Anti-C5/C5a Antibody Picoband® Fluoro488 Conjugated

C5a is a protein fragment released from complement component C5. This gene is mapped to 9q33.2. The protein encoded by this gene is the fifth component of complement, which plays an important role in inflammatory and cell killing processes. This protein is comprised of alpha and beta polypeptide chains that are linked by a disulfide bridge. An activation peptide, C5a, which is an anaphylatoxin that possesses potent spasmogenic and chemotactic activity, is derived from the alpha polypeptide via cleavage with a convertase. C5a plays a key role in increasing migration and adherence of neutrophils and monocytes to vessel walls. Mutations in this gene cause complement component 5 deficiency, a disease where patients show a propensity for severe recurrent infections. Defects in this gene have also been linked to susceptibility to liver fibrosis and to rheumatoid arthritis.

E.coli-derived rat C5a recombinant protein (Position: D1-R77) . Rat C5a shares 62% and 82% amino acid (aa) sequences identity with human and mouse C5a, respectively.

Expressed in normal hepatocytes as well as in epithelial cells lining the stomach, the small and the large intestine. Found also in basal keratinocytes of esophagus and skin. High levels are found in liver, gastrointestinal tract, thyroid and kidney. Also present in the brain. .

Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and s their migration toward sites of inflammation. .

1. Delgado-Cervino, E., Fontan, G., Lopez-Trascara, M. C5 complement deficiency in a Spanish family: molecular characterization of the double mutation responsible for the defect. Molec. Immun. 42: 105-111, 2005. 2. Pfarr, N., Prawitt, D., Kirschfink, M., Schroff, C., Knuf, M., Habermehl, P., Mannhardt, W., Zepp, F., Fairbrother, W. G., Loos, M., Burge, C. B., Pohlenz, J. Linking C5 deficiency to an exonic splicer enhancer mutation. J. Immun. 174: 4172-4177, 2005. Note: Erratum: J. Immun. 182: 5152 only, 2009.