Anti-GARS antibody produced in rabbit

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies^® protocols and other useful information.

Glycyl-tRNA synthetase (GARS) is involved in charging tRNAs with glycine during protein synthesis. Mutations in the gene encoding it are associated with Charcot-Marie-Tooth disease type 2D (CMT2D), which is an autosomal-dominant peripheral neuropathy and distal spinal muscular atrophy type V.

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Prestige Antibodies^® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies^® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:

• IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
• Protein array of 364 human recombinant protein fragments.

Glycyl-tRNA synthetase (GARS) belongs to the aminoacyl-tRNA synthetase (ARS) family and has a unique quaternary structure. It has a catalytic domain with 3 motifs, having charged side chains that help in recognizing glycine and ATP (substrates). GARS possesses an amino-terminal region which consists of the TrpRS (W), HisRS (H) and GluProRS (EP) (WHEP-TRS) domain. The gene encoding this protein is localized to human chromosome 7p15.

Glycyl-tRNA synthetase recombinant protein epitope signature tag (PrEST)

Corresponding Antigen APREST74912

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

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