SRP6317
C1 Esterase inhibitor from human plasma
≥95% (SDS-PAGE)
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Synonym(s):
C1-inhibiting factor, Complement C1 esterase inhibitor, Esterase inhibitor C-1, Plasma protease C1 inhibitor, Serpin G1
UNSPSC Code:
12352204
NACRES:
NA.32
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biological source
human
Assay
≥95% (SDS-PAGE)
form
frozen liquid
mol wt
100 kDa
packaging
pkg of 1 mg
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... Serpin G1(710)
General description
C1 esterase inhibitor is a single chain glycoprotein which inhibits C1, C1r, C1s, plasma kallikrein, factors XIa, XIIa and plasmin of the blood clotting system. It is present in the plasma at 16-33 mg/100mL. It is part of the serpin family.
Biochem/physiol Actions
C1 esterase inhibitor functions as a serine proteinase inhibitor. The concentration of C1 esterase inhibitor protein is reduced to 10-30% of normal in patients with angioedema secondary to C1 esterase inhibitor deficiency (85% of patients with Hereditary Angioedema (HAE)); in 15% of patients with HAE, the concentrations of the inhibitor protein is normal but function is markedly reduced. C1 esterase inhibitor deficiency is a rare condition resulting in facial swelling and abdominal cramping. Usually the condition is hereditary, though it may also occur when the protein is non-functional. C1 esterase inhibitor deficiencies also disturb the fibrinolytic system, the intrinsic coagulation pathway and the complement pathway.
Physical form
Frozen in 20 mM potassium phosphate, pH 7.0, with 250 mM KCl.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
监管及禁止进口产品
Certificates of Analysis (COA)
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In vivo biosynthesis of endogenous and of human C1 inhibitor in transgenic mice: tissue distribution and colocalization of their expression.
Vinci G
Journal of Immunology, 169(10), 5948-5954 (2002)
Ruby H P Law et al.
Genome biology, 7(5), 216-216 (2006-06-02)
Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways. Serpins are conformationally labile and many of the
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