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 (alpha, beta, and gamma), novel PKCs (Delta, Epsilon, Eta, and IPA), and atypical PKCs (Zeta and Lambda/Iota). PKC Gamma is a member of the cPKC subfamily which is activated by Ca2+ and diacylglycerol in the presence of phosphatidylserine. Physiologically, PKC Gamma is activated by a mechanism coupled with receptor-mediated breakdown of inositol phospholipid as other cPKC isotypes. PKC Gamma is expressed solely in the brain and spinal cord and its localization is restricted to neurons. Within the brain, PKC Gamma is the most abundant in the cerebellum, hippocampus and cerebral cortex, where the existence of neuronal plasticity has been demonstrated.

Western Blot: 0.2 ?g/ml; Immunoprecipitation: 2.0 ?g;

Type: Primary
Antigen: PRKCG (protein kinase C, gamma)
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: Human, Mouse, Rat