PKC zeta (pT560) Phospho

GWB-5417D0

A phospho specific peptide corresponding to residues surrounding Threonine 560 of human PKC zeta was used as an immunogen. This antibody detects PKC zeta phosphorylated at Threonine 560.

WB: 1:1 000 - 10 000IHC: 1:100ICC: 1:100IP: 1:50. Protein kinase C (PKC) a class of serine/threonine kinases activated by Ca2+ and/or phospholipids is involved in a variety of cellular processes such as proliferation differentiation and secretion. PKC zeta exhibits a constitutive kinase activity which is independent of Ca2+ phosphatidylserine and diacylglycerol. Arachidonic acid alone or a combination of gamma-linolenic acid and phosphatidylserine slightly enhance PKC zeta activity. PKC zeta in contrast to PKC alpha is insensitive to PKC inhibitors known to interfere either with the regulatory or the catalytic domain and cannot be activated by phorbol ester treatment of NIH 3T3 cells or insect cells overexpressing the respective PKC isoenzyme (1). Results have identified PDK-1 as the kinase that phosphorylates and activates PKC zeta in the PI 3-kinase signaling pathway. This phosphorylation and activation of PKC zeta by PDK-1 is enhanced in the presence of Ptdins-3 4-5-P3. PKCs are enzymes that are regulated at the plasma membrane and a membrane-targeted PKC zeta is constitutively active in the absence of agonist stimulation. The association between PKC zeta and PDK-1 reveals extensive cross-talk between enzymes in the PI 3-kinase signaling pathway. (2) 1. Kochs G et al. Eur J Biochem 216(2):597-606 19932. Chou MM et al. Curr Biol 8(19):1069-773. Manufactured under U. S. Patents No. 5 675 063 and 7 429 487