|Reactivity||Human, Mouse, Rat|
|Calculated MW||83736 Da|
|Other Names||Ribosomal protein S6 kinase alpha-3, S6K-alpha-3, 90 kDa ribosomal protein S6 kinase 3, p90-RSK 3, p90RSK3, Insulin-stimulated protein kinase 1, ISPK-1, MAP kinase-activated protein kinase 1b, MAPK-activated protein kinase 1b, MAPKAP kinase 1b, MAPKAPK-1b, Ribosomal S6 kinase 2, RSK-2, pp90RSK2, RPS6KA3, ISPK1, MAPKAPK1B, RSK2|
|Target/Specificity||A phospho-specific peptide corresponding to residues surrounding Serine 227 of human RSK2 was used as an immunogen. The antibody only detects RSK2 phosphorylated on Serine 227.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||RSK2 Antibody Phospho (pS227) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||ISPK1, MAPKAPK1B, RSK2|
|Function||Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR- independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro- apoptotic proteins BAD and DAPK1 and suppressing their pro- apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. In LPS-stimulated dendritic cells, is involved in TLR4-induced macropinocytosis, and in myeloma cells, acts as effector of FGFR3-mediated transformation signaling, after direct phosphorylation at Tyr-529 by FGFR3. Phosphorylates DAPK1.|
|Cellular Location||Nucleus. Cytoplasm|
|Tissue Location||Expressed in many tissues, highest levels in skeletal muscle|
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Provided below are standard protocols that you may find useful for product applications.
RSK2 is a member of the family of 90-kDa ribosomal S6 kinases (1). These proteins are a class of serine/threonine kinases that are activated in response to various extracellular signals, including growth factors, polypeptide hormones and neurotransmitters (2). RSK2 plays a significant role in mediating extracellular signal-related kinase signal transduction. Mutations in RSK2 have been found to be associated with Coffin-Lowry syndrome (3). The N-terminal kinase of RSK2 is involved in substrate phosphorylation. The isolated N-terminal kinase of RSK2 (amino acids 1-360) is phosphorylated at Serine 227 by PDK1. Data indicate that full activation of RSK2 by growth factors requires the cooperation of extracellular signal-regulated kinase and PDK1 through phosphorylation of Serine 227, Serine 369, and Serine 386 (4).
1. Moller D.E., et al. Am J Physiol. 266(2): C351-359, 1994
2. Frodin M, et al. Mol. Cell. Endocrinol. 151(1-2):65-67, 1999
3. Trivier, E., et al. Nature. 384:567-570, 1996
4. Jensen CJ, et al. J Biol Chem. 274(38):27168-76, 1999
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