Name : Human PAI-1 Protein

Product Source :
Recombinant Human PAI-1 Protein is expressed from HEK293 with His tag at the C-Terminus. It contains Val24-Pro402.[Accession | P05121-1]

Molecular Weight :
The protein has a predicted MW of 43.86 kDa. Due to glycosylation, the protein migrates to 45-55 kDa based on Tris-Bis PAGE result.

Endotoxin Level :
Less than 1EU per μg by the LAL method.

Purity :
> 95% as determined by Tris-Bis PAGE> 95% as determined by HPLC

Formulation :
Lyophilized from 0.22 μm filtered solution in 50mM NaAC, 0.1M NaCl, 100mM L-arginine (pH 5.5). Normally 8% trehalose is added as protectant before lyophilization.

Reconstitution :
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in 50mM NaAC, 0.1M NaCl, 100mM L-arginine (pH 5.5)..

Storage and Stability :
-20 to -80°C for 12 months as supplied from date of receipt.-80°C for 3-6 months after reconstitution.2-8°C for 2-7 days after reconstitution.Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.

Product Concentration :
Tris-Bis PAGE Human PAI-1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. SEC-HPLC The purity of Human PAI-1 is greater than 95% as determined by SEC-HPLC. Bioactivity Data Measured by its ability to inhibit uPA cleavage of a peptide substrate, N-carbobenzyloxy-Gly-Gly-Arg-7-amido-4-methylcoumarin (Z-GGR-AMC). The IC50 value is

Background :
PAI-1 (plasminogen activator inhibitor-1) is a member of plasminogen cascade with an inhibitory role in plasmin activation. PAI-1 is an important regulator of the fibrinolytic process and levels of this antifibrinolytic protein are elevated in diabetes and insulin resistant states.

Synonyms :
PAI; PAI-1; Serpin E1; SERPINE1; PAI1; PLANH1

References & Citations :
(1) Wyrzykowska P, Kasza A. Regulacja ekspresji genu PAI-1 [Regulation of PAI-1 expression]. Postepy Biochem. 2009;55(1):46-53. Polish. PMID: 19514465.

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