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Human DARS Protein (His Tag)

DatasheetSpecific ReferencesReviewsRelated ProductsProtocols
DARSProtein Product Information
Synonym:DARS
Protein Construction:A DNA sequence encoding the mature form of human DARS (P14868) (Met1-Pro501) was expressed with a polyhistide tag at the N-terminus.
Species:Human
Expressed Host:E. coli
Form & Shipping:In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
DARSProtein QC Testing
Purity:> 90 % as determined by SDS-PAGE
Endotoxin:Please contact us for more information.
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:His
Molecule Mass:The recombinant human DARS consists of 516 amino acids and predicts a molecular mass of 59 KDa. It migrates as an approximately 47 KDa band in SDS-PAGE under reducing conditions.
Formulation:Lyophilized from sterile 50mM Tris, 100mM Nacl, 10% glycerol, pH 8.0
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
DARSProtein Usage Guide
Storage:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
14278-H07E
Background

Aspartate tRNA ligase 1, also known as DARS, is part of a multienzyme complex of aminoacyl-tRNA synthetases. It belongs to the class-II aminoacyl-tRNA synthetase family. DARS charges its cognate tRNA with aspartate during protein biosynthesis. DARS catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid(AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

References
  • Escalante C, et al. (1993) Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix. J Biol Chem. 268(8): 6014-23.
  • Maruyama K, et al. (1994) Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 138(1-2):171-4.
  • Reed VS, et al. (1995) Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha. J Biol Chem. 269(52):32932-6.
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    Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"