SERPINA5 Human

The SERPINA5 gene is located on chromosome 14q32.13 and consists of 5 exons spanning approximately 11.5 kb . The gene encodes a protein that is a single, non-glycosylated polypeptide chain containing 408 amino acids, with a molecular mass of 45.9 kDa . The protein is produced in E. coli and is often fused with a 20 amino acid His tag at the N-terminus for purification purposes .

SERPINA5 acts as a heparin-dependent serine protease inhibitor, inactivating serine proteases by binding irreversibly to their serine activation site . It is involved in the regulation of both intravascular and extravascular proteolytic activities, playing significant hemostatic roles in blood plasma . Additionally, it is known to inhibit plasminogen activators, which are involved in fibrinolysis .

The SERPINA5 protein shares a high degree of homology with other members of the serpin superfamily, including alpha-1-antichymotrypsin, alpha-1-antitrypsin, antithrombin III, and angiotensinogen . This homology suggests a common evolutionary origin for these proteins.

Deficiency or dysfunction of SERPINA5 can lead to various clinical conditions. For instance, it was once thought to be the cause of combined deficiency of coagulation factors V and VIII, although this was later disproved . The protein’s role in inhibiting proteases makes it a potential target for therapeutic interventions in disorders involving excessive proteolytic activity.

Human recombinant SERPINA5 is produced using E. coli expression systems. The recombinant protein is purified using proprietary chromatographic techniques to achieve a purity greater than 90% as determined by SDS-PAGE . The protein is typically formulated in a sterile filtered colorless solution containing Tris-HCl buffer, DTT, and glycerol for stability .