Description General description A cell permeable, highly specific inhibitor of protein kinase C (IC50 = 50 nM) that interacts with the protein’s regulatory domain by competing at the binding site of diacylglycerol and phorbol esters. Does not compete with Ca2+ or phospholipids. At higher concentrations inhibits myosin light chain kinase (IC50 > 5 µM), protein kinase A (IC50 > 50 µM), protein kinase G (IC50 > 25 µM), and p60v-src (IC50 > 50 µM). Induces apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells. Requires brief exposure to light for activation. Cell-permeable, highly specific inhibitor of protein kinase C (IC50 = 50 nM) that interacts with the protein′s regulatory domain by competing at the binding site of diacylglycerol and phorbol esters. At higher concentrations inhibits myosin light chain kinase (IC50 > 5 µM), protein kinase A (IC50 > 50 µM), protein kinase G (IC50 > 25 µM), and p60v-src protein tyrosine kinase (IC50 > 50 µM). Does not compete with Ca2+ or phospholipids. Also induces apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells. Inhibition of PKC is dependent on exposure to light in cell-free systems. Ordinary fluorescent light is sufficient for full activation. Packaging 50, 100 μg in Plastic ampoule Biochem/physiol Actions Cell permeable: yes Primary Target PKC Product does not compete with ATP. Reversible: no Target IC50: 50 nM against protein kinase C Warning Toxicity: Standard Handling (A) Reconstitution Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C. Other Notes Jarvis, W.D., et al. 1994. Cancer Res.54, 1707. Svetlov, S., and Nigami, S. 1993. Biochim. Biophys. Acta 1177, 75. Gopalakrishna, R., et al. 1992. FEBS Lett. 314, 149. Shimamato, H., et al. 1992. Br. J. Pharmacol.107, 282. Bruns, R.F., et al. 1991. Biochem. Biophys. Res. Commun.176, 288. Tamaoki, T., et al. 1990. Biotechnology8, 732. Kobayashi, E., et al. 1989. Biochem. Biophys. Res. Commun.159, 548.