Ribosomal Protein S6 (Ser 244) (RPS6) Antibody – Rabbit Polyclonal

Polyclonal

Rabbit

Human, mouse

100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug BSA per ml and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

Affinity Purified (Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.)

Specific for the ~28k rpS6 protein phosphorylated at Ser244

For long term storage -20 degree C is recommended. Stable at -20 degree C for at least 1 year.

28

Chromosome: 4; NC_000070.6 (86854099..86857367, complement). Location: 4; 4 C3

ModBase 3D Structure for P62754

Phosphopeptide corresponding to amino acid residues surrounding the phospho-Ser244 of mouse rpS6.

Synthetic phospho-peptide corresponding to amino acid residues surrounding Ser244 conjugated to KLH

Mouse

Chicken, guinea pig, non-human primate, rat, Xenopus and zebrafish

The antibody has been directly tested for reactivity in Western blots with mouse and human tissue. It is anticipated that the antibody will react with chicken, guinea pig, non-human primate, rat, Xenopus and Zebrafish based on the fact that these species have 100% homology with the amino acid sequence used as antigen.

Ribosomal protein S6 (rpS6) is a critical component of the 40 S ribosomal subunit that mediates translation initiation at the 5'-m7GpppG cap of mRNA. The rpS6 protein is both cytoplasmic and nuclear localized (Chen and Dittmer 2011). In response to mitogenic stimuli, rpS6 undergoes ordered C-terminal phosphorylation by p70 S6 kinases and p90 ribosomal S6 kinases on four Ser residues (Ser-235, Ser-236, Ser-240, and Ser-244) whose modification potentiates rpS6 cap binding activity (Hutchinson et al., 2011). Additionally, rpS6 phosphorylation and function are highly regulated and have been implicated in the regulation of translational initiation and protein synthesis in response to extracellular stimuli such as TRAIL and gamma interferon (IFN-gamma), as well as upon activation of the phosphatidylinositol 3-kinase (PI3K)-Akt-mTOR pathway (Chen and Dittmer 2011).