Spry2 (D3G1A) Rabbit mAb

The Sprouty (Spry) family of proteins are antagonists of receptor tyrosine kinase (RTK)-induced signaling (1, 2). The Spry proteins play crucial roles in regulating growth and development of living organisms. Since originally discovered in Drosophila, four human orthologs of Spry proteins (Spry1-4) have been identified. All human Spry proteins possess a conserved carboxyl-terminal cysteine-rich SPR domain, which harbors a signal for protein translocation from cytosol to membrane ruffles (3,4). The SPR domain also enables the Spry proteins to form homo- or hetero-dimers and to interact with other proteins including kinases and phosphatases. The SPR domain is essential for the inhibitory modulation of Spry proteins on RTK signaling (1,2).Studies have shown that several cancers have reduced levels of Spry2 expression implicating Spry2 as a tumor suppressor (5-8). The regulation of Spry2 expression and activity appears to be a complex process involving casein kinase 1, Shp2 phosphatase, and Spry2-interacting partners (9-11). Phosphorylation of Tyr55 residue of Spry2 is required for the inhibitory function of Spry2 in FGF/MAPK signaling (12,13). 1.Guy, G.R. et al. (2003) J Cell Sci 116, 3061-8. 2.Guy, G.R. et al. (2009) J Endocrinol 203, 191-202. 3.Lim, J. et al. (2000) J Biol Chem 275, 32837-45. 4.Lim, J. et al. (2002) Mol Cell Biol 22, 7953-66. 5.Herold, T. et al. (2014) Blood 124, 1304-11. 6.Gao, M. et al. (2012) EMBO Mol Med 4, 776-90. 7.Sánchez, A. et al. (2008) Oncogene 27, 4969-72. 8.Frank, M.J. et al. (2009) Blood 113, 2478-87. 9.Yim, D.G. et al. (2015) Oncogene 34, 474-84. 10.Okur, M.N. et al. (2014) Mol Cell Biol 34, 271-9. 11.Mason, J.M. et al. (2004) Mol Biol Cell 15, 2176-88. 12.Edwin, F. et al. (2009) Mol Pharmacol 76, 679-91. 13.Fong, C.W. et al. (2003) J Biol Chem 278, 33456-64.