Synthetic phosphopeptide derived from human Cot around the phosphorylation site of Threonine 290.
Conjugation:
Unconjugated
Alternative Names:
Mitogen-activated protein kinase kinase kinase 8, Cancer Osaka thyroid oncogene, Proto-oncogene c-Cot, Serine/threonine-protein kinase cot, Tumor progression locus 2, TPL-2, MAP3K8, COT, ESTF
The role of mitogen-activated protein kinases (MAPKs) in cell signaling pathways is well established. The rat gene Tpl-2, for tumor progression locus 2, and the human and mouse homologues c-Cot, for cancer osaka thyroid oncogene, encode a proto-oncogene serine/threonine protein kinase that was shown to play a role in the functional activation of the MAP kinase pathway. Overexpression of Cot induces MAP kinase activation in COS-1 and NIH/3T3 cells. Cot-mediated activation of MAP kinase is inhibited by both Ras N17, a dominant negative mutant of c-H-Ras, and Raf-1s621A, a dominant negative mutant of Raf-1, suggesting that Cot functions upstream of Ras and Raf-1.Other studies have shown that a kinase-negative, dominant negative mutant of Cot partially blocks Ras or Raf-1-induced MAP kinase activation, arguing that Cot functions downstream of Ras and Raf-1.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
p-Cot (T290) polyclonal antibody detects endogenous levels of Cot protein only when phosphorylated at Thr290.
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