详细说明
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to inhibit the biological activity of IGF-I or IGF-II on MCF‑7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED 50 for this effect is 0.5‑1.5 µg/mL in the presence of 14 ng/mL rhIGF-II.
Source
Mouse myeloma cell line, NS0-derived Glu28-Glu272
Accession #
N-terminal Sequence
AnalysisGlu28
Predicted Molecular Mass
28 kDa
SDS-PAGE
34 kDa, reducing conditions
875-B5 |
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Formulation Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA. | ||
Reconstitution Reconstitute at 100 μg/mL in sterile PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: IGFBP-5
The superfamily of insulin-like growth factor (IGF) binding proteins include the six high-affinity IGF binding proteins (IGFBP) and at least four additional low-affinity binding proteins referred to as IGFBP related proteins (IGFBP-rP). All IGFBP superfamily members are cysteine-rich proteins with conserved cysteine residues, which are clustered in the amino- and carboxy-terminal thirds of the molecule. IGFBPs modulate the biological activities of IGF proteins. Some IGFBPs may also have intrinsic bioactivity that is independent of their ability to bind IGF proteins. Post-transitional modifications of IGFBP, including glycosylation, phosphorylation and proteolysis, have been shown to modify the affinities of the binding proteins to IGF.
Human IGFBP-5 cDNA encodes a 272 amino acid (aa) residue precursor protein with a putative 20 aa residue signal peptide that is processed to generate the 252 aa residue mature protein that is post-translationally modified by O-glycosylations and serine phosphorylations. IGFBP-5 is 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 extracellular 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.
References:
Jones, J.I. and D.R. Clemmons (1995) Endocrine Rev. 16:3.
Kelley, K.M. et al. (1996) Int. J. Biochem. Cell Biol. 28:619.
Long Name:
Insulin-like Growth Factor Binding Protein 5
Entrez Gene IDs:
3488 (Human); 16011 (Mouse)
Alternate Names:
IBP5IBP-5; IGF-binding protein 5; IGFBP5; IGFBP-5; insulin-like growth factor binding protein 5; insulin-like growth factor-binding protein 5