Online Purchasing Account You are logged on as Guest. LoginRegister a New AccountShopping cart (Empty)
United States 

Calphostin C

PKC inhibitor
BML-EI198-0100 100 µg 145.00 USD
Do you need bulk/larger quantities?
Replaces Prod. #: ALX-350-027

Potent and selective inhibitor of the protein kinase C (PKC). Inhibition is via interaction with the regulatory DAG binding site and phorbol ester binding site. Inhibition of PKC has been found to be light dependent. At higher concentrations inhibits myosin light chain kinase, cAMP-dependent protein kinase, protein kinase G, pp60v-src protein tyrosine kinase and DAG kinase. It also inhibits Phospholipase D1 and D2. Induces apoptotic DNA fragmentation and cell death. Kills breast cancer cells.

Has antiviral potential. Inhibits cardiac L-type Ca2+ channels. Cell permeable. Inhibits cell proliferation of malignant glioma cells in light-treated conditions in vitro.

Product Details

Alternative Name:UCN-1028C
Purity:≥95% (HPLC)
Appearance:Dark red solid.
Solubility:Soluble in ethanol, methanol, DMF or DMSO. Poor water solubility.
Shipping:Ambient Temperature
Long Term Storage:-20°C
Use/Stability:Stable for at least 1 year after receipt when stored, as supplied, at 0-4°C. Stock solutions are stable for up to 3 months at -20°C.
Handling:Protect from light.
Regulatory Status:RUO - Research Use Only
Please mouse over

Product Literature References

KCNQ1 is internalized by activation of α1 adrenergic receptors: K. Kurakami, et al.; Biochem. Pharmacol. 169, 113628 (2019), Abstract;
Pathobiology of renal-specific oxidoreductase/myo-inositol oxygenase in diabetic nephropathy: its implications in tubulointerstitial fibrosis: P. Xie, et al.; Am. J. Physiol. Renal Physiol. 298, F1393 (2010), Abstract; Full Text
Potent killing of paclitaxel- and doxorubicin-resistant breast cancer cells by calphostin C accompanied by cytoplasmic vacuolization: B. Guo, et al.; Breast Cancer Res. Treat. 82, 125 (2003), Abstract;
Potent direct inhibition of mammalian phospholipase D isoenzymes by calphostin-c: V.A. Sciorra, et al.; Biochemistry 40, 2640 (2001), Abstract;
Pharmacokinetic features and metabolism of calphostin C, a naturally occurring perylenequinone with antileukemic activity: C.L. Chen, et al.; Pharm. Res. 16, 1003 (1999), Abstract;
Calphostin C, a widely used protein kinase C inhibitor, directly and potently blocks L-type Ca channels: H.C. Hartzell & A. Rinderknecht; Am. J. Physiol. 270, C1293 (1996), Abstract;
Growth inhibition of herpes simplex virus-type 1 in calphostin C-treated astrocytes: C.G. Castagnino, et al.; Intervirology 38, 332 (1995), Abstract;
Inhibition of diacylglycerol kinase by the antitumor agent calphostin C. Evidence for similarity between the active site of diacylglycerol kinase and the regulatory site of protein kinase C: C. Redman, et al.; Biochem. Pharmacol. 50, 235 (1995), Abstract;
Induction of apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells by pharmacological inhibitors of protein kinase C: W.D. Jarvis, et al.; Cancer Res. 54, 1707 (1994), Abstract;
Calphostin C, a specific protein kinase C inhibitor, activates human neutrophils: effect on phospholipase A2 and aggregation: S. Svetlov and S. Nigam; Biochim. Biophys. Acta 1177, 75 (1993), Abstract;
Irreversible oxidative inactivation of protein kinase C by photosensitive inhibitor calphostin C: R. Gopalakrishna, et al.; FEBS Lett. 314, 149 (1992), Abstract;
Inhibition of protein kinase C by calphostin C is light-dependent: R.F. Bruns, et al.; BBRC 176, 288 (1991), Abstract;
Potent and specific inhibitors of protein kinase C of microbial origin: T. Tamaoki and H. Nakano; Biotechnology 8, 732 (1990), Abstract;
Calphostin C (UCN-1028C), a novel microbial compound, is a highly potent and specific inhibitor of protein kinase C: E. Kobayashi, et al.; BBRC 159, 548 (1989), Abstract;
Calphostins (UCN-1028), novel and specific inhibitors of protein kinase C. I. Fermentation, isolation, physico-chemical properties and biological activities: E. Kobayashi, et al.; J. Antibiot. 42, 1470 (1989), Abstract;
Calphostins, novel and specific inhibitors of protein kinase C. II. Chemical structures: T. Iida, et al.; J. Antibiot. 42, 1475 (1989), Abstract;

Related Literature

Integrated solutions for screening Wnt regulators
Integrated solutions for screening Wnt regulators
Download as PDF

Download as PDF

Stem Cells
Stem Cells
Download as PDF

All new literature pieces