Clone REA454 recognizes the human 40S ribosomal protein S6 antigen phosphorylated at serine 235 and 236 (pS235/pS236). Ribosomal protein S6 is one of 33 proteins that comprise the 40 S ribosomal subunit and becomes phosphorylated at several serine residues upon mitogen stimulation. It plays an important role in controlling cell growth and proliferation through the selective translation of particular classes of mRNA. Activation of the p90 ribosomal S6 kinases (RSKs) by serum, growth factors, tumor promoting phorbol esters, and oncogenic Ras is required for ribosomal protein S6 phosphorylation downstream of the Ras/ERK signaling cascade. The phosphorylation sites in ribosomal protein S6 have been mapped to five clustered serine residues – S235, S236, S240, S244, and S247 – which are located at the C terminus and are conserved from Drosophila to mammals. While ribosomal S6 kinase 1 phosphorylates ribosomal protein S6 at all sites, RSK exclusively phosphorylates ribosomal protein S6 at S235 and S236 in vitro and in vivo using an mTOR-independent mechanism.
Additional information: Clone REA454 displays negligible binding to Fc receptors.
RPS6, NP33, RS6
Technical specifications
