Anti-GARS1 Antibody Picoband®

Glycine—tRNA ligase also known as glycyl–tRNA synthetase is an enzyme that in humans is encoded by the GARS1 gene. 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. Two transcript variants encoding different isoforms have been found for this gene.

E.coli-derived human GARS1 recombinant protein (Position: E61-D673) . Human GARS1 shares 95.3% and 95.4% amino acid (aa) sequence identity with mouse and rat GARS1, respectively.

1. Abe, A., Hayasaka, K. The GARS gene is rarely mutated in Japanese patients with Charcot-Marie-Tooth neuropathy. J. Hum. Genet. 54: 310-312, 2009. 2. Antonellis, A., Ellsworth, R. E., Sambuughin, N., Puls, I., Abel, A., Lee-Lin, S.-Q., Jordanova, A., Kremensky, I., Christodoulou, K., Middleton, L. T., Sivakumar, K., Ionasescu, V., Funalot, B., Vance, J. M., Goldfarb, L. G., Fischbeck, K. H., Green, E. D. Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V. Am. J. Hum. Genet. 72: 1293-1299, 2003. 3. Boczonadi, V., Meyer, K., Gonczarowska-Jorge, H., Griffin, H., Roos, A., Bartsakoulia, M., Bansagi, B., Ricci, G., Palinkas, F., Zahedi, R. P., Bruni, F., Kaspar, B., Lochmuller, H., Boycott, K. M., Muller, J. S., Horvath, R. Mutations in glycyl-tRNA synthetase impair mitochondrial metabolism in neurons. Hum. Molec. Genet. 27: 2187-2204, 2018.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.