|Other Names||Urokinase-type plasminogen activator, U-plasminogen activator, uPA, Urokinase-type plasminogen activator long chain A, Urokinase-type plasminogen activator short chain A, Urokinase-type plasminogen activator chain B, PLAU|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP8161b was selected from the C-term region of human PLAU . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Specifically cleaves the zymogen plasminogen to form the active enzyme plasmin.|
|Tissue Location||Expressed in the prostate gland and prostate cancers.|
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Provided below are standard protocols that you may find useful for product applications.
PLAU, a member of the peptidase family S1, is a potent plasminogen activator and is clinically used for therapy of thrombolytic disorders. PLAU specifically cleaves the Arg-|-Val bond in plasminogen to form plasmin. The protein is found in high and low molecular mass forms. Each consists of two chains, A and B. The high molecular mass form contains a long chain A. Cleavage occurs after residue 155 in the low molecular mass form to yield a short A1 chain. The protein is used in Pulmonary Embolism (PE) to initiates fibrinolysis. Structurally, PLAU contains 1 EGF-like domain and 1 kringle domain.
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Sperl, S., et al., Proc. Natl. Acad. Sci. U.S.A. 97(10):5113-5118 (2000).Turkmen, B., et al., Electrophoresis 18(5):686-689 (1997).Conne, B., et al., Thromb. Haemost. 77(3):434-435 (1997).Yoshimoto, M., et al., Biochim. Biophys. Acta 1293(1):83-89 (1996).
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