Anti-QARS polyclonal antibody (DPABH-22477)

Rabbit Anti-Human QARS (aa 317-569) polyclonal antibody for WB, IHC-P Datasheet

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Specifications


Host Species
Rabbit
Antibody Isotype
IgG
Species Reactivity
Human
Immunogen
Recombinant fragment, corresponding to a region within amino acids 317 and 569 of Human QARS (P47897).
Conjugate
Unconjugated

Applications


Application Notes
WB: 1/500 - 1/3000; IHC-P: 1/100 - 1/1000.
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
QARS; glutaminyl-tRNA synthetase; glutamine--tRNA ligase; glutamine tRNA ligase; glutamine-tRNA synthetase; GLNRS
Entrez Gene ID
UniProt ID

Product Background


Gene summary
QARS (Glutaminyl-TRNA Synthetase) is a Protein Coding gene. Diseases associated with QARS include microcephaly, progressive, seizures, and cerebral and cerebellar atrophy and diffuse cerebral and cerebellar atrophy-intractable seizures-progressive microcephaly syndrome. Among its related pathways are Gene Expression and Metabolism. GO annotations related to this gene include nucleotide binding and ligase activity, forming aminoacyl-tRNA and related compounds. Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. Alternative splicing results in multiple transcript variants.
Antigen Description
QARS is a class I aminoacyl-tRNA synthetase. Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. The specificity of this reaction determines the fidelity of mRNA translation. At least 1 synthetase exists in the cytoplasm for each amino acid. Although present in eukaryotes, glutaminyl-tRNA synthetase (QARS) is absent from many prokaryotes, mitochondria, and chloroplasts, in which Gln-tRNA(Gln) is formed by transamidation of the misacylated Glu-tRNA(Gln). Microcephaly, progressive, with seizures and cerebral and cerebellar atrophy (MSCCA) [MIM:615760]: A severe, autosomal recessive, neurodevelopmental and neurodegenerative disorder characterized by progressive microcephaly, severe seizures in infancy, atrophy of the cerebral cortex and cerebellar vermis, and mild atrophy of the cerebellar hemispheres, resulting in profoundly delayed development and hypotonia. Note=The disease is caused by mutations affecting the gene represented in this entry. Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAs, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. In metazoans, 9 aminoacyl-tRNA synthetases specific for glutamine (gln), glutamic acid (glu), and 7 other amino acids are associated within a multienzyme complex. Glutaminyl-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family. Almost all eukaryotic GlnRS enzymes possess a YqeY domain at the N-terminus, which affects affinity for the tRNA; in some bacterial species, such as Deinococcus radiodurans, YqeY is present as a C-terminal domain with similar function. The function about QARS antigen include ATP binding; glutamine-tRNA ligase activity; ligase activity; nucleotide binding.
Pathway
Aminoacyl-tRNA biosynthesis; Aminoacyl-tRNA biosynthesis, eukaryotes; Cytosolic tRNA aminoacylation; Gene Expression; Metabolic pathways.

Citations


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References


Thomann, HU; Ibba, M; et al. Homologous expression and purification of mutants of an essential protein by reverse epitope-tagging. BIO-TECHNOLOGY 14:50-55(1996).
TARGOFF, IN; TRIEU, EP; et al. REACTION OF ANTI-OJ AUTOANTIBODIES WITH COMPONENTS OF THE MULTIENZYME COMPLEX OF AMINOACYL-TRANSFER RNA-SYNTHETASES IN ADDITION TO ISOLEUCYL-TRANSFER RNA-SYNTHETASE. JOURNAL OF CLINICAL INVESTIGATION 91:2556-2564(1993).

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We offer labeled antibodies using our catalogue antibody products and a broad range of intensely fluorescent dyes and labels including HRP, biotin, ALP, Alexa Fluor® dyes, DyLight® Fluor dyes, R-phycoerythrin (R-PE), at scales from less than 100 μg up to 1 g of IgG antibody. Learn More

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