Human DARS Protein (His Tag)

aspRS,HBSL

• 100ug (NPP2069) Please inquiry

Catalog Number	P14278-H07E
Organism Species	Human
Host	E. coli
Synonyms	aspRS,HBSL
Molecular Weight	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.
predicted N	His
SDS-PAGE
Purity	> 90 % as determined by SDS-PAGE
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.
Bio-activity
Research Area	Epigenetics |DNA / RNA |Translation |tRNA synthetase
Formulation	Lyophilized from sterile 50mM Tris, 100mM Nacl, 10% glycerol, pH 8.0 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
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.
Reference	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.