Protein kinase CβII isozyme human 

One unit will transfer 1 nmol of phosphate to histone H3 in 1 min at pH 7.4 at 30 °C.

Solution in 20 mM HEPES, pH 7.4; 2 mM EDTA, 2 mM EGTA, 5 mM DTT, 100 mM NaCl, 0.05% Triton X-100, and 50% glycerol.

Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP₂) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca²⁺ and phospholipid and include PKCα, βI, βII, and γ. Members of the second family are phospholipid-dependent but Ca²⁺-independent, and include PKCδ, ε, η, and θ. Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and ι.
Phosphorylation appears to be an important mechanism of regulation of all PKCs. PKC plays a role in the regulation of cell transformation, growth, differentiation, ruffling, vesicle trafficking, apoptosis and gene expression.

expressed in baculovirus infected insect cells

>95% (SDS-PAGE)

buffered aqueous glycerol solution

calculated mol wt 76.9 kDa

mol wt 80 kDa by SDS-PAGE

human ... PRKCB1(5579)

dry ice

−70°C

Newton, A.C., Protein kinase C: structure, function, and regulation. J. Biol. Chem. 270, 28495, (1995)

Hall, J.L., et al., Hyperglycemia inhibits vascular smooth muscle cell apoptosis through a protein kinase C-dependent pathway. Circ. Res. 87, 574, (2000)

Patel, N.A., et al., Insulin regulates alternative splicing of protein kinase C beta II through a phosphatidylinositol 3-kinase-dependent pathway involving the nuclear serine/arginine-rich splicing factor, SRp40, in skeletal muscle cells. . J. Biol. Chem. 276, 22648, (2001)

Kawano, Y., et al., Changes in glucose transport and protein kinase Cbeta(2) in rat skeletal muscle induced by hyperglycaemia. . Diabetologia 42, 1071, (1999)

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