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.

• Synonym(s): Calphostin C, Cladosporium cladosporioides, UCN-1028c
• Empirical Formula (Hill Notation): C₄₄H₃₈O₁₄
• CAS Number: 121263-19-2
• Molecular Weight: 790.76
• MDL number: MFCD00133155
• UNSPSC Code: 12352200

Properties

• Quality Level: 100
• 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
• 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

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 p60^v-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 p60^v-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.

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.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Safety Information

• Storage Class Code: 11 - Combustible Solids
• WGK: WGK 3
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable