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Osteopontin is a 34kDa extracellular matrix protein with a cell binding domain. It was originally identified as a major component of the non-collagenous organic bone matrix, however, it has subsequently been demonstrated in a wide range of normal adult tissue and body fluids. It is a multifunctional protein involved in bone mineralization, cell adhesion, cell migration, chronic inflammatory disease and transformation. Proteolytic cleavage by thrombin and matrix metalloproteinases close to the integrin-binding Arg-Gly-Asp sequence modulates the function of OPN and its integrin binding properties. Thrombin-cleaved fragments of Osteopontin are overexpressed in malignant glial tumors and provide a molecular niche with survival advantage and provide a novel substrate for plasmin and cathepsin D.
2AR; 2b7; 44 kDa bone phosphoprotein; Apl-1; BNSP; Bone sialoprotein 1; Bsp; BSPI; Calcium oxalate crystal growth inhibitor protein; early T-lymphocyte activation 1; early T-lymphocyte activation 1 protein; Eta; ETA-1; Minopontin; nephropontin; Op; Opn; Opnl; OSP; Osteopontin; osteopontin/immunoglobulin alpha 1 heavy chain constant region fusion protein; osteopontin-like protein; PSEC0156; Ric; Secreted phosphoprotein 1; secreted phosphoprotein 1 (osteopontin, bone sialoprotein I, early T-lymphocyte activation 1); secreted phosphoprotein 1 variant 6; Sialoprotein (osteopontin); SPP1; Spp-1; SPP1/CALPHA1 fusion; Thrombin OPN-R; urinary stone protein; Uropontin
100 µg