Complement 5a (C5a) is an enzymatically generated glycoprotein belonging to the anaphylatoxin family of structurally and functionally related proteins. Generated upon the activation of the complement system, C5a, together with C4a, C3a, and the membrane attack complex (C5b‐9), functions as a central player in host defense by inducing smooth muscle cell contraction, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes through cell degranulation. In addition to acting as a direct mediator of localized inflammatory response, C5a also initiates both the synthesis and release of IL‐8 from monocytes and bronchial epithelial cells, stimulates the proliferation of neurons and hepatocytes, and functions as a potent chemoattractant. Where C5a deficiency, a rare defect of the complement pathway caused by the mutation of the C5a gene, is associated with susceptibility to severe infections, excessive C5a activation has been linked to liver fibrosis, sepsis, adult respiratory distress syndrome, rheumatoid arthritis, Alzheimer’s disease, and ischemic heart disease. Human C5a shares 60% and 54% sequence identity to mouse and rat C5a, respectively. The human C5 gene encodes a 1,676 amino acid glycoprotein that is comprised of a disulfide‐linked C5 alpha and a C5 beta chain, the former of which contains the active, 74 amino acid C5a anaphylatoxin chain. Recombinant Murine C5a is an 8.9 kDa glycoprotein containing the 77 amino acid residues of the C5a anaphylatoxin chain.
Complement Component 5a, Complement 5a, CPAMD4, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4
NLHLLRQKIE EQAAKYKHSV PKKCCYDGAR VNFYETCEER VARVTIGPLC IRAFNECCTI ANKIRKESPH KPVQLGR
Calculated Molecular Weight:
≥ 98% by SDS-PAGE gel and HPLC analyses.
Measured by its ability to support adhesion of Human Umbilical Vein Endothelial Cells (HUVEC) to the Recombinant Murine C5a-coated surface.