208725
Calphostin C, Cladosporium cladosporioides
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.
别名:
Calphostin C, Cladosporium cladosporioides, UCN-1028c
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关于此项目
Assay:
≥95% (HPLC)
Form:
lyophilized solid
Quality level:
Storage condition:
OK to freeze
protect from light
protect from light
产品名称
Calphostin C, Cladosporium cladosporioides, 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.
InChI
1S/C44H38O14/c1-20(56-43(50)22-10-8-7-9-11-22)16-25-31-32-26(17-21(2)57-44(51)58-24-14-12-23(45)13-15-24)42(55-6)40(49)34-28(47)19-30(53-4)36(38(32)34)35-29(52-3)18-27(46)33(37(31)35)39(48)41(25)54-5/h7-15,18-21,45,48-49H,16-17H2,1-6H3
InChI key
LSUTUUOITDQYNO-UHFFFAOYSA-N
assay
≥95% (HPLC)
form
lyophilized solid
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
protect from light
color
light brown
solubility
DMSO: 1 mg/mL
ethanol: soluble
shipped in
ambient
storage temp.
2-8°C
Quality Level
Biochem/physiol Actions
Cell permeable: yes
Primary Target
PKC
PKC
Product does not compete with ATP.
Reversible: no
Target IC50: 50 nM against protein kinase C
Disclaimer
Toxicity: Standard Handling (A)
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.
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.
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.
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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