Product Pathways - Adhesion
PAI-1 (D9C4) Rabbit mAb #11907
|W IP||H M R Mk B||Endogenous||48||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat Mk=Monkey B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
PAI-1 (D9C4) Rabbit mAb recognizes endogenous levels of total PAI-1 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg294 of human PAI-1 protein.
Western blot analysis of extracts from COS-7 and HUVEC cells using PAI-1 (D9C4) Rabbit mAb.
PAI-1 is a secreted protein that belongs to the serine proteinase inhibitor (serpin) superfamily. It inhibits urokinase and tissue plasminogen activators (uPA and tPA) and thus, reduces the conversion of inactive plasminogen to plasmin (1). PAI-1 regulates fibrinolysis and plays an important role in vessel patency and tissue remodeling. Secreted PAI-1 interacts with the extracellular matrix (ECM) component vitronectin, thereby modulating cell-ECM interactions (2,3). PAI-1 is expressed in a variety of tissues with higher expression in liver, vascular endothelial cells, platelets, macrophages, and adipose tissue (1). Increased levels of PAI-1 are associated with deep vein thrombosis (4). Defects in PAI-1 cause plasminogen activator inhibitor-1 deficiency (PAI-1D), which is characterized by increased bleeding after injury or surgery (5). Research studies have shown that high levels of PAI-1 are associated with obesity, aging, insulin resistance, and type 2 diabetes (6-8). PAI-1 is transcriptionally regulated by TGF-β and mediates TGF-β-induced inhibition of cell migration and invasion in cancer cells (9). Studies have shown PAI-1 to be also involved in fibrosis (10).
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- Sigurdardottir, O. and Wiman, B. (1994) Biochim Biophys Acta 1208, 104-10.
- Konstantinides, S. et al. (2001) Circulation 103, 576-83.
- Baldwin, J.F. et al. (2012) J Vasc Surg 56, 1089-97.
- Fay, W.P. et al. (1997) Blood 90, 204-8.
- Pannacciulli, N. et al. (2002) Obes Res 10, 717-25.
- Juhan-Vague, I. et al. (1991) Diabetologia 34, 457-62.
- Hashimoto, Y. et al. (1987) Thromb Res 46, 625-33.
- Humbert, L. and Lebrun, J.J. (2012) Cell Signal , .
- Zhang, L.P. et al. (1999) J Hepatol 31, 703-11.
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For Research Use Only. Not For Use In Diagnostic Procedures.