PAI-1 Antibody #27535
Filter:
- WB
Supporting Data
| REACTIVITY | M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 50 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
PAI-1 Antibody recognizes endogenous levels of total PAI-1 protein.
Species Reactivity:
Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly196 of murine PAI-1 protein. Antibodies are purified by peptide affinity chromatography.
Background
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 also shown PAI-1 to be involved in fibrosis (10).
- Pannekoek, H. et al. (1986) EMBO J 5, 2539-44.
- 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 25, 490-500.
- Zhang, L.P. et al. (1999) J Hepatol 31, 703-11.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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