Reactive species
Human;Mouse
Gene Name
EPRS GLNS PARS QARS QPRS PIG32
Protein name
Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) (Cell proliferation-inducing gene 32 protein) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthe
Immunogen
Synthesized peptide derived from part region of human protein
Specificity
SYEP Monoclonal Antibody detects endogenous levels of protein.
Constitute
Liquid in PBS containing 50% glycerol, and 0.02% sodium azide.
Source
Monoclonal, Mouse,IgG
Dilution rate
WB 1:500-2000
Purification process
The antibody was affinity-purified from mouse antiserum by affinity-chromatography using epitope-specific immunogen.
Background
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a multifunctional aminoacyl-tRNA synthetase that catalyzes the aminoacylation of glutamic acid and proline tRNA species. Alternative splicing has been observed for this gene, but the full-length nature and biological validity of the variant have not been determined. [provided by RefSeq, Jul 2008],
Function
catalytic activity:ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).,catalytic activity:ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).,caution:Was originally thought to be a glutaminyl-tRNA synthetase.,domain:The WHEP-TRS domain is involved in RNA binding.,function:Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA.,sequence caution:Contaminating sequence. Potential poly-A sequence.,sequence caution:Sequencing errors.,similarity:Belongs to the class-I aminoacyl-tRNA synthetase family.,similarity:Contains 3 WHEP-TRS domains.,similarity:In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.,similarity:In the N-terminal se
