Anti-MSK-1 antibody produced in rabbit

The mitogen- and stress-activated kinases, MSK-1 and MSK-2 are activated by ERK/MAPK and p38 MAPK in response to growth and cell stress stimuli. MSK-1 and MSK-2 have 75% homology and interact with ERK1/2 and p38 through MAPK-binding domains near the C-terminus. There is a predominant expression of MSK proteins in heart, brain, skeletal muscles, lung, liver, kidney, pancreas and placenta. Highly conserved phosphorylation sites of MSK-1, Ser260 and Thr581, are followed by proline residues indicating that MSK-1 is activated by more than one MAPK. Endogenous MSK-1 is activated in cells by growth factors, phorbol ester stimulation, exposure to UV irradiation, and oxidative or chemical stress and is localized to nucleus of unstimulated or stimulated cells. MSK-1 is directly involved in the regulation of gene expression since it actively phosphorylates, stabilizes and activates many transcription factors. The major transcription factors that are regulated by MSK-1 include CREB, NF-κB and STAT3. MSKs also evidently phosphorylate Histone H3 at Ser10 and Ser28 and HMG at Ser6. Thus a primary role of MSK proteins is also promotion of gene relaxation and activation by regulating the binding of transcription repressors. Anti-MSK-1 specifically recognizes rat MSK-1 (90 kDa).

synthetic peptide corresponding to the C-terminus of human MSK1 (amino acids 783-800). This sequence is not found in the human and mouse MSK2 isoforms.

Anti-MSK-1 may be used at a minimum working dilution of 1:2000 (immunoblotting in whole cell extracts) or 1:1000 (immunocytochemistry) in fibroblast Rat1 cell line. The antobody has also been used for detection by immunoblotting in mouse fibroblast 10T1/2 cells.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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