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 ED50 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 human IGFBP-5 protein Leu21-Glu272, with an N-terminal Met
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
28-29 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
35-37 kDa, reducing conditions
Publications
Read Publications using 875-B5 in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in Acetonitrile and TFA.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IGFBP-5 Protein, CF
IBP5IBP-5
IGF-binding protein 5
IGFBP5
IGFBP-5
insulin-like growth factor binding protein 5
insulin-like growth factor-binding protein 5
Background
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.
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.
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