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MARS encodes a member of the class I family of aminoacyl-tRNA synthetases. Additionally we are shipping Methionyl-tRNA Synthetase Proteins (4) and many more products for this protein.
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Human Polyclonal MARS Primary Antibody for ICC, IF - ABIN4333967
van Meel, Wegner, Cliften, Willing, White, Kornfeld, Cole: Rare recessive loss-of-function methionyl-tRNA synthetase mutations presenting as a multi-organ phenotype. in BMC medical genetics 2013
Loss of Aats-met in the eye results in retinal degeneration.
Compound Arg618Cys and Tyr307Cys variants were identified in an infant with syndromic interstitial lung and liver disease. Arg618Cys associated with Charcot-Marie-Tooth disease was inherited from an unaffected father.
MRS is frequently overexpressed in NSCLC. Moreover, MRS is related to mTORC1 activity and its overexpression is associated with poor clinical outcomes, indicating that it has potential as a putative therapeutic target.
Genotype-phenotype correlation analysis suggests most of the interstitial lung and liver disease (ILLD), mutations locate in the catalytic domain of MARS. ILLD and Charcot-Marie-Tooth disease, axonal, type 2U might have different disease mechanism.
analysis of the heterotetrameric complex structure of the glutathione transferase (GST) domains shared among the four MSC components, methionyl-tRNA synthetase (MRS), glutaminyl-prolyl-tRNA synthetase (EPRS), AIMP2 and AIMP3
identification of a founder mutation in MARS led to the molecular definition of a specific type of pulmonary alveolar proteinosis and will enable carrier screening in the affected community and possibly open new treatment opportunities.
the association of rare MARS variant with late-onset autosomal dominant Charcot-Marie-Tooth neuropathy
The F370L and I523T mutations did not affect the association of MARS with the multisynthetase complex.
Here we present data suggesting that MARS is a very rare novel cause of late-onset CMT2.
Data show that aminoacyl-tRNA synthetase-interacting multifunctional protein-3 (AIMP3)/p18 is released from aminoacyl-tRNA synthetase-interacting multifunctional protein-3 (AIMP3) by UV irradiation-induced stress.
The last 15 residues of the previously defined N-terminal extension of hcMetRS are part of the catalytic domain, whereas the first 252 residues constitute the N-terminal extended domain.
This gene encodes a member of the class I family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. The encoded protein is a component of the multi-tRNA synthetase complex and catalyzes the ligation of methionine to tRNA molecules.
methionine--tRNA ligase, cytoplasmic
, methionine-tRNA synthetase
, methionyl-tRNA synthetase
, methionine-tRNA ligase, mitochondrial
, methionyl-tRNA synthetase, mitochondrial
, methionine tRNA ligase
, methionyl-tRNA synthetase, cytoplasmic
, cytosolic methionyl-tRNA synthetase
, methionine tRNA ligase 1, cytoplasmic