234397 Complement C5a, His·Tag®, Human, Recombinant, E. coli

234397
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234397-100UG
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      Plastic ampoule 100 μg
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      Description
      OverviewRecombinant, human C5a complement (74 amino acids) fused at the N-terminus to a His•Tag® sequence and a proprietary vector sequence necessary for expression and expressed in E. coli. The recombinant protein is not further processed to remove the additional sequence. Activation of complement by either pathway results in the formation of C5-cleaving enzymes (C5 convertases) on target surfaces. The C5 convertase enzymes cleave the C5 α-chain at peptide bond 74 resulting in the production and release of the C5a glycopeptide. C5a is the most biologically active of the three complement-derived anaphylatoxins. C5a expresses a wide variety of biogical activities which include: inflammatory cell chemotaxis, smooth muscle contraction, and release reactions of neutrophils, mast cells, and macrophages.


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      Catalogue Number234397
      Brand Family Calbiochem®
      References
      ReferencesCarney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391.
      Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59.
      Product Information
      FormLyophilized solid
      Quality LevelMQ100
      Applications
      Biological Information
      Biological activityExhibits equal activity to that of serum-derived C5a based on a myeloperoxidase release assay.
      Purity≥95% by SDS-PAGE
      Physicochemical Information
      ContaminantsEndotoxins: ≤0.1 ng/µg protein
      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 reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 3 months at -70°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      Complement C5a, His·Tag®, Human, Recombinant, E. coli Certificates of Analysis

      TitleLot Number
      234397

      References

      Reference overview
      Carney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391.
      Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59.
      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.

      Revision22-May-2009 JSW
      DescriptionRecombinant, human C5 a complement (74 amino acids) fused at the N-terminus to a His•Tag® sequence and a proprietary vector sequence necessary for expression and expressed in E. coli. The recombinant protein is not further processed to remove the additional sequences. Activation of complement by either pathway results in the formation of C5-cleaving enzymes (C5 convertase) on target surfaces. The C5 convertase enzymes cleave the C5a chain at peptide bond 74, resulting in the production and release of the C5a glycopeptide. C5a is the most biologically active of the three complement-derived anaphylatoxins. C5a exhibits a wide variety of biological activities, including inflammatory cell chemotaxis, smooth muscle contraction, and degranulation of neutrophils, mast cells, and macrophages.
      FormLyophilized solid
      Purity≥95% by SDS-PAGE
      ContaminantsEndotoxins: ≤0.1 ng/µg protein
      Biological activityExhibits equal activity to that of serum-derived C5a based on a myeloperoxidase release assay.
      SolubilityReconstitute in sterile H₂O containing 2.5 mg/ml BSA.
      Storage ≤ -70°C
      Avoid freeze/thaw
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, aliquot and freeze (-70°C). Stock solutions are stable for up to 3 months at -70°C.
      Toxicity Standard Handling
      ReferencesCarney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391.
      Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59.