pQE30-N-Catalytic Domain Histidyl-tRNA Synthetase (E. coli) w/6x His-tag

This plasmid expresses the 320-residue N-terminal catalytic fragment of Histidyl-tRNA Synthetase from E. coli and contains a N-terminal 6x polyhistidine-tag. It catalyzes both the specific aminoacylation of tRNA and pyrophosphate exchange and shows no mischarging of noncognate tRNAs. Size exclusion chromatography showed that it is monomeric, indicating that the C-terminal domain is essential for maintaining the dimeric structure of the enzyme.

Histidyl-tRNA synthetases attach amino acids to the 3' ends of their cognate transfer RNAs in a two-step reaction catalyzed by ATP. The accuracy of this reaction is crucial for the overall fidelity of protein synthesis.

From the laboratory of Christopher S. Francklyn, PhD, University of Vermont.

The Investigator's AnnexePart of The Investigator's Annexe program.

Catalog Number Product Size AVAILABILITY Price Qty
EVM106
pQE30-N-Catalytic Domain Histidyl-tRNA Synthetase (E. coli) w/6x His-tag
Spotted on filter paper In stock
Regular Price:$525.00
Specifications

Product Type: Plasmid
Gene/insert name: N-catalytic domain of E.coli Histidyl-tRNA synthetase
Antibiotic Resistance: Ampicillin
Fusion Tag(s): N-terminal 6x His tag
Grow in E. coli at 37 C: Yes
Selectable markers: Ampicillin
Cloning Site 5': BamHI
Cloning Site 3': HindIII
Insert Size: 960 bp
Vector Backbone and Size: pQE30, 3462 bp
High or low copy: High
Shipped: Ambient temperature (Liquid plasmid DNA in water for domestic orders, spotted on filter paper for international orders)

Provider
From the laboratory of Christopher S. Francklyn, PhD, University of Vermont.
References
  1. Augustine, J., Francklyn, C., Design of an Active Fragment of a Class II Aminoacyl-tRNA Synthetase and Its Significance for Synthetase Evolution. Biochemistry, 36:12, 3473-3482, (1997).

If you publish research with this product, please let us know so we can cite your paper.

Loading...