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anti-Human LARS Antibodies:
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Human Polyclonal LARS Primary Antibody for ELISA, WB - ABIN543848
Ling, Yao, Zheng, Wei, Wang, Wu, Wang: 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. in The Journal of biological chemistry 2005
Show all 3 Pubmed References
Leucyl-tRNA synthetase (LRS) is a leucine sensor of the mTORC1 pathway.
The results showed a decrease in autophagy on addition of leucine, demonstrating crosstalk between leucine sensing, LRS translocation, RagD interaction, and mTORC1 activation.
the KMSKS catalytic loop affects the aminoacylation and editing capacities of leucyl-tRNA synthetase
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.
the carboxy-terminal domain of human mitochondrial (mt) leucyl-tRNA synthetase can be used to correct mt dysfunctions caused by mt-tRNA mutations.
Identification of a mutation in LARS as a novel cause of infantile hepatopathy
This work demonstrates that LRS is a key mediator for amino acid signaling to mTORC1.
hcLeuRS can charge RNALeu with non-cognate amino acids and exclude the incorrect products by multiple editing pathways.
leucyl-tRNA synthetase requires its C-terminal domain for its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex
We identified a novel G3283A transition in the mitochondrial DNA tRNA(Leu (UUR)) gene in a patient with ptosis, ophthalmoparesis and hyporeflexia.
Results show that K600 in human leucyl-tRNA synthetase affects amino acid specificity and tRNA aminoacylation.
findings suggest that LARS1 may play roles in migration and growth of lung cancer cells, which suggest its potential implication in lung tumorigenesis
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.
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
High LARS expression is associated with abdominal aortic aneurysm.
This gene encodes a cytosolic leucine-tRNA synthetase, a member of the class I aminoacyl-tRNA synthetase family. The encoded enzyme catalyzes the ATP-dependent ligation of L-leucine to tRNA(Leu). It is found in the cytoplasm as part of a multisynthetase complex and interacts with the arginine tRNA synthetase through its C-terminal domain. Alternatively spliced transcript variants of this gene have been found\; however, their full-length nature is not known.
cytoplasmic leucyl-tRNA synthetase
, cytosolic leucyl-tRNA synthetase
, leucine tRNA ligase 1, cytoplasmic
, leucine translase
, leucine--tRNA ligase, cytoplasmic
, leucine-tRNA ligase
, leucyl-tRNA synthetase, cytoplasmic
, proliferation-inducing gene 44
, leucyl-tRNA synthetase
, leucine-tRNA ligase, mitochondrial
, leucyl-tRNA synthetase, mitochondrial