Human u-Plasminogen Activator (uPA)/Urokinase Biotinylated Antibody
Human u-Plasminogen Activator (uPA)/Urokinase Biotinylated Antibody Summary
Ser21-Leu432
Accession # P00749
Applications
Human u-Plasminogen Activator/Urokinase Sandwich Immunoassay
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: u-Plasminogen Activator (uPA)/Urokinase
uPA is a serine protease with an extremely limited substrate specificity, cleaving the sequence Cys-Pro-Gly-Arg560-Val561-Val-Gly-Gly-Cys in plasminogen to form plasmin (1). uPA is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium (2). For example, the combination (both low vs. either or both high) of uPA and its inhibitor, plasminogen activator inhibitor-1 (PAI-1), outperforms the single factors as well as other traditional prognostic factors with regard to risk group assessment for breast cancer, particularly in node-negative breast cancer (3). The human uPA is initially synthesized as 431 amino acid precursor with a N-terminal signal peptide (20 residues) (4 - 6). The single chain molecule is processed into a disulfide-linked two-chain molecule. The B chain starting at Ile179 corresponds to the catalytic domain. Two forms of the A chain exist, one starting at Ser21 (the long form) and the other at Lys156 (the short form). The resulting two-chain forms have different molecular weights (MW). The B chain is common for both forms whereas the long and short A chains are unique to the high and low MW forms, respectively. The long A chain contains an EGF-like domain, which is responsible for binding of the uPA receptor (uPAR).
- Ellis, V. (2004) in Handbook of Proteolytic Enzymes. Barrett, A.J. et al. eds., Academic Press, San Diego, pp.1677.
- Duffy, M.J. (2002) Biochem. Soc. Trans. 30:207.
- Harbeck, N. et al. (2002) Clin. Breast Cancer 3:196.
- Riccio, A. et al. (1985) Nucleic Acids Res. 13:2785.
- Nagai, M. et al. (1985) Gene 36:183.
- Jacobs, P. et al. (1985) DNA 4:139.
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