|Reactivity||Human, Mouse, Rat|
|Calculated MW||89865 Da|
|Other Names||Ribosomal protein S6 kinase alpha-5, S6K-alpha-5, 90 kDa ribosomal protein S6 kinase 5, Nuclear mitogen- and stress-activated protein kinase 1, RSK-like protein kinase, RSKL, RPS6KA5, MSK1|
|Target/Specificity||A synthetic phospho-peptide corresponding to residues surrounding Serine 360 of human MSK1 was used as immunogen. The antibody will detect MSK1 phosphorylation on Serine 360.|
|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||MSK1 Antibody Phospho (pS360) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Serine/threonine-protein kinase that is required for the mitogen or stress-induced phosphorylation of the transcription factors CREB1 and ATF1 and for the regulation of the transcription factors RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by histone phosphorylation and functions in the regulation of inflammatory genes. Phosphorylates CREB1 and ATF1 in response to mitogenic or stress stimuli such as UV-C irradiation, epidermal growth factor (EGF) and anisomycin. Plays an essential role in the control of RELA transcriptional activity in response to TNF and upon glucocorticoid, associates in the cytoplasm with the glucocorticoid receptor NR3C1 and contributes to RELA inhibition and repression of inflammatory gene expression. In skeletal myoblasts is required for phosphorylation of RELA at 'Ser-276' during oxidative stress. In erythropoietin-stimulated cells, is necessary for the 'Ser-727' phosphorylation of STAT3 and regulation of its transcriptional potential. Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby regulates its ability to stimulate transcription, which may be important during development and breast tumor formation. Directly represses transcription via phosphorylation of 'Ser-1' of histone H2A. Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress stimuli and EGF, which results in the transcriptional activation of several immediate early genes, including proto- oncogenes c-fos/FOS and c-jun/JUN. May also phosphorylate 'Ser-28' of histone H3. Mediates the mitogen- and stress-induced phosphorylation of high mobility group protein 1 (HMGN1/HMG14). In lipopolysaccharide-stimulated primary macrophages, acts downstream of the Toll-like receptor TLR4 to limit the production of pro- inflammatory cytokines. Functions probably by inducing transcription of the MAP kinase phosphatase DUSP1 and the anti- inflammatory cytokine interleukin 10 (IL10), via CREB1 and ATF1 transcription factors. Plays a role in neuronal cell death by mediating the downstream effects of excitotoxic injury.|
|Cellular Location||Nucleus. Cytoplasm. Note=Predominantly nuclear. Exported into cytoplasm in response to glucocorticoid|
|Tissue Location||Widely expressed with high levels in heart, brain and placenta. Less abundant in lung, kidney and liver|
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Provided below are standard protocols that you may find useful for product applications.
MSK-1 is a mitogen and stress activated protein kinase-1 which belongs to the AGC family of kinases and is related in structure to the ribosomal p70 S6 kinase subfamily. MSK-1can be activated by ERK1/2 and SAPK2 /p38 MAP kinase. It is also known to be required for the phosphorylation of CREB, ATF1 H3 and HMG-14 in response to mitogen and stress (1-2). Similar to RSK, MSK-1 contains two kinase domains (N-term and a C-term) (3). Once phosphorylated on Thr581 and Ser360 by ERK1/2 and SAPK2/p38, MSK-1 autophosphorylate on at least 5 sites. Of these autophosphorylation sites Ser212 and Ser376 get phosphorylated by the C-terminal kinase domain of MSK-1 which is essential for the catalytic activity of the N-terminal kinase domain (4).
1. Deak M, Clifton AD, Lucocq LM, Alessi DR, EMBO J 1998;17:4426-41
2. Pierrat et al. (1998) J.Biol. Chem. 273, 29661
3. New et al (1999) J. Biol. Chem. 274, 1026-18852 4. Claire E. McCoy et al. Biochemical Journal Immediate Publication.November 29, 2004
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