>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
43.2 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
64 kDa, reducing conditions
Publications
Read Publication using 4999-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 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Tris and NaCl.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 400 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Complement Factor H Protein, 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
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).
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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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