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 |
|
Formula: | C44H38O14 |
|
MW: | 790.8 |
|
CAS: | 121263-19-2 |
|
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;