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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Additionally we are shipping Glutaminyl-tRNA Synthetase Proteins (6) and many more products for this protein.
Showing 10 out of 35 products:
Human Monoclonal QARS Primary Antibody for IHC (p), IP - ABIN562548
Smith, Qutob, Watson, Beavis, Potts, Welham, Garimella, Lind, Drew, Cawkwell: Proteomic identification of putative biomarkers of radiotherapy resistance: a possible role for the 26S proteasome? in Neoplasia (New York, N.Y.) 2009
hcmv-miR (show MLXIP Antibodies)-US4-1 may involve in promoting cell apoptosis and benefiting discharge of infectious virus particles via down-regulation of QARS (show EPRS Antibodies) in HCMV-infected HELF cells.
Pathological mutations mapping in the N-terminal domain alter the domain structure, and decrease catalytic activity and stability of GlnRS, whereas missense mutations in the catalytic domain induce misfolding of the enzyme.
Data indicate compound heterozygous mutations [c.169T>C (p.Tyr57His) and c.1485dup (p.Lys496*)] in QARS (show EPRS Antibodies), which encodes glutaminyl-tRNA synthetase (show EPRS Antibodies), in two siblings with early-onset epileptic encephalopathy (EOEE).
interactions between the N-terminal domains of ArgRS (show RARS Antibodies) and AIMP1 (show AIMP1 Antibodies) are important for the catalytic and noncatalytic activities of ArgRS (show RARS Antibodies) and for the assembly of the higher-order MSC (show MSC Antibodies) protein complex with ArgRS (show RARS Antibodies)-GlnRS-AIMP1 (show AIMP1 Antibodies)
results highlight the importance of QARS (show EPRS Antibodies) during brain development and that epilepsy due to impairment of QARS (show EPRS Antibodies) activity is unusually severe in comparison to other aminoacyl-tRNA synthetase disorders
Data indicate that glutaminyl-tRNA synthetase (show EPRS Antibodies) splice variant GlnRSDeltaiABD was present in exosomes extruded from Jurkat cells and functional in protein synthesis.
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. Alternative splicing results in multiple transcript variants.
, glutamyl-prolyl-tRNA synthetase
, glutaminyl-tRNA synthetase
, glutamine--tRNA ligase
, glutamine-tRNA synthetase
, glutamine-tRNA ligase