| Product Name | Human Osteopontin (N-term) ELISA Kit (27258) |
|---|---|
| Description | Osteopontin (OPN) is a secretory glycoprotein first isolated from the bone. At present, it is known as a highly acidic calcium-binding phosphorylated protein with sugar chain bonds, that is secreted from diverse cells, including osteoblasts, renal tubular cells, macrophages, activated T lymphocytes and vascular smooth muscle cells. Its molecular weight can vary depending on the sugar chain formation and phosphorylation, and has been reported to range from 44 to 66 kDa. One major characteristic of OPN is that its molecule contains an Arg-Gly-Asp (RGD) amino acid sequence. This motif is also seen in fibronectin, vitronectin and other extracellular proteins. It is known that OPN binds through this motif to members of the integrin family (e.g., avb3) of cell surface receptors. Another unique characteristic of OPN is that it can assume various molecular forms in vivo by undergoing RNA splicing, saccharification, phosphorylation, sulfation, degradation by protease, etc. OPN is considered to coexist with thrombin locally in tissues such as injured tissue, inflamed tissue, vascularized tissue, and tumor tissue. Coexistence with thrombin increases the likelihood of proteolysis, and this processmay have an important physiological role. Some investigators have reported evidence of enhancement of the cell adhesion of OPN by thrombin treatment. This suggests that cleavage of OPN with thrombin causes the hidden sequence of the adhering sites to be exposed. It has also been reported that the fragments of OPN produced following cleavage by thrombin react with a9b1 integrin. Furthermore, inview of the finding that OPN has many cell-binding sites and can react with various receptors, interactions between OPN and these cells or receptors may play some unknown roles. This kit can specifically measure the N-terminal OPN fragment (hereinafter called 'OPN N-Half') cleaved by thrombin. OPN molecules without thrombin cleavage, on the other hand, are hardly detected by the kit. This kit is a solid phase sandwich ELISA using 2 kinds of high specific antibodies. Tetra Methyl Benzidine (TMB) is used as coloring agent (Chromogen). The strength of coloring is in proportion to the quantities of Human Osteopontin N-Half. |
| Reactivity | Human |
| Background | Osteopontin (OPN) is a secretory glycoprotein first isolated from the bone. At present, it is known as a highly acidic calcium-binding phosphorylated protein with sugar chain bonds, that is secreted from diverse cells, including osteoblasts, renal tubular cells, macrophages, activated T lymphocytes and vascular smooth muscle cells. Its molecular weight can vary depending on the sugar chain formation and phosphorylation, and has been reported to range from 44 to 66 kDa. One major characteristic of OPN is that its molecule contains an Arg-Gly-Asp (RGD) amino acid sequence. This motif is also seen in fibronectin, vitronectin and other extracellular proteins. It is known that OPN binds through this motif to members of the integrin family (e.g., avb3) of cell surface receptors. Another unique characteristic of OPN is that it can assume various molecular forms in vivo by undergoing RNA splicing, saccharification, phosphorylation, sulfation, degradation by protease, etc. OPN is considered to coexist with thrombin locally in tissues such as injured tissue, inflamed tissue, vascularized tissue, and tumor tissue. Coexistence with thrombin increases the likelihood of proteolysis, and this processmay have an important physiological role. Some investigators have reported evidence of enhancement of the cell adhesion of OPN by thrombin treatment. This suggests that cleavage of OPN with thrombin causes the hidden sequence of the adhering sites to be exposed. It has also been reported that the fragments of OPN produced following cleavage by thrombin react with a9b1 integrin. Furthermore, inview of the finding that OPN has many cell-binding sites and can react with various receptors, interactions between OPN and these cells or receptors may play some unknown roles. This kit can specifically measure the N-terminal OPN fragment (hereinafter called 'OPN N-Half') cleaved by thrombin. OPN molecules without thrombin cleavage, on the other hand, are hardly detected by the kit. |
All Research Products are sold for laboratory RESEARCH USE ONLY and ARE NOT TO BE USED FOR HUMAN OR ANIMAL THERAPEUTIC OR DIAGNOSTIC APPLICATIONS. The information presented is believed to be accurate; however, said information and products are offered without warranty or guarantee since the ultimate conditions of use and the variability of the materials treated are beyond our control. Nothing disclosed herein is to be construed as a recommendation to use our products in violation of any patents. ARP American Research Products, Inc. does not submit its products for regulatory review by any government body or other organization, and we do not validate them for clinical, therapeutic or diagnostic use, or for safety and effectiveness. You are solely responsible for making sure that the way you use the products complies with applicable laws, regulations and governmental policies and for obtaining all necessary approvals, intellectual property rights, licenses and permissions that you may need related to your use. Under no circumstances shall ARP American Research Products, Inc. be liable for damages, whether consequential, compensatory, incidental or special, strict liability or negligence, breach of warranty or any other theory arising out of the use of the products available from ARP American Research Products, Inc. Nothing contained herein warrants that the use of the products will not infringe on the claims of any patents covering the product itself or the use thereof in combination with other products or in the operation of any process. ARP American Research Products, Inc. disclaims any and all representations or warranties of any kind whatsoever, express or implied, including without limitation any implied warranties of merchantability or fitness for a particular purpose, of non-infringement, or regarding results obtained through the use of any product, whether arising from a statute or otherwise in law or from a course of performance, dealing or usage of trade.
