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204878 Complement C1r, Human, Activated, Two-Chain Form

204878
Purchase on Sigma-Aldrich

Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
204878-250UG Plastic ampoule 250 μg
Description
OverviewNative, 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.
Catalogue Number204878
Brand Family Calbiochem®
References
ReferencesVilliers, C.L., et al. 1983. Biochem. J. 215, 369.
Ziccardi, R.J. and Cooper, N.R. 1976. J. Immunol. 116, 496.
Product Information
CAS number80295-34-7
FormLiquid
FormulationIn 140 mM NaCl, 10 mM imidazole, 2 mM EDTA, pH 7.4.
Quality LevelMQ100
Applications
Biological Information
Biological activity≥90% of C1r will bind with excess C1-INH
Purity≥90% by SDS-PAGE
SourcePrepared from serum that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
ContaminantsIgG, IgA, IgM, albumin, C1s, C4BP, C1-INH: ≤trace amounts
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications

Documentation

Complement C1r, Human, Activated, Two-Chain Form SDS

Title

Safety Data Sheet (SDS) 

Complement C1r, Human, Activated, Two-Chain Form Certificates of Analysis

TitleLot Number
204878

References

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

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision27-May-2008 RFH
DescriptionNative, 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.
FormLiquid
FormulationIn 140 mM NaCl, 10 mM imidazole, 2 mM EDTA, pH 7.4.
Concentration Label Please refer to vial label for lot-specific concentration
SourcePrepared from serum that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
CAS number80295-34-7
Purity≥90% by SDS-PAGE
ContaminantsIgG, IgA, IgM, albumin, C1s, C4BP, C1-INH: ≤trace amounts
Biological activity≥90% of C1r will bind with excess C1-INH
Storage ≤ -70°C
Avoid freeze/thaw
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesVilliers, C.L., et al. 1983. Biochem. J. 215, 369.
Ziccardi, R.J. and Cooper, N.R. 1976. J. Immunol. 116, 496.