Recombinant Human Serpin E1/PAI-1 Protein, CF Summary
Details of Functionality
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 <13 nM, as measured under the described conditions.
Spodoptera frugiperda, Sf 21 (stably transfected)-derived human Serpin E1/PAI-1 protein Met1-Pro402, with a C-terminal 10-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
<1.0 EU per 1 μg of the protein by the LAL method.
44 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Serpin E1/PAI-1 Protein, CF
Endothelial plasminogen activator inhibitor
PLANH1plasminogen activator inhibitor 1
serine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogenactivator inhibitor type 1), member 1
serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitortype 1), member 1
As a member of the Serpin superfamily of serine protease inhibitors, Serpin E1/PAI‑1 is the principal inhibitor of urokinase‑type plasminogen activator (uPA) and tissue‑type PA (1, 2). As important regulators of extracellular matrix remodeling, uPA and PAI‑1 play a major role in many processes such as angiogenesis, tumor invasion and obesity (2‑4). For example, uPA and PAI-1 are the only tumor prognostic factors validated at the highest level of evidence with regard to their clinical utility in breast cancer (5). The human PAI-1 is initially synthesized as 402 amino acid precursor with a N‑terminal signal peptide (6, 7). PAI‑1 may exist in one of two possible conformations, designated as active or latent (8). The purified rhPAI‑1 is active against rhuPA. The heterogeneity at the N‑terminus of the purified rhPAI‑1 has been observed before for both the recombinant and native proteins (9).
Silverman, G.A. et al. (2001) J. Biol. Chem. 276:33293.
Stefansson, S. et al. (2003) Curr. Pharm. Des. 9:1545.
Duffy, M.J. (2002) Clin. Chem. 48:1194.
Juhan-Vague, I. et al. (2003) J. Thromb. Haemost. 1:1575.
Harbeck, N. et al. (2002) Clin. Breast Cancer 3:196.
Pannekoek, H. et al. (1986) EMBO J. 5:2539.
Ginsburg, D. et al. (1986) J. Clin. Invest. 78:1673.
Wang, Z. et al. (1996) Biochemistry 35:16443.
Stromqvist, M. et al. (1994) Protein Expr. Purif. 5:309.
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