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QARS1
Glutaminyl-tRNA synthetase 1QARS
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. [provided by RefSeq, Jan 2013]
Top validated antibodies |
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| Proteintech Group |  12645-1-AP |
4 references | Polyclonal |
WB
EL
ICC
IP
IHC
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| antibodies-online | ABIN396609 |
5 references | Monoclonal |
WB
EL
IP
IHC
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| Novus Biologicals | H00005859-M01 |
2 references | Monoclonal |
WB
EL
IP
IHC
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| Abnova Corporation | H00005859-M01 |
1 references | Monoclonal |
WB
EL
IP
IHC
|
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| LSBio | LS-C133074 |
Monoclonal |
WB
EL
IP
IHC
|
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