|Detection of Human Serpin E1/PAI‑1 by Western Blot. Western blot shows lysates of HUVEC human umbilical vein endothelial cells. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human Serpin E1/PAI‑1 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1786) followed by Streptavidin-HRP (Catalog # DY998) in 3% BSA. A specific band was detected for Serpin E1/PAI‑1 at approximately 48 kDa (as indicated). This experiment was conducted under reducing conditions.|
As a member of the Serpin superfamily of serine protease inhibitors, Serpin E1/PAI-1 is the principle 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).
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