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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Zusätzlich bieten wir Ihnen RARS Antikörper (51) und RARS Proteine (5) und viele weitere Produktgruppen zu diesem Protein an.
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Data indicate that the N terminus of Pro-EMAP II binds to its C terminus, arginyl-tRNA synthetase, and the neurofilament light subunit.
interactions between the N-terminal domains of ArgRS and AIMP1 (zeige AIMP1 ELISA Kits) are important for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC (zeige MSC ELISA Kits) protein complex with ArgRS-GlnRS (zeige QARS ELISA Kits)-AIMP1 (zeige AIMP1 ELISA Kits)
The mRNA of human cytoplasmic arginyl-tRNA synthetase recruits prokaryotic ribosomes independently.
report describe 4 patients with hypomyelination and mutations in RARS
The crystal structures of the L-arginine (zeige GATM ELISA Kits)-complexed, and L-canavanine-complexed forms of arginyl-tRNA synthetase from Homo sapiens.
Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity
leucyl-tRNA synthetase (zeige LARS2 ELISA Kits) requires its C-terminal domain for its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex
RARS over-expression impairs aminoacyl t-RNA synthetase interacting multifunctional protein (AIMP1 (zeige AIMP1 ELISA Kits)) secretion by both HeLa and MCF7 cells.
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. Arginyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family.
, Arginyl-tRNA ligase
, arginine--tRNA ligase, cytoplasmic
, arginyl-tRNA synthetase, cytoplasmic
, arginyl-tRNA synthetase
, arginyL-tRNA synthetase
, arginine tRNA ligase 1, cytoplasmic