Cycloheximide | CAS 66-81-9 | Gene Selection Antibiotics | AG Scientific, Inc.

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  • CAS: 66-81-9
  • Formula: C15H23NO4
  • MW: 281.35 Da
  • Appearance: White or cream color powder
  • Purity: ≥95.0%




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Cycloheximide is an antibiotic active against many yeasts and fungi. Inhibits protein synthesis in eukaryotes (but not in prokaryotes) by interfering with the translocation step. It inhibits chain initiation as well as chain elongation by acting on the 60S subunit of the eukaryote ribosome, interacting directly with enzyme translocase. Cycloheximide is used as an inhibitor to study cell-free protein biosynthesis in eukaryotes and also used to block ribosome-dependent in vivo polypeptide synthesis. It induces apoptosis in a variety of cells, but can also delay or inhibit apoptosis by other agents.

Cycloheximide’s longstanding application as a gene selection antibiotic has a powerful new role in Genome editing utilizing the CRISPR/Cas9 systemA Candida albicans CRISPR system permits genetic engineering of essential genes and gene families.

Cycloheximide is in stock. Call for bulk quotations, typical lead for subdivision, packing and shipping larger quantities is 7-14 days.
Research size order 100mg 250mg lead is shorter.

Additional Information

SynonymsActidione, Naramycin A, NSC-185, U-4527, 3-[2-(3,5-Dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]glutarimide
Product #C-1189
CAS #66-81-9
Chemical Name3-[2-(3,5-Dimethyl-2-oxocyclohexyl)-2-hydroxyethyl]glutarimide
MW281.35 Da
AppearanceWhite or cream color powder
SolubilitySoluble in Chloroform, Ethanol and Methanol
PreparationStore solutions at -20°C
Storage TempStore desiccated at +4°C
Therapeutic AreaInfectious diseases
UseCycloheximide is a highly effective antibiotic with activity against mold, yeast, and phytopathogenic fungi, with lower activity against bacteria.

Additional Information

MDL NumberMFCD00082346

Additional Information

GHS Pictograms
UN #'SUN 2811
HandlingWarning: Toxic. Wear gloves and mask when handling. Avoid contact by all means of exposure. Store in a tightly-sealed vial.

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msds 1C-1189, Cycloheximide, SDS, diamond format.pdf
Certificate of Analysis 1C-1189, J1235.pdf
Certificate of Analysis 2C-1189, J1000.pdf
Certificate of Analysis 3C-1189, H1121.pdf
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Citationsvan Galen, Josse, et al. "Sphingomyelin homeostasis is required to form functional enzymatic domains at the trans-Golgi network." J Cell Biol 206.5 (2014): 609-618.
Simpson-Lavy, Kobi J., and Mark Johnston. "SUMOylation regulates the SNF1 protein kinase." Proceedings of the National Academy of Sciences (2013): 201304839.
Miller, William P., et al. "The translational repressor 4E-BP1 contributes to diabetes-induced visual dysfunction." Investigative ophthalmology & visual science 57.3 (2016): 1327-1337.
Lee, Chang-Woo, et al. "Pellino 1 Communicates Intercellular Signaling in Chronic Skin Inflammatory Microenvironment." bioRxiv (2018): 334433.
Cokol, Murat, et al. "Systematic exploration of synergistic drug pairs." Molecular systems biology 7.1 (2011): 544.\n
Kimball, Scot R., et al. "Rapid turnover of the mTOR complex 1 (mTORC1) repressor REDD1 and activation of mTORC1 signaling following inhibition of protein synthesis." Journal of Biological Chemistry 283.6 (2008): 3465-3475.
Pursell, Natalie W., et al. "Solubility-Promoting Function of Hsp90 Contributes to Client Maturation and Robust Cell Growth." Eukaryotic Cell, vol. 11, no. 8, 2012, pp. 1033-1041., doi:10.1128/ec.00099-12.
ReferenceVyas, Valmik K., M. Inmaculada Barrasa, and Gerald R. Fink. "A Candida albicans CRISPR system permits genetic engineering of essential genes and gene families." Science advances 1.3 (2015): e1500248.
INFLAMMATION:\n IL-27 Activates Human Monocytes via STAT1 and Suppresses IL-10 Production but the Inflammatory Functions of IL-27 Are Abrogated by TLRs and p38\n George D. Kalliolias and Lionel B. Ivashkiv\n J. Immunol., May 2008; 180: 6325 - 6333.
PROTEIN SYNTHESIS, POST-TRANSLATIONAL MODIFICATION, AND DEGRADATION:\n Rapid Turnover of the mTOR Complex 1 (mTORC1) Repressor REDD1 and Activation of mTORC1 Signaling following Inhibition of Protein Synthesis\n Scot R. Kimball, A. N. Dang Do, Lydia Kutzler, Douglas R. Cavener, and Leonard S. Jefferson\n J. Biol. Chem., Feb 2008; 283: 3465 - 3475.

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