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| Replacement Information |
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| Description | |
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| Overview | Recombinant, 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. |
| Available in Bulk - request a quote! | |
| Catalogue Number | 234397 |
| Brand Family | Calbiochem® |
| References | |
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| References | Carney, D.F. and Hugli, T.E. 1993. Protein Sci. 2, 1391. Hugli, T.E., et al. 1981. Mol. Cell. Biochem. 41, 59. |
| Product Information | |
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| Form | Lyophilized solid |
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| Biological Information | |
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| Biological activity | Exhibits equal activity to that of serum-derived C5a based on a myeloperoxidase release assay. |
| Purity | ≥95% by SDS-PAGE |
| Physicochemical Information | |
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| Contaminants | Endotoxins: ≤0.1 ng/µg protein |
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