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Elongation factor G inhibitor
ALX-380-261-G001 1 g 129.00 USD
ALX-380-261-G005 5 g 503.00 USD
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Thiazole-containing peptide antibiotic. Inhibits protein synthesis by preventing binding of GTP to the 50S ribosomal subunit. Inhibits binding of elongation factor G (EF-G) and the dissociation of EF-G from the ribosome.

Product Details

Source:Isolated from Streptomyces azureus.
MI:14: 9364
Appearance:White to off-white solid.
Activity:≥900 U/mg
Solubility:Soluble in acetic acid, DMSO (10mg/ml) or dimethyl formamide; insoluble in water.
Shipping:Ambient Temperature
Long Term Storage:-20°C
Handling:Protect from light and moisture.
Regulatory Status:RUO - Research Use Only
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Product Literature References

Effects of thiostrepton alone or in combination with selumetinib on triple-negative breast cancer metastasis: F.D. Korkmaz, et al.; Mol. Biol. Rep. 49, 10387 (2022), Abstract;
In vivo assembling of bacterial ribosomal protein L11 into yeast ribosomes makes the particles sensitive to the prokaryotic specific antibiotic thiostrepton: A. Garcia-Marcos, et al.; Nucl. Acids Res. 35, 7109 (2007), Abstract; Full Text
Interaction of thiostrepton and elongation factor-G with the ribosomal protein L11-binding domain: W.S. Bowen, et al.; J. Biol. Chem. 280, 2934 (2005), Abstract; Full Text
Interactions of the N-terminal domain of ribosomal protein L11 with thiostrepton and rRNA: S.L. Bausch, et al.; J. Biol. Chem. 280, 29956 (2005), Abstract; Full Text
Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome: M.V. Rodnina, et al.; PNAS 96, 9586 (1999), Abstract; Full Text
The antibiotics micrococcin and thiostrepton interact directly with 23S rRNA nucleotides 1067A and 1095A: G. Rosendahl & S. Douthwaite; Nucl. Acids Res. 22, 357 (1994), Abstract; Full Text
Characterization of an 8.7-kilobase thiostrepton resistance-encoding plasmid (pGIF3) of Streptomyces incarnatus: H. Malina & M. Robert-Gero; Appl. Environ. Microbiol. 58, 895 (1992), Abstract; Full Text
Alpha-sarcin cleavage of ribosomal RNA is inhibited by the binding of elongation factor G or thiostrepton to the ribosome: S.P. Miller & J.W. Bodley; Nucl. Acids Res. 19, 1657 (1991), Abstract; Full Text
Recognition of the highly conserved GTPase center of 23 S ribosomal RNA by ribosomal protein L11 and the antibiotic thiostrepton: P.C. Ryan, et al.; J. Mol. Biol. 221, 1257 (1991), Abstract;
Similarities and differences in the inhibition patterns of thiostrepton and viomycin: evidence for two functionally different populations of P sites when occupied with AcPhe-tRNA: U.R. Kutay, et al.; Biochim. Biophys. Acta 1050, 193 (1990), Abstract;
Studies on translocation. VI. Thiostrepton prevents the formation of a ribosome-G factor-guanine nucleotide complex: J.W. Bodley, et al.; BBRC 41, 1406 (1970), Abstract;