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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Additionally we are shipping RARS Antibodies (48) and RARS Proteins (5) and many more products for this protein.
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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 (show AIMP1 ELISA Kits) are important for the catalytic and noncatalytic activities of ArgRS and for the assembly of the higher-order MSC (show MSC ELISA Kits) protein complex with ArgRS-GlnRS (show QARS ELISA Kits)-AIMP1 (show 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 (show 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 (show 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 (show 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