Product Datasheet  
MAPKAPK2 (Phospho-Thr334) Antibody  
Catalog Number: 12103  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species：  
  • Rabbit
  • Amount：  
  • 100μgμg
  • Swiss-Prot No.：  
  • Swiss-Prot#:P49137;
    NCBI Gene#:9261
  • Form of Antibody：  
  • Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
  • Storage：  
  • Store at -20˚C
  • Immunogen：  
  • Peptide sequence around phosphorylation site of threonine 334 (P-Q-T(p)-P-L) derived from Human MAPKAPK2.
  • reactivity：  
  • Hu Ms Rt
  • appl_detail：  
  • Western blotting: 1:500~1:3000
    Immunohistochemistry: 1:50~1:100
  • other_names：  
  • EC 2.7.11.1; MAP kinase-activated protein kinase 2; MAPK-activated protein kinase 2; MAPK2; MAPKAP kinase 2; MAPKAPK-2; MAPKAPK2; RPS6KC1; kinase MAPKAPK2
  • Purification：  
  • Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy usi
  • Specificity：  
  • The antibody detects endogenous levels of MAPKAPK2 only when phosphorylated at threonine 334.
  • Applications：  
  • WB IHC
  • Background：  
  • Stress-activated serine/threonine-protein kinase involved in cytokines 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, 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 dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively.



 
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