Anti-QARS1 Antibody Picoband® Fluoro647 Conjugated

Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene. 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.

Aflatoxin B1 aldehyde reductase member 2; AFB1 aldehyde reductase 1; AFB1-AR 1; Aldoketoreductase 7; Succinic semialdehyde reductase; SSA reductase; AKR7A2; AFAR; AFAR1; AKR7

Expressed in basement membranes of lung and kidney. Muscle- and neuron-specific isoforms are found. Isoforms (y+) with the 4 AA insert and (z+8) isoforms with the 8 AA insert are all neuron-specific. Isoforms (z+11) are found in both neuronal and non-neuronal tissues.

Catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate. May have an important role in producing the neuromodulator gamma-hydroxybutyrate (GHB) . Has broad substrate specificity. Has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro) . Can reduce 1,2-naphthoquinone and 9,10-phenanthrenequinone (in vitro) . Can reduce the dialdehyde protein-binding form of aflatoxin B1 (AFB1) to the non-binding AFB1 dialcohol. May be involved in protection of liver against the toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

1. Lamour, V., Quevillon, S., Diriong, S., N'Guyen, V. C., Lipinski, M., Mirande, M. Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer. Proc. Nat. Acad. Sci. 91: 8670-8674, 1994. 2. Lo, W.-S., Gardiner, E., Xu, Z., Lau, C.-F., Wang, F., Zhou, J. J., Mendlein, J. D., Nangle, L. A., Chiang, K. P., Yang, X.-L., Au, K.-F., Wong, W. H., Guo, M., Zhang, M., Schimmel, P. Human tRNA synthetase catalytic nulls with diverse functions. Science 345: 328-332, 2014. 3. Zhang, X., Ling, J., Barcia, G., Jing, L., Wu, J., Barry, B. J., Mochida, G. H., Hill, R. S., Weimer, J. M., Stein, Q., Poduri, A., Partlow, J. N., and 13 others. Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures. Am. J. Hum. Genet. 94: 547-558, 2014.