 0.01% Tween80.

The recombinant human CFH consists of 383 amino acids and has a calculated molecular mass of 43 kDa. The apparent molecular mass of rh CFH is approximately 55-60 kDa in SDS-PAGE under reducing conditions due to glycosylation.

Ser860-Arg1231

< 1.0 EU/μg protein as determined by the LAL method.

> 95 % as determined by SDS-PAGE

Samples are stable for up to twelve months from date of receipt at -20 to -80 centigrade.
Store it under sterile conditions at -20 to -80 centigrade. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.