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Catalog Number | orb1961240 |
---|---|
Category | Proteins |
Description | Mouse Insulin-like growth factor-binding protein 5(IGFBP-5) belongs to the superfamily of insulin-like growth factor (IGF) binding proteins. It contains 1 IGFBP N-terminal domain and 1 thyroglobulin type-1 domain. Mouse IGFBP-5 shows 97% aa sequence identity with those of human and rat IGFBP-5. It is expressed mostly in kidney, uterus and gastrocnemius muscle. It also expressed by fibroblasts, myoblasts and osteoblasts, making it the predominant IGFBP found in bone extracts. IGFBP-5 has a strong affinity for hydroxyapatite, allowing it to bind to bone cells. When bound to extracelluar matrix, IGFBP-5 is protected from proteolysis and potentiates IGF activity, but when it is soluble, IGFBP-5 is cleaved to a biologically inactive 21 kDa fragment. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. |
Tag | C-6xHis |
Purity | 98.00% |
Protein Sequence | Leu20-Glu271 |
UniProt ID | Q07079 |
MW | 38 KDa (reducing condition) |
Application notes | Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing. |
Expression System | HEK293 Cells |
Biological Origin | Mouse |
Biological Activity | Mouse Insulin-like growth factor-binding protein 5(IGFBP-5) belongs to the superfamily of insulin-like growth factor (IGF) binding proteins. It contains 1 IGFBP N-terminal domain and 1 thyroglobulin type-1 domain. Mouse IGFBP-5 shows 97% aa sequence identity with those of human and rat IGFBP-5. It is expressed mostly in kidney, uterus and gastrocnemius muscle. It also expressed by fibroblasts, myoblasts and osteoblasts, making it the predominant IGFBP found in bone extracts. IGFBP-5 has a strong affinity for hydroxyapatite, allowing it to bind to bone cells. When bound to extracelluar matrix, IGFBP-5 is protected from proteolysis and potentiates IGF activity, but when it is soluble, IGFBP-5 is cleaved to a biologically inactive 21 kDa fragment. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. |
Expression Region | Leu20-Glu271 |
Storage | -20°C |
Note | For research use only |