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204860 Complement C3b, Human

204860
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Prix & Disponibilité

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204860-250UG
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      Ampoule plast. 250 μg
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      Description
      OverviewNative, human C3b complement component. Cleavage of the C3-α chain at peptide bond 77 by either of the complement C3 convertase enzymes results in production of C3a (M.W. 9083) and C3b (M.W. 180,000) fragments. The C3b fragment is a glycoprotein composed of the modified C3-α chain (α′) (M.W. 105,000) and the intact C3-β chain (M.W. 75,000). Nascent C3b has the transient ability to form a covalent ester bond with a variety of target surfaces. Once bound to target surfaces C3b becomes an essential subunit of both the classical and alternative pathway C5 cleaving enzymes. In addition, surface-bound C3b has opsonic and immune adherence activities which are mediated via binding to CR1 (CD35) complement receptors.
      Catalogue Number204860
      Brand Family Calbiochem®
      References
      ReferencesWong, W.W. and Fearon, D.T. 1987. Methods Enzymol. 150, 579.
      Arnout, M.A., et al. 1981. J. Immunol. 127, 1348.
      Product Information
      FormLiquid
      FormulationIn PBS, pH 7.2, filtered through a 0.22 µm filter.
      Quality LevelMQ100
      Applications
      Biological Information
      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.
      Physicochemical Information
      ContaminantsIgG, IgA, IgM, C5, Factor H, or Factor I: ≤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 C3b, Human FDS

      Titre

      Fiche de données de sécurité des matériaux (FDS) 

      Complement C3b, Human Certificats d'analyse

      TitreNuméro de lot
      204860

      Références bibliographiques

      Aperçu de la référence bibliographique
      Wong, W.W. and Fearon, D.T. 1987. Methods Enzymol. 150, 579.
      Arnout, M.A., et al. 1981. J. Immunol. 127, 1348.
      Fiche technique

      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 C3b complement component. Cleavage of the C3-α chain at peptide bond 77 by either of the complement C3 convertase enzymes results in production of C3a (M.W. 9083) and C3b (M.W. 180,000) fragments. The C3b fragment is a glycoprotein composed of the modified C3-α chain (α') (M.W. 105,000) and the intact C3-β chain (M.W. 75,000). Nascent C3b has the transient ability to form a covalent ester bond with a variety of target surfaces. Once bound to target surfaces C3b becomes an essential subunit of both the classical and alternative pathway C5 cleaving enzymes. In addition, surface-bound C3b has opsonic and immune adherence activities which are mediated via binding to CR1 (CD35) complement receptors.
      FormLiquid
      FormulationIn PBS, pH 7.2, filtered through a 0.22 µm filter.
      SourcePrepared from serum that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
      Purity≥90% by SDS-PAGE
      ContaminantsIgG, IgA, IgM, C5, Factor H, or Factor I: ≤trace amounts
      Storage ≤ -70°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
      Toxicity Standard Handling
      ReferencesWong, W.W. and Fearon, D.T. 1987. Methods Enzymol. 150, 579.
      Arnout, M.A., et al. 1981. J. Immunol. 127, 1348.