anti-PKC α (Protein Kinase C α), pAb

Protein kinase C (PKC) is a family of serine-threonine kinases that regulate a broad spectrum of cellular functions. The family is composed of nine genes that express structurally related phospholipid-dependent kinases with distinct means of regulation and tissue distribution. Based on their structures and sensitivities to Ca2+ and diacylglycerol (DAG), they have been classified into conventional PKCs (α, β, and γ), novel PKCs (δ, ε, η, and θ), and atypical PKCs (ζ and λ/ι). Mammalian PKC α consists of 672 amino acids and is distributed in all tissues, in contrast to other PKC isotypes whose expression is restricted in the particular tissues. PKC α is activated by a variety of stimuli originating from receptor activation, cell contact and physical stresses. Kinase activity of PKC α is regulated by phosphorylation of three conserved residues in its kinase domain: the activation-loop site Thr-497, the autophosphorylation site Thr-638, and the hydrophobic C-terminal site Ser-657. In some types of cells, PKC α is implicated in cell growth, in contrast, it may play a role in cell cycle arrest and differentiation in other types of cells. The responses are modulated by dynamic interactions with cell-type specific factors. This is a calcium-activated, phospholipid-dependent, serine- and threonine-specific enzyme. May play a role in cell motility by phosphorylating CSPG4. PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters.