The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Measured by its ability to inhibit recombinant human complement component C1a cleavage of a colorimetric peptide substrate, N Carbobenzyloxy-Lys- ThioBenzyl ester (Z-K-SBzl). The expected IC50 is ≤ 2.6 nM.
< 0.100 Eu/µg
>95% by SDS-PAGE .
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Preparation and Storage
Stability and Storage
Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Upon reconsitution add a carrier protein (0.1% BSA). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
C1 esterase inhibitor
C1 inhibiting factor
complement component 1 inhibitor
Plasma protease C1 inhibitor
Serine (or cysteine) proteinase inhibitor clade G member 1
serine/cysteine proteinase inhibitor clade G member 1
serpin peptidase inhibitor, clade G (C1 inhibitor), member 1
Activation of the C1 complex is under control of the C1-inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. Inhibits chymotrypsin and kallikrein.
Involvement in disease
Defects in SERPING1 are the cause of hereditary angioedema (HAE) [MIM:106100]; also called hereditary angioneurotic edema (HANE). HAE is an autosomal dominant disorder characterized by episodic local subcutaneous edema and submucosal edema involving the upper respiratory and gastrointestinal tracts. HAE due to C1 esterase inhibitor deficiency is comprised of two clinically indistinguishable forms. In HAE type 1, representing 85% of patients, serum levels of C1 esterase inhibitor are less than 35% of normal. In HAE type 2, the levels are normal or elevated, but the protein is non-functional.
Belongs to the serpin family.
Highly glycosylated (49%) with N- and O-glycosylation. Can be proteolytically cleaved by E.coli stcE.