Native, human, activated C1s complement component. Present in human serum at 31 µg/ml. Nonactivated C1s is found in circulating blood plasma as a Ca2+-dependent dimer in association with one C1q molecule and two C1r molecules to form the first component of complement (C1). Ensuing C1q binding to classical complement pathway activators, each C1r protein is cleaved to form activated C1r enzyme. Dimeric C1r enzyme cleaves, and thus activates, each C1s molecule into two disulfide-linked fragments of M.W. 59 kDa and 28 kDa. The 28 kDa peptide contains the C1s enzymatic active site. Activated C1s continues activation via classical pathway by cleaving, and thus activating, C2 and C4.
| Product information | |||
|---|---|---|---|
| Form | Liquid | ||
| Formulation | In 130 mM NaCl, 50 mM sodium phosphate, pH 7.2. | ||
| Molar mass | 87000 | ||
| Avoid freeze/thaw | Yes | ||
| Purity | ≥95% by SDS-PAGE | ||
| Source | Prepared from serum that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV. | ||
| CAS number | 80295-35-8 | ||
| Store and ship information | |||
|---|---|---|---|
| Storage | ≤ -70°C | ||
| Ship |
Dry Ice Only
Standard Handling |
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