IGFBP5 Polyclonal Antibody

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 Cayman’s IGFBP5 Polyclonal Antibody is directed against a synthetic peptide sequence that partially overlaps the IGFBP5 region identified as a nuclear localization signal.² IGFBP5 (272 amino acids) has a calculated molecular weight of 30.6 kDa. Cayman’s IGFBP5 Polyclonal Antibody can be used for Western blot applications and recognizes IGFBP5 at 33 kDa from mouse and rat samples. Reported glycosylation and phosphorylation sites may explain the band migration to 33 kDa.^1,5

WARNING This product is not for human or veterinary use.

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. The Journal of Biological Chemisty 281(20), 14184-14191 (2006).

3. Shimasaki, S., Shimonaka, M., Zhang, H.P., 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. The Journal of Biological Chemisty 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. The Journal of Biological Chemisty 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).