- CITATIONS: 1
|Application ||WB, IHC|
|Calculated MW||45568 Da|
|Other Names||MAP kinase-activated protein kinase 2, MAPK-activated protein kinase 2, MAPKAP kinase 2, MAPKAP-K2, MAPKAPK-2, MK-2, MK2, MAPKAPK2|
|Target/Specificity||A synthetic peptide corresponding to residues near C-terminus of human MAPKKAP Kinase-2 was used as immunogen.|
|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||MAPKAP Kinase-2 Antibody Phospho (pT334) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Stress-activated serine/threonine-protein kinase involved in cytokine production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, CEP131, ELAVL1, HNRNPA0, HSF1, HSP27/HSPB1, KRT18, KRT20, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to the dissociation of HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impairment of their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post- transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA0, PABPC1 and TTP/ZFP36, leading to the regulation of the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post- transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity, leading to inhibition of dependent degradation of ARE-containing transcripts. Phosphorylates CEP131 in response to cellular stress induced by ultraviolet irradiation which promotes binding of CEP131 to 14-3-3 proteins and inhibits formation of novel centriolar satellites (PubMed:26616734). Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA0 and PARN, leading to stabilization of GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.|
|Cellular Location||Cytoplasm. Nucleus. Note=Phosphorylation and subsequent activation releases the autoinhibitory helix, resulting in the export from the nucleus into the cytoplasm|
|Tissue Location||Expressed in all tissues examined.|
Provided below are standard protocols that you may find useful for product applications.
MAPKAP Kinase-2 is part of mitogen-activated protein (MAP) kinase family which includes MAP kinase kinase kinase (1) and MAP kinase kinase (2). Once activated MAP Kinase-2 will in turn regulate the phosphorylation and activation of many substrates including cell surface molecules, cytoskeletal proteins, transcription factors, and protein kinases (3). MAPKAPK-2MAPKAP Kinase-2 is also known to be a MAP kinase substrate phosphorylating low molecular weight heat shock proteins (Hsp27 in humans) and tyrosine hydroxylase (4). In vitro kinase assay, MAPKAP Kinase-2 is phosphorylated by p38 MAPK at Thr222, Ser272 and Thr334, all essential in MAPKAPK-2 activity (5).
1. Kyriakis, J. M., App, H., Zhang, X. F., Banerjee, P., Brautigan, D. L., Rapp, U. R., and Avruch, J. (1992) Nature 358, 417-421
2. Ahn, N. G., Seger, R., and Krebs, E. G. (1992) Curr. Opin. Cell Biol. 4, 992-999
3. Davis, R. J. (1993) J. Biol. Chem. 268, 14553-14556
4. Rouse, J., Cohen, P., Trigon, S., Morange, M., Alonso-Liamazares, A., Zamannillo, D., Hunt, T., and Nebreda, A. R. (1994) Cell 78, 1027-1037
5. Ben-Levy, R. et al. (1995) EMBO J. 14, 5920-5930.
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