Anti-GARS1 Antibody Picoband®, APC Conjugate

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