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

204879
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204879-250UG
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      Plastic ampoule 250 μg
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      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

      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 ≤ -70°C
      Avoid freeze/thaw
      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.