PKCα/β2 Antibody (Thr^638/641), pAb, Rabbit

Protein kinase C ('PKC', EC 2.7.11.13) is a cyclic nucleotide-independent enzyme that phosphorylates serine and threonine residues in many target proteins. The PKC family has been divided into three groups by the enzymes' cofactor requirements: conventional (c)PKC isoforms (comprising α, βI (also known as β1), βII (also known as β2) and γ), that require diacylglycerol (DAG), Ca2+, and phospholipid for activation; novel (n)PKC isoforms (comprising δ, ε, η (also known as PKC-L), θ and µ (the mouse homolog of human PKCµ, known as PKD)) that require DAG but not Ca2+; and atypical (a)PKC isoforms, namely ζ, ι, and λ (the mouse homolog of human PKC ι) that require neither Ca2+ nor DAG. A new PKC member has recently been discovered and is referred to as PKCν. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. PKC activity is regulated through three distinct phosphorylation sites, the activation loop threonine (Thr497 in PKCα and Thr500 in PKCβ2), the turn loop autophosphorylation threonine (Thr638 in PKCα and Thr641 in PKCβ2) and the hydrophobic loop serine (Ser657 in PKCα and Ser660 in PKCβ2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms.