uPA / PLAU antibody

Principal name

uPA / PLAU antibody

Alternative names for uPA / PLAU antibody

Urokinase-type plasminogen activator, U-plasminogen activator, Urokinase, Urokinase-type plasminogen activator long chain A, Urokinase-type plasminogen activator short chain A, Urokinase-type plasminogen activator chain B

SwissProt ID

P00749 (Human), P04185 (Pig), P06869 (Mouse), P15120 (Chick), P29598 (Rat), Q05589 (Bovin), Q6SLL2 (Canfa), Q8MHY7 (Rabit)

Gene ID

5328 (PLAU), 18792 (Plau)

Available reactivities

Hu (Human), Ms (Mouse), Rt (Rat), Can (Canine)

Available hosts

Mouse, Goat, Rabbit, Sheep

Available applications

Enzyme Immunoassay (E), Western blot / Immunoblot (WB), Frozen Sections (C), Paraffin Sections (P), Immunoprecipitation (IP), Radioimmunoassay (R), Dot blot (Dot)

Background of uPA / PLAU antibody

uPA (urokinase-type plasminogen activator) and tPA (tissue plasminogen activator) are serine proteases that are members of the trypsin family, and they are essential to the intrinsic coagulation system. tPA is primarily involved in fibrinolysis, whereas uPA principally mediates cell migration and tissue remodeling processes. uPA and tPA are responsible for cleaving plasminogen, a large serum β-globulin that is deposited on the Fibrin strands within a thrombus. uPA and tPA preferentially target plasminogen at the Arg-Val bond to produce plasmin (also designated fibrinolysin), which is a trypsin-like enzyme that acts on Arg-Lys bonds in Fibrin and Fibrinogen and contributes to the systematic activation of the coagulation cascade. uPA and tPA each consist of two chains that are designated A and B. The A chain of uPA can be cleaved, resulting in low and high molecular mass forms. uPA and tPA are regulated by the serpin family members PAI-1 and PAI-2, which are serine proteinase inhibitors that complex with uPA, tPA and other targeted proteinases and then slowly disassociate to produce cleaved species that fold into stable inactive conformations.

General readings

Morgan H, Hill PA. Human breast cancer cell-mediated bone collagen degradation requires plasminogen activation and matrix metalloproteinase activity. Cancer Cell Int. 2005 Feb 08;5(1):1.

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