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Members of the Protein kinase C (PKC) family of serine/threonine protein kinases are grouped by their activation mechanism. Classical or conventional PKCs (PKC alpha-, betaI- , betaII- and gamma-) are activated by phosphatidylserine in a calcium dependent manner and can bind diacylglycerol. The Ca2+ insensitive novel PKCs (PKCs epsilon-, delta-, theta- and eta) are also activated by diacylglycerol and phosphatidylserine. The atypical PKCs (PKCs iota- and zeta-) are insensitive to Ca2+, DAG and phorbolesters. All PKCs isoforms consist of a highly conserved catalytic domain connected to a regulatory domain via a hinge region. PKCs are involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascades involving MAPK1/3 (ERK1/2) and RAP1GAP.
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