Complement C3 (beta chain) Mouse Monoclonal Antibody [11-10]

Function

Human Complement C3 (C3) is synthesized as a single-chain pro-molecule (185 kDa) that tsuffers several posttranslational modifications. Before being a mature protein, C3 is split into beta-chain (70 kDa) and alpha chain (115 kDa) and forms a rare internal thioester bond. C3 plays a central role in the activation of the complement system. It’s processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.

Background References

1. Hao W et al. Gut dysbiosis induces the development of depression-like behavior through abnormal synapse pruning in microglia-mediated by complement C3. Microbiome. 2024 Feb

2. Xu L et al. Inhibition of complement C3 signaling ameliorates locomotor and visual dysfunction in autoimmune inflammatory diseases. Mol Ther. 2023 Sep

Tissue Specificity

Plasma. The acylation stimulating protein (ASP) is expressed in adipocytes and released into the plasma during both the fasting and postprandial periods.

Post-translational Modification

C3b is rapidly split in two positions by factor I and a cofactor to form iC3b (inactivated C3b) and C3f which is released. Then iC3b is slowly cleaved (possibly by factor I) to form C3c (beta chain + alpha' chain fragment 1 + alpha' chain fragment 2), C3dg and C3f. Other proteases produce other fragments such as C3d or C3g. C3a is further processed by carboxypeptidases to release the C-terminal arginine residue generating the acylation stimulating protein (ASP). Levels of ASP are increased in adipocytes in the postprandial period and by insulin and dietary chylomicrons.; (Microbial infection) C3 is cleaved by Staphylococcus aureus aureolysin; this cleavage renders C3a and C3b inactive. C3b is rapidly degraded by host factors CFH and CFI preventing its deposition on the bacterial surface while C3a is further inactivated by aureolysin.; Phosphorylated by FAM20C in the extracellular medium.

Subcellular Location

Secreted

UNIPROT

SwissProt: P01024 Human

Synonyms