A3646
Aminoacyl-tRNA Synthetase from Escherichia coli
buffered aqueous glycerol solution, ≥2,000 units/mg protein
Synonym(s):
ARS, tRNA-ligase
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About This Item
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form
buffered aqueous glycerol solution
Quality Level
specific activity
≥2,000 units/mg protein
shipped in
wet ice
storage temp.
−20°C
Application
Aminoacyl tRNA synthetase may be useful in the study of protein synthesis and regulation .
Biochem/physiol Actions
Aminoacyl tRNA synthetase attaches amino acids to their corresponding tRNA, which is essential for protein synthesis. Both classes of aminoacyl tRNA synthetases are multi-domain proteins .
Other Notes
Mixture of amino acid activating enzymes
EC Ligase sub-class 6.1.1
Quality
Crude
Unit Definition
One unit will activate and attach 1.0 picomole (10-12 mole) of labeled amino acid to tRNA in 10 min at pH 7.6 at 37 °C (amino acid used: L-arginine).
Physical form
Solution in 50% glycerol containing 10 mM Tris HCl, pH 7.2, 10 mM MgCl2, 30 mM 2-mercaptoethanol and 10 mM KCl
Analysis Note
Protein determined by biuret.
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Skin Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Regulatory Information
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C L Harris
Journal of bacteriology, 169(6), 2718-2723 (1987-06-01)
Aminoacyl-tRNA synthetases from several strains of Escherichia coli are shown to elute as a high-molecular-weight complex on 6% agarose columns (Bio-Gel A-5M). In contrast, very little synthetase activity was observed in such complexes on Sephadex G-200 columns, suggesting that these
Irem Avcilar-Kucukgoze et al.
Cell chemical biology, 27(7), 839-849 (2020-06-20)
Arginyltransferase ATE1 mediates posttranslational arginylation and plays key roles in multiple physiological processes. ATE1 utilizes arginyl (Arg)-tRNAArg as the donor of Arg, putting this reaction into a direct competition with the protein synthesis machinery. Here, we address the question of
C R Woese et al.
Microbiology and molecular biology reviews : MMBR, 64(1), 202-236 (2000-03-08)
The aminoacyl-tRNA synthetases (AARSs) and their relationship to the genetic code are examined from the evolutionary perspective. Despite a loose correlation between codon assignments and AARS evolutionary relationships, the code is far too highly structured to have been ordered merely
Ziwei Liu et al.
PLoS genetics, 17(7), e1009675-e1009675 (2021-07-30)
Emerging evidence indicates that tRNA-derived small RNAs (tsRNAs) are involved in fine-tuning gene expression and become dysregulated in various cancers. We recently showed that the 22nt LeuCAG3´tsRNA from the 3´ end of tRNALeu is required for efficient translation of a
Lance W Rider et al.
The Journal of biological chemistry, 284(16), 10324-10333 (2009-01-14)
Dihydrouridine synthases (DUSs) are flavin-dependent enzymes that catalyze site-specific reduction of uracils in tRNAs. The mechanism of DUS 2 from Saccharomyces cerevisiae was studied. Previously published turnover rates for this DUS were very low. Our studies show that the catalytic
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