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Antigenic Specificity | S6 pS240, Human |
Clone | REA420 |
Host Species | Recombinant Human |
Reactive Species | human |
Isotype | IgG1 |
Format | fluorescein (FITC) conjugate |
Size | 100 tests in 1 mL |
Concentration | 1:11 |
Applications | Intracellular flow cytometry |
Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
Description | S6 pS240 Antibody, anti-human, FITC, REAfinity™. Clone REA420 recognizes the human 40S ribosomal protein S6 antigen phosphorylated at serine 240 (pS240). 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. | Additional information: Clone REA420 displays negligible binding to Fc receptors. |
Immunogen | n/a |
Other Names | RPS6, NP33, RS6 |
Gene, Accession # | Gene ID: 6194 |
Catalog # | 130-106-560 |
Price | $260 |
Order / More Info | S6 pS240, Human Antibody from MILTENYI BIOTEC B.V. & Co. KG |
Product Specific References | Selman, C. et al. (2009) Ribosomal protein S6 kinase 1 signaling regulates mammalian life span. Science 326 (5949): 140-144. | Lott, J. B. et al. (1988) Isolation and characterization of cloned cDNAs that code for human ribosomal protein S6. Gene 65 (1): 31-39. | Shah, O. J. et al. (2003) Mitotic regulation of ribosomal S6 kinase 1 involves Ser/Thr, Pro phosphorylation of consensus and non-consensus sites by Cdc2. J. Biol. Chem. 278 (18): 16433-16442. |