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Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. Additionally we are shipping EPRS Proteins (6) and EPRS Kits (2) and many more products for this protein.
Showing 10 out of 41 products:
analysis of the heterotetrameric complex structure of the glutathione transferase (GST (show SLCO6A1 Antibodies)) domains shared among the four MSC (show MSC Antibodies) components, methionyl-tRNA synthetase (show MARS Antibodies) (MRS), glutaminyl-prolyl-tRNA synthetase (EPRS), AIMP2 (show AIMP2 Antibodies) and AIMP3 (show EEF1E1 Antibodies)
Dynamic model simulations predicted an inhibitory GAIT-element-interacting factor to account for this relationship and led to the identification of a truncated form of EPRS, a GAIT constituent that mediates binding to target transcripts.
Study reveals a unique role of Cdk5 (show CDK5 Antibodies)/p35 (show ANXA1 Antibodies) in activation of the major noncanonical function of EPRS, namely translational control of macrophage inflammatory gene expression.
Results show that glutamyl-prolyl-tRNA synthetase has a regulated, noncanonical activity that blocks synthesis of a specific protein.
EPRS phosphorylation events regulate GAIT-mediated gene silencing.
The rules presented here for the regulated ribosome bypass of noncanonical initiation codons in the EPRS 5'-leader add complexity into the nature of uORF-mediated translation control mechanisms during eIF2alpha (show EIF2A Antibodies)-P and additionally illustrate the roles that previously unexamined uORFs with noncanonical initiation codons can play in modulating gene expression.
IFN-gamma (show IFNG Antibodies) activates the macrophage GAIT system via induced phosphorylation of EPRS and L13a (show RPL13A Antibodies). L13a (show RPL13A Antibodies) is phosphorylated at Ser (show SIGLEC1 Antibodies)(77) by the DAPK (show DAPK1 Antibodies)-ZIPK (show DAPK3 Antibodies) cascade, but EPRS is phosphorylated only at Ser (show SIGLEC1 Antibodies)(999).
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.
bifunctional aminoacyl-tRNA synthetase
, bifunctional glutamate/proline--tRNA ligase
, cell proliferation-inducing gene 32 protein
, glutamate tRNA ligase
, glutamatyl-prolyl-tRNA synthetase
, glutaminyl-tRNA synthetase
, proliferation-inducing gene 32 protein
, proliferation-inducing protein 32
, proline tRNA ligase
, proline-tRNA ligase
, prolyl-tRNA synthetase
, glutamine-proline-tRNA synthetase