SERPINA5 Human, Active
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
Description
SERPINA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (20-406 a.a) and having a molecular mass of 45.9kDa.
SERPINA5 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
SERPINA5, also known as Protein C inhibitor (PCI), plays a crucial role in regulating the balance between coagulation (blood clotting) and fibrinolysis (clot breakdown). It achieves this by inhibiting the activation of thrombin-activatable fibrinolysis inhibitor (TAFI) and Protein C. As a member of the serpin family, SERPINA5 inhibits plasminogen activators and activated Protein C. Found in plasma and the liver, SERPINA5 is implicated in various cellular processes such as inflammation, proliferation, apoptosis, and the migration, invasion, and metastasis of tumor cells. For instance, it regulates the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator. Furthermore, SERPINA5 plays a role in controlling key serine proteases involved in metastatic prostate disease.
Recombinant human SERPINA5, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 408 amino acids (with amino acids 20-406 present) and has a molecular weight of 45.9 kDa. The recombinant protein is purified using proprietary chromatographic techniques and contains a 21 amino acid His-tag at the N-terminus.
The SERPINA5 protein solution is provided at a concentration of 0.5 mg/ml and is formulated in a buffer containing 150 mM sodium chloride (NaCl), 10% glycerol, and 20 mM MES buffer at a pH of 6.0.
The biological activity of SERPINA5 is assessed by measuring its ability to inhibit the cleavage of the substrate Boc-VPR-AMC by thrombin. The IC50 value, which represents the concentration of SERPINA5 required to inhibit 50% of the thrombin activity, is less than or equal to 2 nM.
Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.
MGSSHHHHHH SSGLVPRGSH MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.
Product Science Overview
Serpin Peptidase Inhibitor, Clade A Member 5, also known as SERPINA5, is a significant member of the serpin superfamily. This family of proteins is primarily known for their role as serine protease inhibitors, which are crucial in regulating various physiological processes, including coagulation, inflammation, and immune responses .
SERPINA5 is a serine protease inhibitor that plays a pivotal role in maintaining the balance between coagulation and fibrinolysis. It achieves this by differentially inhibiting the activation of Thrombin-Activatable Fibrinolysis Inhibitor (TAFI) and Protein C . This protein is secreted in plasma and the liver, where it inhibits plasminogen activators as well as activated protein C .
The serpin family is notable for its unique mechanism of action. Unlike other protease inhibitors that competitively bind to the active site of proteases, serpins undergo a significant conformational change to irreversibly inhibit their target protease. This conformational change disrupts the active site of the protease, rendering it inactive .
SERPINA5 is involved in several critical biological processes. It is a key regulator in the coagulation cascade, ensuring that blood clotting occurs appropriately and preventing excessive bleeding or clotting. Additionally, it plays a role in the regulation of fibrinolysis, the process by which blood clots are broken down .
Mutations or deficiencies in SERPINA5 can lead to various clinical conditions. For instance, an imbalance in its activity can result in either excessive bleeding or thrombosis. Understanding the function and regulation of SERPINA5 is therefore crucial for developing therapeutic strategies for related disorders .
