TAO2 Antibody (Phospho-Ser181)

Polyclonal Antibody

Wet Ice

The antibody has been directly tested for reactivity in Western blots with human, mouse and rat tissue. It is anticipated that the antibody will react with canine, finch, Xenopus and zebra fish based on the fact that these species have 100% homology with the amino acid sequence used as antigen.
Western blot of rat cortex lysate showing specific immunolabeling of the ~120k TAO2 phosphorylated at Ser181 (Control). The phosphospecificity of this labeling is shown in the second lane (lambda-phosphatase: lambda -Ptase). The blot is identical to the control except that it was incubated in lambda -Ptase (1200 units for 30 min) before being exposed to the Ser181 TAO2 antibody. The immunolabeling is completely eliminated by treatment with lambda -Ptase.

Liquid. 100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

In vitro, TAO (thousand and one amino acid) protein kinase 2 (TAO2) activates MAP/ERK kinases (MEKs) 3, 4, and 6 toward their substrates p38 MAP kinase JNK/SAPK (Chen et al., 1999; Chen and Cobb, 2001). This and more recent work has led to the proposal that the TAO protein kinases play an essential role in signaling from physiological agonists to the stress-responsive p38 MAPKs (Chen et al., 2003). Autophosphorylation of TAO may play a role in the mechanism of TAO activation. The MEK binding domain of TAO is autophosphorylated on both serine and threonine residues and Ser181 is located within this domain.

Serine/threonine-protein kinase TAO2

Prepared from rabbit serum by affinity purification via sequential chromatography on phospho- and dephosphopeptide affinity columns.

Dog; Human; Mouse; Rat; Zebrafish