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Recombinant Mouse IGF-I R/IGF1R Protein

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity

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Recombinant Mouse IGF-I R/IGF1R Protein Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse (rm) IGF-I R/IGF1R is present at 0.5 μg/mL, the concentration of rmIGF-I that produces 50% of the optimal binding response is found to be approximately 10-60 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse IGF-I R/IGF1R protein
Met1-His936 with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Glu31 & Asp742
Structure / Form
Covalently-linked heterotetramers (2 alpha and 2 beta subunits) & covalently-linked single chain homodimers
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, 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
104.5 kDa (single chain), 80.7 kDa ( alpha subunit) & 23.2 kDa ( beta subunit).
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
160-170 kDa, 120-130 kDa & 45-52 kDa, reducing conditions.
Publications
Read Publications using
6630-GR in the following applications:

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in PBS containing at least 0.1% human or bovine serum albumin.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse IGF-I R/IGF1R Protein

  • CD221 antigen
  • CD221
  • EC 2.7.10
  • EC 2.7.10.1
  • IGF1R
  • IGF-1R
  • IGF-I R
  • IGF-I receptor
  • IGFIR
  • IGF-IR
  • IGFR
  • insulin-like growth factor 1 receptor
  • Insulin-like growth factor I receptor
  • JTK13
  • MGC142170
  • MGC142172
  • MGC18216
  • soluble IGF1R variant 1
  • soluble IGF1R variant 2

Background

The insulin-like growth factor I receptor (IGF-I R or IGF1R, designated CD221) is a 450 kDa disulfide‑linked heterotetrameric transmembrane glycoprotein consisting of two 130 kDa alpha and two 95 kDa beta  subunits (1, 4). The IGF-1 R cDNA encodes a preproreceptor that is proteolytically cleaved to produce the extracellular alpha subunit (amino acid (aa) 31-737), which contains a cysteine-rich region and two ligand‑binding fibronectin type III (FN-III) domains, and the beta  subunit (aa 742-1369), which contains an extracellular FN-III domain, transmembrane and cytoplasmic tyrosine kinase domains (1). Extracellular portions of mature mouse IGF-I R share 99.7% aa identity with rat, 96% with human, canine and porcine, and 95% with bovine and equine IGF-I R. IGF-I R is expressed in all cell types and tissues. It binds insulin-like growth factor I (IGF-I) with high affinity, IGF-II with lower affinity, and insulin with lowest affinity (2, 3). Both IGF-I R and the structurally similar insulin receptor (Ins R) activate the same signaling pathways in response to their respective ligands (3). IGF-I R/Ins R hybrids are formed in proportion to their expression and respond primarily to IGF-I, probably down‑regulating cellular response to insulin (2, 5). IGF signaling is also modulated by IGF binding proteins and the scavenger receptor, IGF-II R (4). Expression or glycosylation of IGF-I R may be altered in cancer cells (4, 5). Mice lacking IGF-I R show intrauterine growth deficiency and die at birth due to respiratory failure, and IGF-I R mutations in humans can retarded pre- and postnatal growth (6-8). IGF-I and its receptor are particularly important for neurogenesis, with deficiency producing microcephaly and learning disorders (9-11). Low expression of IGF-I R enhances lifespan in both mouse and human by increasing resistance to oxidative stress (12, 13).  IGF-I R expression in human embryonic stem cells is important for their survival and clonogenicity (14).

  1. Wada, J. et al. (1993) Proc. Natl. Acad. Sci. USA 90:10360.
  2. Slaaby, R. et al. (2006) J. Biol. Sci. 281:25869.
  3. Boucher, J. et al. (2010) J. Biol. Chem. 285:17235.
  4. Samani, A.A. et al. (2007) Endocr. Rev. 28:20.
  5. Chitnis, M.M. et al. (2008) Clin. Cancer Res. 14:6364.
  6. Liu, J-P. et al. (1993) Cell 75:59.
  7. Abuzzahab, M.J. et al. (2003) N. Engl. J. Med. 349:2211.
  8. Walenkamp, M.J.E. and J.M. Wit (2007) Eur. J. Endocrinol. 157:S15.
  9. D’Ercole, A.J. et al. (2008) Endocrinology 149:5958.
  10. Annenkov, A. (2009) Mol. Neurobiol. 40:195.
  11. Mason, J.L. et al. (2003) J. Neurosci. 23:7710.
  12. Holzenberger, M. et al. (2003) Nature 421:182.
  13. Suh, Y. et al. (2008) Proc. Natl. Acad. Sci. USA 105:3438.
  14. Bendall, S.C. et al. (2007) Nature 448:1015.

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