Phospho-p38 MAPK (Thr180, Tyr182) Polyclonal Antibody, Invitrogen™

Description

Predicted to react with bovine, chicken, dog, monkey, mouse and zebrafish based on sequence homology. For the detection of phosphoproteins, serine phosphatase inhibitors such as 10mM NaF should be added to the sample buffer. Milk or other casein-based blocking solutions are not recommended as casein is a phosphoprotein and its use can result in high background. In Western blot, this antibody detects a band at ∽39kDa in Western blots of anisomycin C-6 glioma cell lysates. Rabbit anti Rat p38 MAPK (pThr180/pTyr182) antibody recognizes mitogen-activated protein kinase p38 (p38 MAPK), also known as mitogen-activated protein kinase 14 (MAPK 14), when phosphorylated at threonine 180 and tyrosine 182.

MAPK14 (p38 alpha) is a member of the stress-activated protein kinase class of MAPKs. The p38 MAPK cascade regulates a variety of cellular responses to stress, inflammation, and other signals. p38 MAPK is relatively inactive in the nonphosphorylated form and becomes rapidly activated by dual phosphorylation of a Thr-Gly-Tyr motifs. There are four isoforms of p38 MAPK, which differ in their tissue expression and affinity for upstream activators and downstream effectors. When cells are exposed to tumor necrosis factor, interleukin-1, heat shock, or other activating stimuli, activation of MAPK kinase-3 occurs by phosphorylation. Activated MAPK kinase-3/6 phosphorylate each residue of Thr180 and Tyr182 in p38 MAPK. Phospho-p38 MAPK activates ATF-2, CHOP-1, MEF-2 and other transcription factors through phosphorylation.