| item: | Mouse Osteopontin Assay Kit |
| vendor: | Immuno-Biological Laboratories, Inc. |
| catalog number: | 27351 |
| quantity: | 1 x 96 wells |
| description: | This kit #27351 has improved stability and convenience from the former kit #17351. However, the improved kit not only has overcome this problem but also produced some advantages as follows. At first, we have changed the formulation of HRP conjugated antibody from lyophilized product to liquid (0.4mL X 1). By this change, the stability of the conjugate has improved so that the conjugate can use for 12 months even in stored at 2-8C and use several times. And further, we have changed the formulation of TMB tablet (1mg X 2) to liquid (15mL X 1) with one bottle. By this change, the liquid TMB can use itself without preparation. And further, the stability of this liquid TMB has improved so that the liquid TMB can use for 12 months and use several times. Meantime, this change of formulation does not reflect change of performance. This meaning is that measurement value is not affected by this change in comparison with former kit. Osteopontin (OPN) is a secreted glycoprotein that was originally isolated from bone. At present, it 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 ?v?3. Another important of OPN is is the presence of various molecular forms 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, in- flammation, and angiogenesis and in tumor tissues. Osteopontin is susceptible to proteolytic fragmentation, and this process may have physiologic importance. A report demonstrated that thrombin treatment enhanced OPN cell adhesive activity, suggesting that cleavage of OPN by thrombin exposes a cryptic adhesive sequence. More recently, it was shown that an aminoterminal OPN fragment contains a cryptic binding site that can be recognized by ?9?1 integrin. Furthermore, OPN contains multiple cell binding sites and interacts with various receptors; these interactions may have distinct functional. |
| URL: | www.ibl-america.com/elisa.html |
| catid: | 17896 |
| category name: | Assay Kit Search |
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