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.
| 説明 |
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. |
| Species |
Mouse
|
| Expression Host |
HEK293 Cells
|
| Tag |
C-6xHis
|
| Accession Number |
Q07079
|
| 別名 |
IGFBP-5, IGF-binding protein 5, BP-5, Insulin-like growth factor-binding protein 5
|
| Amino Acid |
Leu20-Glu271
|
| Construction |
Leu20-Glu271
|
| Protein Purity |
Greater than 90% as determined by reducing SDS-PAGE. (QC verified)
|
| 分子量 |
38 KDa (reducing condition)
|
| Endotoxin |
< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
|
| Formulation |
Lyophilized from a solution filtered through a 0.22 μm filter, containing 20 mM PB, 150 mM NaCl, pH 7.4.
|
| Reconstitution |
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.
|
| Stability & Storage |
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted protein solutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
|
| Shipping |
In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry ice.
|
| Research Background |
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.
|
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