>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
42.5 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
60-65 kDa, reducing conditions
Publications
Read Publication using 4779-FH in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Reconstitution Instructions
Reconstitute at 250 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Complement Factor H (aa 860-1231), CF
adrenomedullin binding protein
age-related maculopathy susceptibility 1
AHUS1
AMBP1
ARMD4
ARMS1
beta-1H
beta-1-H-globulin
beta-1-H-globulin
CFH
CFHL3
Complement Factor H
factor H
factor H-like 1
FH
FHL1
H factor 1 (complement)
H factor 1
H factor 2 (complement)
HF
HF1
HF1ARMS1
HF2
HUS
HUSMGC88246
Background
Complement Factor H is a 155 kDa glycoprotein that provides critical negative regulation to the alternative pathway of complement cascade. It is secreted by Kupffer cells, hepatocytes, vascular endothelial cells, and platelets, and circulates in the serum at high concentration (1). Complement Factor H is composed of 20 SCRs (short consensus repeats), each of which consists of approximately 60 amino acids with four invariant Cys residues (2). Alternate splicing generates an isoform that is truncated following SCR7. Complement Factor H interacts with cell surface polyanions including heparin and sialoglycoproteins (3 - 6), and immobilized Complement 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 functions as a cofactor for the C3b inactivator, Factor I (1, 3, 6, 8). The recombinant protein expressed here 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, human Complement Factor H shares 60% and 63% amino acid sequence identity with mouse and rat Complement 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 Complement 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 Complement Factor H binding molecules that interfere with immune clearance of the infection (15).
Schmidt, C.Q. et al. (2008) Clin. Exp. Immunol. 151:14.
Ripoche, J. et al. (1988) Biochem. J. 249:593.
Meri, S. and M.K. Pangburn (1990) Proc. Natl. Acad. Sci. 87:3982.
Jokiranta, T.S. et al. (2005) Am. J. Pathol. 167:1173.
Blackmore, T.K. et al. (1998) J. Immunol. 160:3342.
Hellwage, J. et al. (2002) J. Immunol. 169:6935.
DiScipio, R.G. et al. (1998) J. Immunol. 160:4057.
Sharma, A.K. and M.K. Pangburn (1996) Proc. Natl. Acad. Sci. 93:10996.
Oppermann, M. et al. (2006) Clin. Exp. Immunol. 144:342.
Pangburn, M.K. et al. (2000) J. Immunol. 164:4742.
Martinez, A. et al. (2003) Hypertens. Res. 26:S55.
de Cordoba, S.R. and E.G. de Jorge (2008) Clin. Exp. Immunol. 151:1.
Jain, A. et al. (2002) J. Biol. Chem. 277:13700.
Fedarko, N.S. et al. (2000) J. Biol. Chem. 275:16666.
Kraiczy, P. and R. Wurzner (2006) Mol. Immunol. 43:31.
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