|Detection of Human Serpin E1/PAI‑1 by Western Blot. Western blot shows lysates of HUVEC human umbilical vein endothelial cells and HepG2 human hepatocellular carcinoma cell line. PVDF membrane was probed with 1:1000 dilution of Rabbit Anti-Human Serpin E1/PAI‑1 Monoclonal Antibody (Catalog # MAB17861) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for Serpin E1/PAI‑1 at approximately 48 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
|Detection of Human Serpin E1/PAI‑1 by Simple WesternTM. Simple Western lane view shows lysates of HUVEC human umbilical vein endothelial cells, loaded at 0.2 mg/mL. A specific band was detected for Serpin E1/PAI‑1 at approximately 55 kDa (as indicated) using 1:100 dilution of Rabbit Anti-Human Serpin E1/PAI‑1 Monoclonal Antibody (Catalog # MAB17861). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.|
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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