|Related Categories||Alphabetical Index, Antibodies, Antibodies for Cell Biology, Antibodies for Kinase/Phosphatase Biology, Antibodies in Array,|
|species reactivity||rat, mouse|
|western blot: 1:20,000 using mouse NIH 3T3 fibroblast lysate|
|western blot: 1:50,000 using rat brain extract|
|antibody form||whole antiserum|
|mol wt||antigen mol wt 80 kDa|
|contains||15 mM sodium azide|
|shipped in||dry ice|
mouse ... Prkca(18750)|
rat ... Prkca(24680)
Synthetic peptide corresponding to amino acids 659-672 from the C-terminal variable (V5) region of rat PKC α conjugated to KLH.
synthetic peptide corresponding to amino acids 659-672 from the C-terminal variable (V5) region of rat PKCα.
PKC α is a conventional isoform of Protein Kinase C (76-93 kD) and a member of serine/threonine (Ser/Thr) protein kinases. It is expressed ubiquitously in tissues and is the major isoform of PKC in fibroblasts. Stimulation and overexpression of PKC α increases the growth rate of cells in culture4. Anti-Protein Kinase C α antibody is useful for studying expression of PKC α in normal and neoplastic tissues. It is also useful for detecting PKC α isoenzyme in brain tissue and cell extracts. Furthermore, it can be used in chemiluminescence detection systems to detect PKC α. Rabbit anti-protein kinase c α antibody reacts specifically with PKC α (80 kD) of rat brain extract or NIH3T3 mouse fibroblast lysate.
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 α antibody specifically recognises PKC α (80 kDa). A faint band at 45 kDa may be observed.
Anti-Protein Kinase C α may be used for detection in rat brain extract and mouse NIH 3T3 fibroblast lysate by immunoblotting at a working dilution of 1:50,000-1:20,000. Detection by immunoblotting is also possible in baby hamster kidney cells (1:10000) 1 and in common voles 2. Detection by immunohistochemistry in retinal sections of European moles is possible at a working dilution of 1:10000 3. The antibody is also suitable for protein microarray.
Anti-protein kinase c α antibody can be used in immunohistochemical staining and microarray assays. It can also be used in immunoblotting1 and western blotting.
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Keywords: Buffers, Cell biology, Epigenetics, Immunohistochemistry, Immunoprecipitation, Molecular biology, Neuroscience, Western blot
2. Not only vasopressin, but also the intracellular messenger protein kinase Ca in the suprachiasmatic nucleus correlates with expression of circadian rhythmicity in voles Jansen K et al Neuropeptides 37, 57-65, (2003)
3. Cone photoreceptors and potential UV vision in a subterranean insectivore, the European mole Glösmann M et al J. Vis. 8, 1-12, (2008)
Near Complete Loss Of Retinal Ganglion Cells In The Math5/brn3b Double Knockout Elicits Severe Reductions Of Other Cell Types During Retinal Development. Moshiri, A., et al. Dev. Biol. 316, 214-27, (2008)
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