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204860 Complement C3b, Human

Complement C3b, Human, is a native C3b complement component. It is a glycoprotein composed of the modified C3-α chain (αʹ) (M.W. 105,000) and the intact C3-β chain (M.W. 75,000).

Complement C3b, Human MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.
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204860
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Overview

Replacement Information

Products

Catalogue NumberPackaging Qty/Pack
204860-250UG Plastic ampoule 250 μg
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
Global Trade Item Number
Catalogue Number GTIN
204860-250UG 04055977219630

Documentation

Complement C3b, Human SDS

Title

Safety Data Sheet (SDS) 

Complement C3b, Human Certificates of Analysis

TitleLot Number
204860

References

Reference overview
Wong, W.W. and Fearon, D.T. 1987. Methods Enzymol. 150, 579.
Arnout, M.A., et al. 1981. J. Immunol. 127, 1348.
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 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 Avoid freeze/thaw
≤ -70°C
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.