LARS Antibody, FITC conjugated

1. Leucyl-tRNA synthetase (LRS) is a leucine sensor of the mTORC1 pathway. PMID: 28963468
2. The results showed a decrease in autophagy on addition of leucine, demonstrating crosstalk between leucine sensing, LRS translocation, RagD interaction, and mTORC1 activation. PMID: 28882589
3. the KMSKS catalytic loop affects the aminoacylation and editing capacities of leucyl-tRNA synthetase PMID: 25817995
4. Lack of a CP1 hairpin in LeuRS led to complete loss of aminoacylation, amino acid activation, and tRNA binding; however, the mutants retained post-transfer editing. PMID: 25051973
5. the carboxy-terminal domain of human mitochondrial (mt) leucyl-tRNA synthetase can be used to correct mt dysfunctions caused by mt-tRNA mutations. PMID: 24413190
6. Identification of a mutation in LARS as a novel cause of infantile hepatopathy PMID: 22607940
7. This work demonstrates that LRS is a key mediator for amino acid signaling to mTORC1. PMID: 22424946
8. hcLeuRS can charge RNALeu with non-cognate amino acids and exclude the incorrect products by multiple editing pathways. PMID: 20805241
9. leucyl-tRNA synthetase requires its C-terminal domain for its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex PMID: 16055448
10. We identified a novel G3283A transition in the mitochondrial DNA tRNA(Leu (UUR)) gene in a patient with ptosis, ophthalmoparesis and hyporeflexia. PMID: 17363246
11. Results show that K600 in human leucyl-tRNA synthetase affects amino acid specificity and tRNA aminoacylation. PMID: 17378584
12. findings suggest that LARS1 may play roles in migration and growth of lung cancer cells, which suggest its potential implication in lung tumorigenesis PMID: 18446061
13. Study of crystal structures of the editing domain from 2 eukaryotic cytosolic LeuRS; shows a conserved structural core containing the active site for hydrolysis, with distinct bacterial, archeal, or eukaryotic peripheral insertions. PMID: 19426743
14. the introduction of bulky residues into the amino acid binding pocket failed to block deacylation of tRNA, indicating that the architecture of the amino acid binding pocket is different compared to that of other characterized LeuRSs PMID: 19702327

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HGNC: 6512

OMIM: 151350

KEGG: hsa:51520

STRING: 9606.ENSP00000377954

UniGene: Hs.432674