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 typically 0.1-0.6 µg/mL in the presence of 6 ng/mL recombinant human IGF-I.
Source
Mouse myeloma cell line, NS0-derived human IGFBP-1 protein Ala26-Asn259
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
25 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
32 kDa, reducing conditions
Publications
Read Publications using 871-B1 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 PBS.
Purity
>97%, 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-1 Protein, CF
alpha-pregnancy-associated endometrial globulin
amniotic fluid binding protein
binding protein-25
binding protein-26
binding protein-28
growth hormone independent-binding protein
hIGFBP-1
IBP1
IBP-1
IGF-binding protein 1
IGFBP1
IGFBP-1
IGF-BP25
insulin-like growth factor binding protein 1
insulin-like growth factor-binding protein 1
Placental protein 12
PP12AFBP
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-1 cDNA encodes a 259 amino acid (aa) residue precursor protein with a putative 25 aa residue signal peptide that is processed to generate the 234 aa residue mature protein. IGFBP-1 contains an integrin receptor recognition sequence (RGD sequence) but lacks potential N-linked glycosylation sites. IGFBP-1 is expressed in liver, decidua, kidneys and is the most abundant IGFBP in amniotic fluid. Serum levels of IGFBP-1 are lowest after meals. Hepatocyte production of IGFBP-1 is regulated at the transcriptional level due to the affects of insulin and corticosteriods. IGFBP-1 binds equally well to IGF-I and IGF-II, with phosphorylated forms of IGFBP-1 exhibiting higher binding affinities.
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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