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Triacsin C

Acyl-CoA synthetase inhibitor
BML-EI218-0100 100 µg 154.00 USD
BML-EI218-1000 1 mg 671.00 USD
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Replaces Prod. #: ALX-380-285

Analog of polyunsaturated fatty acid. Potent inhibitor of long-chain fatty acyl CoA synthetase. Selectively inhibits arachidonoyl-CoA synthetase in intact cells and the nonspecific acyl-CoA synthetase in cell sonicates IC50=3.6-8.7µM. Inhibits neutrophil functions. Blocks β-cell apoptosis induced by fatty acids (lipoapoptosis) and synthesis of triglycerides, diglycerides and cholesterol esters. Potent vasodilator.

Product Details

Alternative Name:2,4,7-Undecatrienal nitrosohydrazone, 2E,4E,7E-Undecatriene-1-triazene, WS1228A
Purity:≥90% (TLC)
Appearance:Liquid. In DMSO.
Solubility:Soluble in DMSO (25mg/ml) or methanol (5mg/ml).
Shipping:Blue Ice
Long Term Storage:-20°C
Use/Stability:Stable for up to 1 year after receipt when stored at -20°C.
Handling:Protect from light. Keep under inert gas.
Technical Info/Product Notes:Note: Product is not sterile.
Regulatory Status:RUO - Research Use Only
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Product Literature References

Francisella tularensis Exploits AMPK Activation to Harvest Host-Derived Nutrients Liberated from Host Lipolysis: S.R. Dominguez, et al.; Infect. Immun. 90, e0015522 (2022), Abstract;
Syntaxin 17 promotes lipid droplet formation by regulating the distribution of acyl-CoA synthetase 3: H. Kimura, et al.; J. Lipid Res. 59, 805 (2018), Abstract;
Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation: M. To, et al.; Mol. Biol. Cell 28, 270 (2017), Abstract;
Liver Perilipin5 expression worsens hepatosteatosis but not insulin resistance in high fat fed mice: M.B. Trevino, et al.; Mol. Endocrinol. 29, 1414 (2015), Application(s): Cell culture, Abstract; Full Text
CGI-58/ABHD5 is a coenzyme A-dependent lysophosphatidic acid acyltransferase: G. Montero-Moran, et al.; J. Lipid Res. 51, 709 (2010), Abstract;
Inhibition of long-chain acyl coenzyme A synthetases during fatty acid loading induces lipotoxicity in macrophages: V. Saraswathi & A.H. Hasty; Arterioscler. Thromb. Vasc. Biol. 29, 1937 (2009), Abstract;
Anti-atherosclerotic activity of triacsin C, an acyl-CoA synthetase inhibitor: D. Matsuda, et al.; J. Antibiot. (Tokyo) 61, 318 (2008), Abstract;
The effect of fatty acid-CoA ligase 4 on the growth of hepatic cancer cells: C. Hu, et al.; Cancer Biol. Ther. 7, 131 (2008), Abstract;
ADRP/adipophilin is degraded through the proteasome-dependent pathway during regression of lipid-storing cells: Y. Masuda, et al.; J. Lipid Res. 47, 87 (2006), Abstract; Full Text
Triacsin C inhibits the formation of 1H NMR-visible mobile lipids and lipid bodies in HuT 78 apoptotic cells: E. Iorio, et al.; Biochim. Biophys. Acta 1634, 1 (2003), Abstract;
Complete inhibition of mouse macrophage-derived foam cell formation by triacsin C: I. Namatame, et al.; J. Biochem. 125, 319 (1999), Abstract;
Protection against lipoapoptosis of beta cells through leptin-dependent maintenance of Bcl-2 expression: M. Shimabukuro, et al.; PNAS 95, 9558 (1998), Abstract; Full Text
Triacsin C blocks de novo synthesis of glycerolipids and cholesterol esters but not recycling of fatty acid into phospholipid: evidence for functionally separate pools of acyl-CoA: R.A. Igal, et al.; Biochem. J. 324, 529 (1997), Abstract; Full Text
Acylglycerol recycling from triacylglycerol to phospholipid, not lipase activity, is defective in neutral lipid storage disease fibroblasts: R.A. Igal & R.A Coleman; J. Biol. Chem. 271, 16644 (1996), Abstract;
Comparison of the reactivity of tetradecenoic acids, a triacsin, and unsaturated oximes with four purified Saccharomyces cerevisiae fatty acid activation proteins: L.J. Knoll, et al.; J. Biol. Chem. 270, 20090 (1995), Abstract;
Long chain acyl coenzyme A and signaling in neutrophils. An inhibitor of acyl coenzyme A synthetase, triacsin C, inhibits superoxide anion generation and degranulation by human neutrophils: H.M. Korchak, et al.; J. Biol. Chem. 269, 30281 (1994), Abstract;
The acyl-CoA synthetase inhibitor triacsin C enhanced eicosanoid release in leukocytes: S. Oh-ishi, et al.; Jpn. J. Pharmacol. 59, 417 (1992), Abstract; Full Text
Evidence for an essential role of long chain acyl-CoA synthetase in animal cell proliferation. Inhibition of long chain acyl-CoA synthetase by triacsins caused inhibition of Raji cell proliferation: H. Tomoda, et al.; J. Biol. Chem. 266, 4214 (1991), Abstract; Full Text
Triacsin C: a differential inhibitor of arachidonoyl-CoA synthetase and nonspecific long chain acyl-CoA synthetase: E.J. Hartman, et al.; Prostaglandins 37, 655 (1989), Abstract;

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