|Application ||FC, IF, IHC-P, WB, E|
|Calculated MW||48507 Da|
|Antigen Region||396-426 aa|
|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||This Urokinase (PLAU) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 396-426 amino acids from the C-terminal region of human Urokinase (PLAU).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Urokinase (PLAU) Antibody (C-term) is for research use only and 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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