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204879 Complement C1s, Human, Activated, Two-Chain Form

204879
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
204879-250UG Plastic ampoule 250 μg
Description
OverviewNative, 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.
Catalogue Number204879
Brand Family Calbiochem®
References
ReferencesCooper, N.R. 1985. Adv. Immunol. 37, 151.
Sim, R.B. 1981. Methods Enzymol. 80, 6.
Product Information
CAS number80295-35-8
FormLiquid
FormulationIn 130 mM NaCl, 50 mM sodium phosphate, pH 7.2.
Quality LevelMQ100
Applications
Biological Information
Purity≥95% 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
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
Global Trade Item Number
Catalogue Number GTIN
204879-250UG 04055977219722

Documentation

Complement C1s, Human, Activated, Two-Chain Form SDS

Title

Safety Data Sheet (SDS) 

Complement C1s, Human, Activated, Two-Chain Form Certificates of Analysis

TitleLot Number
204879

References

Reference overview
Cooper, N.R. 1985. Adv. Immunol. 37, 151.
Sim, R.B. 1981. Methods Enzymol. 80, 6.

Citations

Title
  • Kerr, F.K., et al. 2005. Journal of Biological Chemistry 280, 39510.
  • 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 C1s complement component. Present in human serum at 31 µg/ml. Non-activated 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 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. 59,000 and 28,000. The 28,000 peptide contains the C1s enzymatic active site. Activated C1s continues activation via the classical pathway by cleaving, and thus activating, C2 and C4.
    FormLiquid
    FormulationIn 130 mM NaCl, 50 mM sodium phosphate, pH 7.2.
    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 number80295-35-8
    Purity≥95% by SDS-PAGE
    Storage Avoid freeze/thaw
    ≤ -70°C
    Do Not Freeze Ok to freeze
    Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
    Toxicity Standard Handling
    ReferencesCooper, N.R. 1985. Adv. Immunol. 37, 151.
    Sim, R.B. 1981. Methods Enzymol. 80, 6.
    Citation
  • Kerr, F.K., et al. 2005. Journal of Biological Chemistry 280, 39510.