|Application ||WB, E|
|Other Accession||NP_002878, 5917, 104458 (mouse), 287191 (rat)|
|Predicted||Mouse, Rat, Cow|
|Calculated MW||75379 Da|
|Other Names||Arginine--tRNA ligase, cytoplasmic, 126.96.36.199, Arginyl-tRNA synthetase, ArgRS, RARS|
|Format||0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Goat Anti-RARS Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.|
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Provided below are standard protocols that you may find useful for product applications.
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.
Toward a confocal subcellular atlas of the human proteome. Barbe L, et al. Mol Cell Proteomics, 2008 Mar. PMID 18029348.
Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines. Bottoni A, et al. J Cell Physiol, 2007 Aug. PMID 17443684.
Large-scale mapping of human protein-protein interactions by mass spectrometry. Ewing RM, et al. Mol Syst Biol, 2007. PMID 17353931.
Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes. Kimura K, et al. Genome Res, 2006 Jan. PMID 16344560.
The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex. Ling C, et al. J Biol Chem, 2005 Oct 14. PMID 16055448.
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