Glutaminyl tRNA Synthetase (QARS) Antibody

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Description
QARS Antibody is a Rabbit Polyclonal antibody against QARS. 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.
Documents del producto
Product specifications
Category | Primary Antibodies |
Immunogen Target | Glutaminyl tRNA Synthetase (QARS) |
Host | Rabbit |
Reactivity | Human, Mouse |
Recommended Dilution | ELISA: 1 µg/ml, WB: 1/500 - 1/2000, IHC-P: 1/50 - 1/200, IF/ICC: 1/50 - 1/100. Not tested in IHC-F. Optimal dilutions/concentrations should be determined by the end user. |
Clonality | Polyclonal |
Conjugation | Unconjugated |
Isotype | IgG |
Purification | Purified by affinity chromatography. |
Size 1 | 20 µl |
Size 2 | 100 µl |
Size 3 | 2 × 100 µl |
Form | Liquid |
Tested Applications | ELISA, WB, IHC, IF/ICC |
Buffer | PBS, pH 7.3, containing 0.02% sodium azide, 50% glycerol. |
Availability | Shipped within 5-10 working days. |
Storage | Aliquot and store at -20°C. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
UniProt ID | P47897 |
Gene ID | 5859 |
NCBI Accession | NP_005042.1 |
Background | Antibody anti-QARS |
Status | RUO |
Note | Concentration: > 0.2 mg/ml - |
Descripción
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Glutaminyl tRNA Synthetase (QARS) Antibody
QARS Antibody is a Rabbit Polyclonal antibody against QARS. 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.
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