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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Additionally we are shipping Glutaminyl-tRNA Synthetase Antibodies (21) and many more products for this protein.
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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 Proteins), which encodes glutaminyl-tRNA synthetase (show EPRS Proteins), in two siblings with early-onset epileptic encephalopathy (EOEE).
interactions between the N-terminal domains of ArgRS (show RARS Proteins) and AIMP1 (show AIMP1 Proteins) are important for the catalytic and noncatalytic activities of ArgRS (show RARS Proteins) and for the assembly of the higher-order MSC (show MSC Proteins) protein complex with ArgRS (show RARS Proteins)-GlnRS-AIMP1 (show AIMP1 Proteins)
results highlight the importance of QARS (show EPRS Proteins) during brain development and that epilepsy due to impairment of QARS (show EPRS Proteins) activity is unusually severe in comparison to other aminoacyl-tRNA synthetase disorders
Data indicate that glutaminyl-tRNA synthetase (show EPRS Proteins) 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