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 recognizes an epitope located within the amino acid residues 660-673 at the C-terminal variable (V5) region of PKCβ2 (80 kDa).
Specificity
The antibody shows no cross-reactivity with PKC peptides corresponding to C-terminal sequences from PKC β1 (658-671) and PKC γ (684-697) conjugated to BSA.
Immunogen
synthetic peptide corresponding to the C-terminal variable (V5) region (amino acids 660-673) of PKC β2.
Application
Anti-Protein Kinase C β2 antibody may be used for immunoblotting at a working dilution of 1:8000 using rat brain cytosolic extract. It is suitable for protein microarray.
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Protein kinase Calpha (PKCalpha) has been implicated in cancer, but the mechanism is largely unknown. Here, we show that PKCalpha promotes head and neck squamous cell carcinoma (SCCHN) by a feed-forward network leading to cell cycle deregulation. PKCalpha inhibitors decrease
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Diabetic nephropathy (DN) has emerged as the major causative pathology in patients entering end-stage renal disease (ESRD) worldwide and it is responsible for 30-40% of all ESRD cases. Treatments for DN are centered on control of hyperglycemia and blood pressure
Domain interactions in protein kinase C.
C J Pears et al.
Journal of cell science, 100 ( Pt 4), 683-686 (1991-12-01)
Journal of molecular and cellular cardiology, 51(4), 479-484 (2010-11-03)
Cardiac hypertrophy is a complex adaptive response to mechanical and neurohumoral stimuli and under continual stressor, it contributes to maladaptive responses, heart failure and death. Protein kinase C (PKC) and several other kinases play a role in the maladaptative cardiac
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