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Browse our anti-Glycyl-tRNA Synthetase (GARS) Antibodies

Full name:: anti-Glycyl-tRNA Synthetase Antibodies (GARS)

On www.antibodies-online.com are 76 Glycyl-tRNA Synthetase (GARS) Antibodies from 23 different suppliers available. Additionally we are shipping Glycyl-tRNA Synthetase Proteins (13) and Glycyl-tRNA Synthetase Kits (9) and many more products for this protein. A total of 102 Glycyl-tRNA Synthetase products are currently listed.

Synonyms:: Aat-gly, CG6778, CMT2D, Dmel\\CG6778, DSMAV, fb02f03, gars, GB13467, Gena201, GENA202, GlyRS, GRS, HMN5, MGC79495, NI36_08435, Nmf249, RGD1559871, Sgrp23, si:dkey-276i5.1, SMAD1, team, wu:fb02f03

list all antibodies	Gene Name	GeneID	UniProt
	GARS	2617	P41250
	GARS	297113
	GARS	353172	Q9CZD3
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Most Popular Reactivities for anti-Glycyl-tRNA Synthetase (GARS) Antibodies

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anti-Human Antibodies:

anti-Rat (Rattus) Antibodies:

16 WB Antibodies

anti-Mouse (Murine) Antibodies:

18 WB Antibodies

All available anti-Glycyl-tRNA Synthetase Antibodies

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Relevant Pathways for anti-Glycyl-tRNA Synthetase Antibodies

Ribonucleoside Biosynthetic Process

More product categories related to Glycyl-tRNA Synthetase Antibody

More Antibodies against Glycyl-tRNA Synthetase Interaction Partners

Human Glycyl-tRNA Synthetase (GARS) interaction partners

we have demonstrated that CMT2D mice display a pathological phenotype restricted to the nervous system, and that GlyRS-mediated disruption of Nrp1/VEGF-A signalling appears to be permissive to capillary maturation and maintenance.
ignificant alterations of the vesicle-associated membrane protein-associated protein B (VAPB) and its downstream pathways such as mitochondrial calcium uptake and autophagy were detected in dominant GARS mutations. The role of VAPB has been supported by similar results in the GarsC210R mice. Our data suggest that altered mitochondria-associated endoplasmic reticulum (ER) membranes (MAM) may be important disease mechanisms
In support of GARS variant pathogenicity, our patient shows striking phenotypic overlap with other patients having ARS-related recessive diseases; this observation is consistent with the essential function of GARS in both cellular locations. In summary, our clinical, genetic, and functional analyses expand the phenotypic spectrum associated with GARS variants
In this Chinese Han population a novel Charcot-Marie-Tooth disease-associated gene mutations of GARS (c.794C>T) was discovered.
At the active site, a glycyl-AMP molecule is synthesized and is waiting for the transfer of the glycyl moiety to occur.
GlyRS functions as a chaperone that critically supports neddylation.
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.
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.
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.
This study presents genetic evidence for common mutant-specific interactions between two CMT-associated aminoacyl-tRNA synthetases, lending support for a shared mechanism responsible for the synthetase-induced peripheral neuropathies.
We developed an ELISA to detect anti-glycyl-tRNA synthetase by using recombinant protein
Report crystal structures of wild type and mutant GlyRS in complex with tRNA and with small substrates and describe the molecular details of enzymatic recognition of the key tRNA identity elements in the acceptor stem and the anticodon loop.
we believe that these two novel GARS mutations are the underlying causes of the distal hereditary motor neuropathy type V phenotype
GRS bound to different ERK-activated tumor cells, and released phosphatase 2A (PP2A) from CDH6.

Fruit Fly (Drosophila melanogaster) Glycyl-tRNA Synthetase (GARS) interaction partners

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.

Mouse (Murine) Glycyl-tRNA Synthetase (GARS) interaction partners

ignificant alterations of the vesicle-associated membrane protein-associated protein B (VAPB) and its downstream pathways such as mitochondrial calcium uptake and autophagy were detected in dominant GARS mutations. The role of VAPB has been supported by similar results in the GarsC210R mice. Our data suggest that altered mitochondria-associated endoplasmic reticulum (ER) membranes (MAM) may be important disease mechanisms
Gars mutations are associated with Charcot-Marie-Tooth disease type 2D.
Results link the aberrant GlyRS-HDAC6 interaction to Charcot-Marie-Tooth disease type 2D pathology and suggest HDAC6 as an effective therapeutic target.
findings link the selective pathology of Charcot-Marie-Tooth disease type 2D to the neomorphic binding activity of GlyRS(CMT2D) that antagonizes the VEGF-Nrp1 interaction, meaning the VEGF-Nrp1 signalling axis is an actionable target for treating CMT2D
These results suggest that this animal model of CMT using an adenovirus may provide information regarding CMT as well as a useful strategy for the treatment of neuropathic pain.
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(G93A);Gars(C201R/+) double heterozygous mutant mice and increased lifespan by 29% on the genetic background investigated

Zebrafish Glycyl-tRNA Synthetase (GARS) interaction partners

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.

Pig (Porcine) Glycyl-tRNA Synthetase (GARS) interaction partners

Expression levels of ADSL, GARS-AIRS-GART, and DGAT1 were higher in longissimus lumborum muscle than in heart or liver tissues

Glycyl-tRNA Synthetase (GARS) Antigen Profile

Antigen Summary

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.

Alternative names and synonyms associated with Glycyl-tRNA Synthetase (GARS)

glycyl-tRNA synthetase (GARS) antibody
Glycyl-tRNA synthetase (GlyRS) antibody
glycyl-tRNA synthetase (Gars) antibody
glycine--tRNA ligase (LOC408392) antibody
glycyl-tRNA synthetase L homeolog (gars.L) antibody
glycyl-tRNA synthetase (gars) antibody
glycyl-tRNA synthetase (LOC692991) antibody
glycine--tRNA ligase (glyQ) antibody
glycyl-tRNA synthetase (TTHA0543) antibody
Glycine--tRNA ligase (NI36_RS08405) antibody

Aat-gly antibody
CG6778 antibody
CMT2D antibody
Dmel\\CG6778 antibody
DSMAV antibody
fb02f03 antibody
gars antibody
GB13467 antibody
Gena201 antibody
GENA202 antibody
GlyRS antibody
GRS antibody
HMN5 antibody
MGC79495 antibody
NI36_08435 antibody
Nmf249 antibody
RGD1559871 antibody
Sgrp23 antibody
si:dkey-276i5.1 antibody
SMAD1 antibody
team antibody
wu:fb02f03 antibody

Protein level used designations for GARS

AP-4-A synthetase , Charcot-Marie-Tooth neuropathy 2D , Charcot-Marie-Tooth neuropathy, neuronal type, D , diadenosine tetraphosphate synthetase , glycine tRNA ligase , glycine--tRNA ligase , Aats-gly-PA , Aats-gly-PB , Aats-gly-PC , CG6778-PA , CG6778-PB , CG6778-PC , glycyl-tRNA synthetase , glyRS , storage granule protein 23 , glycyl-tran synthetase , Glycyl-tRNA synthetase

GENE ID	SPECIES
2617	Homo sapiens
39644	Drosophila melanogaster
297113	Rattus norvegicus
353172	Mus musculus
408010	Bos taurus
408392	Apis mellifera
428403	Gallus gallus
446482	Xenopus laevis
463329	Pan troglodytes
475268	Canis lupus familiaris
493218	Xenopus (Silurana) tropicalis
692991	Bombyx mori
884595	Chlamydia trachomatis D/UW-3/CX
3169948	Thermus thermophilus HB8
100174405	Pongo abelii
100388470	Callithrix jacchus
337230	Danio rerio
100512260	Sus scrofa
100723446	Cavia porcellus
101926831	Macaca fascicularis
31214473	Staphylococcus aureus

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