Phospho-S6 Ribosomal Protein (Ser235/236) (2F9) Rabbit mAb (BSA and Azide Free)

One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of S6 protein (4,5). 1.Dufner, A. and Thomas, G. (1999) Exp Cell Res 253, 100-9. 2.Peterson, R.T. and Schreiber, S.L. (1998) Curr Biol 8, R248-50. 3.Jefferies, H.B. et al. (1997) EMBO J 16, 3693-704. 4.Ferrari, S. et al. (1991) J Biol Chem 266, 22770-5. 5.Flotow, H. and Thomas, G. (1992) J Biol Chem 267, 3074-8. 6.Kotecha, N. et al. (2008) Cancer Cell 14, 335-43.