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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Zusätzlich bieten wir Ihnen Glutaminyl-tRNA Synthetase Proteine (6) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 35 products:
Human Monoclonal QARS Primary Antibody für 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 (zeige MLXIP Antikörper)-US4-1 may involve in promoting cell apoptosis and benefiting discharge of infectious virus particles via down-regulation of QARS (zeige EPRS Antikörper) 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 (zeige EPRS Antikörper), which encodes glutaminyl-tRNA synthetase (zeige EPRS Antikörper), in two siblings with early-onset epileptic encephalopathy (EOEE).
interactions between the N-terminal domains of ArgRS (zeige RARS Antikörper) and AIMP1 (zeige AIMP1 Antikörper) are important for the catalytic and noncatalytic activities of ArgRS (zeige RARS Antikörper) and for the assembly of the higher-order MSC (zeige MSC Antikörper) protein complex with ArgRS (zeige RARS Antikörper)-GlnRS-AIMP1 (zeige AIMP1 Antikörper)
results highlight the importance of QARS (zeige EPRS Antikörper) during brain development and that epilepsy due to impairment of QARS (zeige EPRS Antikörper) activity is unusually severe in comparison to other aminoacyl-tRNA synthetase disorders
Data indicate that glutaminyl-tRNA synthetase (zeige EPRS Antikörper) 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