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GARS encodes glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases that charge tRNAs with their cognate amino acids. Additionally we are shipping Glycyl-tRNA Synthetase Kits (14) and Glycyl-tRNA Synthetase Proteins (8) and many more products for this protein.
Showing 10 out of 61 products:
Human Polyclonal GARS Primary Antibody for WB - ABIN392465
Shiba, Schimmel, Motegi, Noda: Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. in The Journal of biological chemistry 1994
Show all 2 references for ABIN392465
Human Polyclonal GARS Primary Antibody for EIA, WB - ABIN360353
Antonellis, Ellsworth, Sambuughin, Puls, Abel, Lee-Lin, Jordanova, Kremensky, Christodoulou, Middleton, Sivakumar, Ionasescu, Funalot, Vance, Goldfarb, Fischbeck, Green: Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V. in American journal of human genetics 2003
Show all 2 references for ABIN360353
Chicken Polyclonal GARS Primary Antibody for WB - ABIN2787816
Förster, Zerressen-Harte, Fürste, Perbandt, Betzel, Erdmann: Comparative X-ray structure analysis of human and Escherichia coli tRNA(Gly) acceptor stem microhelices. in Biochemical and biophysical research communications 2008
Our findings suggest that mutant GlyRS gains access to ectopic sub-compartments of the motor neuron, providing a possible explanation for the selective neuropathology caused by mutations in a widely expressed gene.
Data indicate that dimerization is required for the dominant neurotoxicity of disease-associated GARS mutations and provide a rapid, tractable model for studying newly identified GARS variants for a role in human disease.
one of the mRNAs isoforms tightly controls expression and localization of human GARS.
This study reports two crystal structures of human GlyRS variants, in the free form and in complex with tRNA(Gly) respectively, and reveal new aspects of the glycylation mechanism.
GARS mutations are an uncommon cause of Charcot-Marie-Tooth Disease (CMT) in Taiwan. The p.Asp146Tyr and p.Met238Arg mutations are associated with early-onset axonal CMT.
Expression of three CMT-mutant GARS proteins in Drosophila induces defects in motor performance and motor and sensory neuron morphology, and shortens lifespan.
The c.999G>T mutation is a novel mutation of the glycyl-tRNA synthetase gene that has not been previously reported. The phenotype of this family is Charcot-Marie-Tooth disease type 2D, which is first reported in Chinese population.
we propose that the disease-causing L129P mutant of glycyl-tRNA synthetase is linked to a distribution defect in peripheral nerves in vivo.
our data indicate that impaired function is a key component of GARS-mediated CMT disease and emphasize the need for careful genetic and functional evaluation before implicating a variant in disease onset.
We developed an ELISA to detect anti-glycyl-tRNA synthetase by using recombinant protein
findings link the selective pathology of Charcot-Marie-Tooth disease type 2D to the neomorphic binding activity of GlyRS(CMT2D) that antagonizes the VEGF (show VEGFA Antibodies)-Nrp1 (show NRP1 Antibodies) interaction, meaning the VEGF (show VEGFA Antibodies)-Nrp1 (show NRP1 Antibodies) signalling axis is an actionable target for treating CMT2D
Results indicate that Charcot-Marie-Tooth peripheral neuropathies, type 2D (CMT2D) phenotype is caused by novel pathogenic roles for the mutant GARS that specifically affect peripheral neurons.
a glycyl-tRNA synthetase (GARS) mutation causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy
Gars(C201R) mutation significantly delayed disease onset in the SOD1 (show SOD1 Antibodies)(G93A);Gars(C201R/+) double heterozygous mutant mice and increased lifespan by 29% on the genetic background investigated
Expression levels of ADSL (show ADSL Antibodies), GARS-AIRS-GART (show GART Antibodies), and DGAT1 (show DGAT1 Antibodies) were higher in longissimus lumborum muscle than in heart or liver tissues
This gene encodes glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases that charge tRNAs with their cognate amino acids. The encoded enzyme is an (alpha)2 dimer which belongs to the class II family of tRNA synthetases. It has been shown to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.
, glycyl-tRNA synthetase
, glycine--tRNA ligase
, AP-4-A synthetase
, Charcot-Marie-Tooth neuropathy 2D
, Charcot-Marie-Tooth neuropathy, neuronal type, D
, diadenosine tetraphosphate synthetase
, glycine tRNA ligase
, storage granule protein 23
, glycyl-tran synthetase