Polyclonal Anti-IGF1R

Price

200.00 USD

Size

100ug/vial

Reactivities

Hum, Mouse, Rat

Format

Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3.

References

1.Abbott, A. M., Bueno, R., Pedrini, M. T., Murray, J. M., Smith, R. J. Insulin-like growth factor I receptor gene structure. J. Biol. Chem. 267: 10759-10763, 1992.\n2.Dey, B. R., Furlanetto, R. W., Nissley, S. P. Cloning of human p55-gamma, a regulatory subunit of phosphatidylinositol 3-kinase, by a yeast two-hybrid library screen with the insulin-like growth factor-I receptor. Gene 209: 175-183, 1998.\n3.Giovannone, B., Lee, E., Laviola, L., Giorgino, F., Cleveland, K. A., Smith, R. J. Two novel proteins that are linked to insulin-like growth factor (IFG-I) receptors by the Grb10 adapter and modulate IGF-I signaling. J. Biol. Chem. 278: 31564-31573, 2003.\n

Storage Temp

At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.Avoid repeated freezing and thawing.

Scientific Background

IGF1R(Insulin-like Growth Factor 1 (IGF-1) Receptor) is a protein found on the surface of human cells. It is a transmembrane receptor that is activated by a hormone called Insulin-like growth factor 1 (IGF-1) and by a related hormone called IGF-2. It belongs to the large class of tyrosine kinase receptors. The IGF1R gene is mapped on 15q26.3. IGF-1 plays an important role in growth and continues to have anabolic effects in adults - meaning that it can induce hypertrophy of skeletal muscle and other target tissues. Using a yeast 2-hybrid system, Dey et al. (1998) identified a regulatory subunit of phosphatidylinositol (PI) 3-kinase, PIK3R3, as a binding partner of IGF1R. Functional interaction between BRCA1 and SP1 in the regulation of the IGF1R gene was studied in Schneider cells, a Drosophila cell line which lacks endogenous SP1. In these cells, BRCA1 suppressed 45% of the SP1-induced trans-activation of the IGF1R promoter. Overexpression of the Grb10-binding fragment of Gigyf1 resulted in a significant increase in Igf1-stimulated Igf1r tyrosine phosphorylation. Like the insulin receptor, the IGF-1 receptor is a receptor tyrosine kinase - meaning it signals by causing the addition of a phosphate molecule on particular tyrosines. IGF-1 activates the Insulin receptor at approximately 0.1x the potency of insulin. Part of this signaling may be via IGF1R-InsulinReceptor heterodimers.