SERPINE1 Human
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Description
SERPINE1 Human Recombinant fused to an N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 400 amino acids (24-402) and having a molecular mass of 45kDa.
SERPINE1 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Plasminogen activator inhibitor-1 (PAI-1) is a key regulator of fibrinolysis, the process of breaking down blood clots. It acts by inhibiting tissue plasminogen activator (tPA) and urokinase plasminogen activator (uPA), which are enzymes that convert plasminogen to plasmin. Plasmin is responsible for degrading fibrin, the main component of blood clots. PAI-1 belongs to a family of proteins called serpins (serine protease inhibitors), specifically SERPINE1. While another PAI, plasminogen activator inhibitor-2 (PAI-2), is mainly present during pregnancy, SERPINE1 is the primary inhibitor of plasminogen activators in the body.
This recombinant SERPINE1 protein is produced in E. coli and designed for research purposes. It is a single, non-glycosylated polypeptide chain consisting of 400 amino acids (residues 24-402) with a molecular weight of 45 kDa. A 21 amino acid His-Tag is fused to the N-terminus to facilitate purification, which is achieved using proprietary chromatographic techniques.
The protein is supplied in a buffer containing 50mM Sodium Acetate (pH 5.5), 10% glycerol, and 0.1M Sodium Chloride.
The protein exhibits potent inhibitory activity against uPA, as evidenced by an IC50 value of less than 3nM. This measurement is based on the protein's ability to block uPA-mediated cleavage of the substrate Z-GGRAMC.
MGSSHHHHHH SSGLVPRGSH MVHHPPSYVA HLASDFGVRV FQQVAQASKD RNVVFSPYGVASVLAMLQLT TGGETQQQIQ AAMGFKIDDK GMAPALRHLY KELMGPWNKD EISTTDAIFVQRDLKLVQGF MPHFFRLFRS TVKQVDFSEV ERARFIINDW VKTHTKGMIS NLLGKGAVDQLTRLVLVNAL YFNGQWKTPF PDSSTHRRLF HKSDGSTVSV PMMAQTNKFN YTEFTTPDGHYYDILELPYH GDTLSMFIAA PYEKEVPLSA LTNILSAQLI SHWKGNMTRL PRLLVLPKFSLETEVDLRKP LENLGMTDMF RQFQADFTSL SDQEPLHVAQ ALQKVKIEVN ESGTVASSSTAVIVSARMAP EEIIMDRPFL FVVRHNPTGT VLFMGQVMEP.
Product Science Overview
The gene encoding PAI-1, known as SERPINE1, is located on chromosome 7 (7q21.3-q22) in humans . PAI-1 is a single-chain glycoprotein with a molecular weight of approximately 43 kDa . It acts as a “bait” for tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA), which are key enzymes in the conversion of plasminogen to plasmin . Plasmin is the principal enzyme responsible for the degradation of fibrin, a major component of blood clots .
PAI-1 functions by inhibiting the activity of tPA and uPA, thereby preventing the formation of plasmin and subsequently inhibiting fibrinolysis . This inhibition is achieved through active site binding, where PAI-1 forms a stable complex with tPA or uPA, rendering them inactive . Additionally, PAI-1 can bind to the uPA/uPA receptor complex, leading to its degradation .
Elevated levels of PAI-1 are associated with an increased risk of thrombosis and atherosclerosis, as excessive inhibition of fibrinolysis can lead to the persistence of blood clots . Conversely, congenital deficiency of PAI-1 can result in a hemorrhagic diathesis, a condition characterized by an increased tendency to bleed due to insufficient suppression of fibrinolysis .
PAI-1 has also been implicated in various other physiological and pathological processes, including wound healing, organ fibrosis, aging, autophagy, immune responses, tumor invasion, and metastasis . Elevated PAI-1 levels are often observed in conditions such as insulin resistance, metabolic syndrome, and diabetes, making it a valuable biomarker for cardiovascular health and endothelial function .
Human recombinant PAI-1 is a laboratory-produced form of the protein that is used in various research and clinical applications. It is synthesized using recombinant DNA technology, which involves inserting the human SERPINE1 gene into a suitable expression system, such as bacteria or mammalian cells, to produce the protein in large quantities . Recombinant PAI-1 is used as a marker for acute myocardial infarction and in the diagnosis of several thrombolytic disorders . It also protects platelets against the inhibitory effects of plasma and has a role complementary to that of α2-antiplasmin .
