Complement C1r, Human, Activated, Two-Chain Form

Native, human, activated, C1r complement component. Generally the non-activated form composed of a single-chain glycoprotein. Present in normal human serum at 34 µg/ml. Non-activated C1r is found in circulating blood plasma as a dimer that associates with one C1q molecule and two C1s molecules to form the first component of complement (C1). Ensuing C1q binding to classical complement pathway activators, each C1r proenzyme monomer is activated by cleavage into two disulfide-linked fragments of M.W. 60,000 and 35,000. The 35 kDa peptide contains C1r enzymatic active site. Activated C1r continues activation via classical pathway by cleaving, and thus activating C1s.

Native, human, activated, C1r complement component. Generally, non-activated form composed of a single-chain glycoprotein. Present in normal human serum at 34 µg/ml. Non-activated C1r is found in circulating blood plasma as a dimer that associates with one C1q molecule and two C1s molecules to form the first component of complement (C1). Ensuing C1q binding to the classical complement pathway activators, each C1r proenzyme monomer is activated by cleavage into two disulfide-linked fragments of M.W. 60,000 and 35,000. The 35,000 peptide contains C1r enzymatic active site. Activated C1r continues activation via the classical pathway by cleaving, and thus activating C1s.

≥80% of C1r will bind with excess C1-INH

Please refer to vial label for lot-specific concentration.

Toxicity: Standard Handling (A)

In 140 mM NaCl, 10 mM imidazole, 2 mM EDTA, pH 7.4.

Prepared from serum that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.

Following initial thaw, aliquot and freeze (-70°C).

Villiers, C.L., et al. 1983. Biochem. J. 215, 369.
Ziccardi, R.J. and Cooper, N.R. 1976. J. Immunol. 116, 496.

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