Mouse Osteopontin N-half ELISA

Osteopontin (OPN) is known as a highly acidic calcium-binding glycosylated phosphoprotein secreted by many cell types, including osteoblasts, kidney tubule cells, macrophages, activated T cells, and vascular smooth muscle cells. Its molecular weights have been reported in the range of 66 kDa to 44 kDa depending on glycosylation and phosphorylation. One important feature of OPN is that it contains an Arg-Gly-Asp (RGD) amino acid sequence. This motif is present in fibronectin, vitronectin and a variety of other extra cellular proteins that bind members of the integrin family of cell surface receptors such as avß3. Another important point is the presence of various molecular forms of OPN in vivo due to differential RNA splicing, glycosylation, phosphorylation, sulfation, and susceptibility to proteases. Both OPN and thrombin are likely to be localized together at the site of injury, inflammation, and angiogenesis and in tumor tissues. Osteopontin is susceptible to proteolytic fragmentation, and this process may have physiologic importance. The kit can specifically assay for N-terminal fragment of thrombin-cleaved Mouse OPN (OPN N-Half), and almost can not detect uncleaved OPN.