Protein Kinase C (PKC)

Sino Biological provides a comprehensive set of tools for protein kinase C (PKC) related studies, including proteins, antibodies (rabbit mAbs, mouse mAbs, and rabbit pAbs), ELISA kits, and ORF cDNA clones. Protein kinase C (PKC) is a family of serine/threonine protein kinases, which play important roles in several signal transduction cascades. Over ten isozymes of protein kinase C (PKC) are divided into three subfamilies, based on their second messenger requirements: conventional (or classical), novel, and atypical. Conventional protein kinase C isozymes require Ca²⁺, diacylglycerol (DAG), and a phospholipid such as phosphatidylserine for activation. Novel protein kinase C isozymes require DAG, but do not require Ca²⁺ for activation. However, atypical protein kinase C isozymes require neither Ca²⁺ nor DAG for activation.

Protein Kinase C (PKC) Products

• PKC alpha
• PKC epsilon
• PKC nu / PRKD3
• PKC beta
• PKC gamma
• PKC zeta
• PKC delta
• PKC iota

Protein Kinase C (PKC) Background

Protein kinase C (PKC) is a family of serine/threonine protein kinases, which play important roles in several signal transduction cascades. The ten isozymes of protein kinase C (PKC) are divided into three subfamilies, based on their second messenger requirements: conventional (or classical), novel, and atypical. The protein kinase C (PKC) family occupies the tip of a branch of the AGC kinases from which the related kinases protein kinase N (PKN), Akt/PKB, p70 S6 kinase, and the phosphoinositide-dependent kinase-1 (PDK-1) diverge. At the very tip of the branch are the four conventional isozymes: PKCα (the first protein kinase C isozyme cloned), the alternatively spliced PKCβI and PKCβII and PKCγ; next are the four novel isozymes, PKCδ, PKCε, PKCη, and PKCθ; closest to the point of divergence are the atypical isozymes PKCζ and PKCι (human; murine isozyme is PKCλ). Conventional protein kinase C isozymes require Ca²⁺, diacylglycerol (DAG), and a phospholipid such as phosphatidylserine for activation. Novel protein kinase C isozymes require DAG, but do not require Ca²⁺ for activation. However, atypical protein kinase C isozymes require neither Ca²⁺ nor DAG for activation.

The structure of all protein kinase C (PKC) consists of a regulatory domain and a catalytic domain tethered together by a hinge region. The catalytic region is highly conserved among the different isoforms, as well as, to a lesser degree, among the catalytic region of other serine/threonine kinases. The second messenger requirement differences in the isoforms are a result of the regulatory region, which are similar within the classes, but differ among them.

Protein Kinase C (PKC) Related Studies

1. Nishizuka Y (1995) Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9 (7): 484–96.
2. Mellor H, et al. (1998) The extended protein kinase C superfamily. Biochem. J. 332 (Pt 2): 281–92.
3. Reyland ME. (2009) Protein kinase C isoforms: Multi-functional regulators of cell life and death. Front Biosci. 14:2386-99.
4. Newton AC. (2010) Protein kinase C: poised to signal. Am J Physiol Endocrinol Metab. 298(3):E395-402.