Search results for: Proteins and Antibodies Human and Animal Rabbit Anti Human uPA IgG Fraction
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Characterization of urokinase-type plasminogen activator of rat decidual tissue.
Urokinase-type plasminogen activator (uPA) from artificially induced decidual tissue of rat has been purified to homogeneity employing chromatographic techniques and the final preparation has a specific activity of 12,084 I.U./mg. The purified preparation resolves into a single band following SDS-PAGE and has an apparent molecular weight of 45 kDa. HPLC of the purified fraction also yields a single peak at 45 kDa. Decidual uPA is immunogenic in rabbit and a monospecific antiserum raised against it does not cross react with human melanoma tPA or rat Yoshida sarcoma tPA but elicits a precipitin reaction with human uPA and extracts of rat placenta and kidney. The enzyme has a pH optimum of 7.5, a kM of 1.0 microM, is heat stable upto ten minutes at 42 degrees C and inhibited by anti-uPA IgG.A R Pawse, U Tarachand
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Urokinase-type plasminogen activator mediates basic fibroblast growth factor-induced bovine endothelial cell migration independent of its proteolytic activity.
The dependence of urokinase-type plasminogen activator (uPA) induction on endogenous basic fibroblast growth factor (bFGF) activity during endothelial cell migration was investigated utilizing a combination of wounded endothelial cell monolayers and substrate overlay techniques. Purified polyclonal rabbit immunoglobulin G (IgG) against bFGF blocked the appearance of uPA-dependent lytic activity normally observed at the edge of a wounded bovine aortic endothelial (BAE) cell monolayer. Additionally, the migration of cells into the denuded area was inhibited 30-50% by antibodies either to bFGF or to bovine uPA. Incubation of wounded monolayers with either purified bovine uPA or agents able to induce PA activity, such as phorbol myristate acetate (PMA), vanadate, or bFGF, resulted in enhanced migration of cells (28-50%). Anti-bovine uPA IgG blocked a significant fraction (25%) of BAE cell migration induced by exposure to exogenous bFGF. The role of uPA in migration of wounded BAE cells was not dependent on plasmin generation. Furthermore, the amino terminal fragment (ATF) of human recombinant (hr) uPA, which is enzymatically inactive, stimulated endothelial cell movement in the presence of anti-bFGF IgG. These results suggest that BAE cell migration from the edge of a wounded monolayer is dependent upon local increases of uPA mediated by endogenous bFGF. Moreover, the data support the conclusion that migration is stimulated via a signalling mechanism dependent upon occupancy of the uPA receptor but independent of uPA-mediated proteolysis.L E Odekon, Y Sato, D B Rifkin