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IGFBP-5 Protein, Mouse, Recombinant (His)

IGFBP-5 Protein, Mouse, Recombinant (His)

Catalog Number: orb1961240

DispatchUsually dispatched within 5-10 working days
$ 230.00
Catalog Numberorb1961240
CategoryProteins
DescriptionMouse 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.
TagC-6xHis
Purity98.00%
Protein SequenceLeu20-Glu271
UniProt IDQ07079
MW38 KDa (reducing condition)
Application notesReconstitute 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 SystemHEK293 Cells
Biological OriginMouse
Biological ActivityMouse 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 RegionLeu20-Glu271
Storage-20°C
NoteFor research use only