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Cycloheximide CulturePure®
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Cycloheximide CulturePure® is a purified version (≥98% pure) of Cycloheximide that is free of toxic isomers. It is a glutarimide antibiotic and natural fungicide isolated from Streptomyces griseus and a protein synthesis inhibitor in eukaryotic cells. It was discovered by Alma Whiffen-Barksdale of Upjohn Company in 1946. It is routinely used as a selection agent in several types of isolation media. It can be used as a tool in molecular biology to determine the half life of proteins, or in in chase experiments to analyze protein degradation.
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Cas Number: 66-81-9
Molecular Formula: C15H23NO4
Molecular Weight: 281.35
Mechanism of Action: Cycloheximide binds to the ribosome and inhibits the eEF2-mediated translocation step in protein synthesis, thus blocking translational elongation.
Storage Conditions: ≤30°C
Spectrum: Cycloheximide is used for fungi and yeast, including fungi found in brewing test media. It has lower activity against bacteria.
Microbiology Applications: Cycoloheximide is routinely used as a selection agent in several types of isolation media:
Columbia Blood Agar - Campylobacter Selective Supplement (Butzler)
Dermasel agar - Selective Supplement for dermatophyte fungi
Campylobacter Agar - Campylobacter Selective Supplement (Preston)
Listeria Selective Agar - Listeria Selective Supplement
Listeria Enrichment Broth - Listeria Selective Enrichment Supplement
Listeria Enrichment Broth - Modified Listeria Selective Enrichment Supplement
STAA Agar - STAA Selective Supplement
Legionella CYE Agar - Legionella GVPC Selective Supplement
Campylobacter Agar - Campylobacter Selective Supplement (Karmali)
Bolton Broth - Bolton Broth Selective Supplement
Representative susceptibility data includes:
- Candida albicans 12.5 µg/ml
- Saccharomyces cerevisiae: 0.2 µg/ml
- Mycosphaerella graminicola: 5.62-100 µg/ml
Source: Streptomyces griseus
Loss on Drying: ≤1.0%
Melting Point: 107-120°C
Identification: HPLC
Potency (on a dry basis): ≥900 u/mg (on dried basis)
Purity Level: (HPLC): ≥95.0%
References: Baliga BS, Pronczuk AW and Munro HN (1969) Mechanism of cycloheximide inhibition of protein synthesis in a cell-free system prepared from rat liver. J Biol Chem. 244(16):4480-4489 PMID 5806588
Doyle SM, Diamond M and McCabe PF (2010) Chloroplast and reactive oxygen species involvement in apoptotic-like programmed cell death in Arabidopsis suspension cultures. J. Exper. Bot 61 (2):473–482 PMID 19933317
Lee S et al (2012) Global mapping of translation initiation sites in mammalian cells at single-nucleotide resolution. Proc Natl Acad Sci USA. 109(37):E2424-32 PMID 22927429
Neeman M and Degani H (1989) Early estrogen-induced metabolic changes and their inhibition by actinomycin D and cycloheximide in human breast cancer cells: 31P and 13C NMR studies. PNAS 86 (14):5585-5589 PMID 2748604
Pajak B, Gajkowska B, Orzechowski A (2005) Cycloheximide-mediated sensitization to TNF-alpha-induced apoptosis in human colorectal cancer cell line COLO 205; role of FLIP and metabolic inhibitors. J. Physiol. Pharmacol.56 (3)101-118. PMID 16077198
Schneider-Poetsch T et al (2009) Inhibition of eukaryotic translation elongation by cycloheximide and lactimidomycin. Nat. Chem. Biol 6: 209-217 PMID 20118940
Cycloheximide from TOKU-E:
Buchanan BW, Lloyd ME, Engle SM, and Rubenstein EM (2016) Cycloheximide chase analysis of protein degradation in Saccharomyces cerevisiae. J. Vis. Exp. (110), e53975
Cycloheximide Solution from TOKU-E:
Jimenez-Moreno N et al (2019) LIR-dependent LMX1A/LMX1B autophagy crosstalk shapes human midbrain dopaminergic neuronal resilience. bioRxiv 636712 link
Dane techniczne
| Opakowanie | 1 g |