|4508||Phospho-TAK1 (Thr184/187) (90C7) Rabbit mAb||
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Phospho-TAK1 (Thr184/187) Antibody detects endogenous levels of TAK1 only when phosphorylated at both threonine 184 and threonine 187. This antibody weakly cross-reacts with TAK1 singly phosphorylated at threonine 184.Species predicted to react based on 100% sequence homology:
Mouse, Rat, Chicken, Xenopus, Zebrafish, Bovine
Polyclonal antibodies are produced by immunizing animals with a phosphopeptide corresponding to residues surrounding Thr184 and Thr187 of human TAK1. Antibodies are purified by protein A and peptide affinity chromatography.
TAK1 is a mitogen-activated protein kinase kinase kinase that can be activated by TGF-β, bone morphogenetic protein and other cytokines including IL-1 (1,2). In vivo activation of TAK1 requires association with TAK1 binding protein 1 (TAB1), which triggers phosphorylation of TAK1 (3,4). Another adaptor protein, TAB2, links TAK1 with TRAF6 and mediates TAK1 activation upon IL-1 stimulation (5). Once activated, TAK1 phosphorylates MAPK kinases MKK4 and MKK3/6, which activate p38 MAPK and JNK, respectively. In addition, TAK1 activates the NF-κB pathway by interacting with TRAF6 and phosphorylating the NF-κB inducing kinase (NIK) (2).
TAK1 activation requires multiple phosphorylations in its activation loop. Mutations of Thr187 and Thr184, residues located in the activation loop of TAK1, impairs phosphorylation of both TAK1 and TAB1 and reduces the kinase activity of TAK1, suggesting that autophosphorylation of these residues is necessary for TAK1 activation (4).
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