10008207  IGFBP5 Polyclonal Antibody

IGF-Binding Protein 5; IBP-5; Insulin-like Growth Factor Binding Protein 5



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• See more Immunocytochemistry; Western Blot; Antibodies; Apoptosis; Cancer; Endocrinology

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Antigen: human IGFBP5 amino acids 192-206 (CRRHMEASLQELKAS) · Host: rabbit · Application(s): WB · Insulin-like growth factor binding protein 5 (IGFBP5) is a secreted protein that binds IGF-1 and restricts it from accessing its cell-surface receptor (IGF-1R). This aids in regulation of cell growth, differentiation, and apoptosis.1 IGFBP5 also displays IGF-1 independent transactivational activity in the nucleus.2 Some tissues and cell types with higher levels of this protein include kidney, heart, placenta, and skeletal cells.3 Expression has also been reported in a variety of cancers, including mammary gland and neuroblastoma.1,4 IGFBP5 (272 amino acids) has a calculated molecular weight of 30.6 kDa. Reported glycosylation and phosphorylation sites may explain the band migration to 33 kDa.1,5
1  Beattie, J., Allan, G.J., Lochrie, J.D., et al. Insulin-like growth factor-binding protein-5 (IGFBP-5): A critical member of the IGF axis. Biochem J 395 1-19 (2006).
2  Zhao, Y., Yin, P., Bach, L.A., et al. Several acidic amino acids in the N-domain of insulin-like growth factor-binding protein-5 are important for its transactivation activity. J Biol Chem 281(20) 14184-14191 (2006).
3  Shimasaki, S., Shimonaka, M., Zhang, H., et al. Identification of five different insulin-like growth factor binding proteins (IGFBPs) from adult rat serum and molecular cloning of a novel IGFBP-5 in rat and human. J Biol Chem 266(16) 10646-10653 (1991).
4  Tanno, B., Negroni, A., Vitali, R., et al. Expression of insulin-like growth factor-binding protein 5 in neuroblastoma cells is regulated at the transcriptional level by c-Myb and B-Myb via direct and indirect mechanisms. J Biol Chem 277(26) 23172-23180 (2002).
5  Pampusch, M.S., Xi, G., Kamanga-Sollo, E., et al. Production of recombinant porcine IGF-binding protein-5 and its effect on proliferation of porcine embryonic myoblast cultures in the presence and absence of IGF-I and Long-R3-IGF-I. J Endocrinol 185 197-206 (2005).

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Pricing Information

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Pricing updated 2010-09-09.
Prices are subject to change without notice.