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Merck

SBR00022

Sigma-Aldrich

Blasticidin S Ready Made Solution

10 mg/mL (20 mM HEPES), 0.22 μm filtered

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About This Item

Fórmula empírica (notación de Hill):
C17H27N8O5Cl
Peso molecular:
458.90
UNSPSC Code:
12352106
NACRES:
NA.76

Quality Level

sterility

0.22 μm filtered

assay

≥98% (HPLC)

form

liquid

concentration

10 mg/mL (20 mM HEPES)

color

colorless to faint yellow

antibiotic activity spectrum

fungi

mode of action

protein synthesis | interferes

storage temp.

−20°C

SMILES string

CN(CCC(CC(=O)NC1C=CC(OC1C(=O)O)N2C=CC(=NC2=O)N)N)C(=N)N.Cl

InChI

1S/C17H26N8O5.ClH/c1-24(16(20)21)6-4-9(18)8-12(26)22-10-2-3-13(30-14(10)15(27)28)25-7-5-11(19)23-17(25)29;/h2-3,5,7,9-10,13-14H,4,6,8,18H2,1H3,(H3,20,21)(H,22,26)(H,27,28)(H2,19,23,29);1H

InChI key

YQXYQOXRCNEATG-UHFFFAOYSA-N

General description

Blasticidin S, originally isolated from S. griseochromogenes, is a bacterial metabolite renowned for its antibacterial and fungicidal activities. This compound serves as a potent inhibitor of protein synthesis, exhibiting activity against various microorganisms, including bacteria (B. subtilis, S. lutea, E. coli, P. fluorescens, and M. tuberculosis), tumor cell lines, and nematodes.

In research, Blasticidin S has become a valuable tool, notably as a marker for strain manipulations. Recent applications involve the use of Blasticidin S as a selection agent for cells carrying plasmids conferring blasticidin resistance. The resistance is mediated by the blasticidin S deaminase genes (bsr from Bacillus cereus or BSD from Aspergillus terreus). These genes produce enzymes that catalyze the hydrolytic deamination of the cytosine moiety in blasticidin S, leading to the formation of a non-toxic deaminohydroxy derivative. This resistance mechanism is crucial in various studies involving genetic manipulations and selections in cell biology and biochemical research.

Application

Blasticidin S has been:
  • studies to have fungicidal properties and prevents rice blast disease.
  • used as a selection agent for transformed cells that contain the resistance genes bls, bsr, or bsd. Blasticidin S has been used to select HEK293-T cells with TLR-2 constructs and HEK-D5 cells.
  • used to study protein synthesis at the level of peptide bond formation.

Biochem/physiol Actions

Mode of Action: It inhibits protein synthesis in bacteria and eukaryotes. Blasticidin S inhibits hydrolysis of peptidyl-tRNA induced by release factors. It enhances the binding of tRNA to the large subunit of ribosomes and to an extent inhibits peptide bond formation.

Antimicrobial Spectrum: Active against mycobacteria, several Gram-positive and Gram-negative bacteria

Features and Benefits

  • High-quality antibiotic suitable for multiple research applications
  • Ideal for Cell Biology and Biochemical research

Other Notes

For additional information on our range of Biochemicals, please complete this form.

pictograms

Skull and crossbones

signalword

Danger

hcodes

Hazard Classifications

Acute Tox. 3 Oral

Storage Class

6.1D - Non-combustible acute toxic Cat.3 / toxic hazardous materials or hazardous materials causing chronic effects

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Understanding the mechanisms of inhibitors of translation termination may inform development of new antibacterials and therapeutics for premature termination diseases. We report the crystal structure of the potent termination inhibitor blasticidin S bound to the ribosomal 70S•release factor 1 (RF1)
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Journal of inorganic biochemistry, 127, 73-78 (2013-07-25)
Blasticidin S is a representative of the aminoacylnucleoside class of antibiotics and it possesses fungicidal properties against the virulent fungus which causes a serious rice blast disease in Asia. It is widely used to control rice blast by foliar application
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Proceedings of the National Academy of Sciences of the United States of America, 110(30), 12283-12288 (2013-07-05)
The antibiotic blasticidin S (BlaS) is a potent inhibitor of protein synthesis in bacteria and eukaryotes. We have determined a 3.4-Å crystal structure of BlaS bound to a 70S⋅tRNA ribosome complex and performed biochemical and single-molecule FRET experiments to determine

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