Anti-Plasminogen Activator/PLAU antibody produced in goat

Urokinase-type plasminogen activator is a serine protease with extremely limited substrate specificity, cleaving the sequence Cys-Pro-Gly-Arg560-Val561-Val-Gly-Gly-Cys in plasminogen to form plasmin. It is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium.

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Urokinase-type plasminogen activator is also known as PLAU and uPA. The human uPA is initially synthesized as 431 amino acid precursor with an N-terminal signal peptide (20 residues). The single chain molecule is processed into a disulfide-linked two-chain molecule of different molecular weights. Two forms of the A chain exist, starting at Ser21 (the long form) and Lys156 (the short form). The long and short A chains are unique to the high and low molecular weight forms, respectively. The long A chain contains an EGF (epidermal growth factor)-like domain, responsible for binding of the PLAU receptor. The B chain corresponds to the catalytic domain. The gene encoding it is localized on human chromosome 10.

Peptide with sequence C-HFLPWIRSHTKEEN from the C Terminus of the protein sequence according to NP_002649.1.

Supplied at 0.5 mg/mL in Tris saline with 0.02% sodium azide and 0.5% bovine serum albumin.