Protein Kinase C (PKC, 76-93 kD) is a family of Ser/Thr specific protein kinases that perform key functions in numerous signalling pathways, in biological systems, through their various isoforms. The conventional PKC isoforms (cPKC) are PKC-α, β1, β2 and γ; activated by phosphatidylserine, calcium or phorbol esters. Proteolysis of PKC in vivo is thought to be mediated by calpains I and II. Calpains cleave PKC in the V3 hinge region to produce two distinct fragments, one comprising the N-terminal regulatory domain (30 kD) and the other fragment containing the C-terminal kinase domain (50 kD) that is catalytically active. Multiple functions such as, cellular and vascular regulations, angiogenesis, cell growth, apoptosis, changes in basement membrane thickness, extracellular matrix organisation, MAPK signalling, are attributed to PKC isoforms. These varied functions implicate PKC isoforms in cardiac hypertrophies and diabetic nephropathy and cardiovascular complications. Anti-Protein Kinase C β2 antibody specifically recognises PKC β2 (80 kDa).
Immunogen
synthetic peptide corresponding to amino acid residues 654-665 from human PKCβ2.
Application
Anti-Protein Kinase C β2 antibody may be used for detection by immunoblotting at a working concentration of 2μg/mL.
Physical form
Solution in phosphate buffered saline containing 1.0 mg/mL BSA and 0.05% sodium azide.
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