PLAUR / CD87 / uPAR Protein (His & Fc tag) (recombinant mouse)

Activity: Measured by its binding ability in a functional ELISA. Immobilized human uPA at 5 µg/ml (100 µl/well) can bind mouse PLAUR with a linear ranger of 1.6-40 ng/ml. Protein Construction: A DNA sequence encoding the extracellular domain (Met 1-Thr 297) of mouse PLAUR (NP_035243.1) precursor was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the C-terminus. Sequence: Met 1-Thr 297. Fusion tag: C-His-Fc Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Apparent Molecular Mass: 80-90 kDa. Protein function: Urokinase plasminogen activator (uPA) and/or its receptor (uPAR) are essential for metastasis, and overexpression of these molecules is strongly correlated with poor prognosis in a variety of malignant tumours. uPAR and uPA levels in both resected tumor tissue and plasma are of independent prognostic significance for patient survival in several types of human cancer. This system has classically been thought to drive tumor progression by mediating directed extracellular proteolysis on the surface of migrating or invading cells, and intervening with this proteolysis by targeting uPAR has been proposed to represent a novel approach for inhibiting tumor progression. uPAR, also known as PLAUR or CD87, has been implicated in the growth, metastasis, and angiogenesis of several solid and hemotologic malignancies. uPAR is a highly glycosylated, 55-60kDa integral membrane protein linked to the plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. It is part of a cell surface system that also consists of the Protein function: Acts as a receptor for urokinase plasminogen activator. Plays a role in localizing and promoting plasmin formation. Mediates the proteolysis-independent signal transduction activation effects of U-PA. [The UniProt Consortium]