Protein kinase C delta (PKCδ) is a member of the protein kinase C (PKC) family of serine-threonine kinases. It is a 79 kd protein kinase that shows strict dependence on the presence of phospholipids, but shows no activation by Ca2+ (1). Phosphatidylinositol is the most potent activator of PKC delta. Northern blot analysis indicated that PKCdelta is widely distributed in almost all the tissues and is a major isoform of PKC expressed in hemopoietic cells (2). PKCdelta is involved in fundamental cellular functions regulated by diacylglycerols and mimicked by phorbol esters.
PRKCD; MAY1; MGC49908; nPKC-delta
1. Leibersperger, H. et al: Immunological demonstration of a calcium-unresponsive protein kinase C of the delta-type in different species and murine tissues. Predominance in epidermis. J Biol Chem. 1991 Aug 5;266(22):14778-84.
2. Mischak, H. et al: Mouse protein kinase C-delta, the major isoform expressed in mouse hemopoietic cells: sequence of the cDNA, expression patterns, and characterization of the protein. Biochemistry. 1991 Aug 13;30(32):7925-31.
Sample Kinase Activity Plot. For specific information on a given lot, see related technical data sheet.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability and Shipping:
Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
Yang Weiwei et al., EGFR-Induced and PKCε Monoubiquitylation-Dependent NF-KB Activation Upregulates PKM2 Expression and Promotes Tumorigenesis Molecular Cell November 2012 10.1016/j.molcel.2012.09.028
J Xue et al., Tumour suppressor TRIM33 targets nuclear [beta]-catenin degradation Nature Communications February 2015 10.1038/ncomms7156
Lu Q et al., PKC-delta mediates mineralocorticoid receptor activation by angiotensin II to modulate smooth muscle cell function. Endocrinology August 2019 10.1210/en.2019-00258
E. McAllister Fiona et al., Correlation profiling for determining kinase-substrate relationships Methods March 2013 10.1016/j.ymeth.2013.03.012
M Tandon et al., SD-208, a novel protein kinase D inhibitor, blocks prostate cancer cell proliferation and tumor growth in vivo by inducing G2/M cell cycle arrest. PLoS One March 2015 10.1371/journal.pone.0119346
Sletten Torunn et al., Nucleolin Regulates Phosphorylation and Nuclear Export of Fibroblast Growth Factor 1 (FGF1) PLoS One March 2014 10.1371/journal.pone.0090687
Tandon Manuj et al., New Pyrazolopyrimidine Inhibitors of Protein Kinase D as Potent Anticancer Agents for Prostate Cancer Cells PLoS One September 2013 10.1371/journal.pone.0075601
J. Coultrap Steven et al., Improving a Natural CaMKII Inhibitor by Random and Rational Design PLoS One October 2011 10.1371/journal.pone.0025245
Decornez H?l?ne et al., Design, Selection, and Evaluation of a General Kinase-Focused Library ChemMedChem June 2009 10.1002/cmdc.200900164
Qiu Chen Jin et al., Absolute quantitation of endogenous proteins with precision and accuracy using a capillary Western system Analytical Biochemistry November 2013 10.1016/j.ab.2013.07.022
Bhandaria Deepali et al., Cyclin-dependent kinase 5 activates guanine nucleotide exchange factor GIV/Girdin to orchestrate migration?proliferation dichotomy PNAS July 2015 10.1073/pnas.1514157112
Apoptosis/Autophagy, Cardiovascular Disease, ERK/MAPK Pathway, Neurobiology, NfkB Pathway, PKA/PKC Pathway, Ser/Thr Kinases