Anti-IARS1 Antibody Picoband® Fluoro488 Conjugated

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. Isoleucine-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family and has been identified as a target of autoantibodies in the autoimmune disease polymyositis/dermatomyositis. Alternatively spliced transcript variants have been found.

70 kDa ribosomal protein S6 kinase 1 antibody, KS6B1_HUMAN antibody, p70 alpha antibody, P70 beta 1 antibody, p70 ribosomal S6 kinase alpha antibody, p70 ribosomal S6 kinase beta 1 antibody, p70 S6 kinase alpha antibody, P70 S6 Kinase antibody, p70 S6 kinase alpha 1 antibody, p70 S6 kinase alpha 2 antibody, p70 S6K antibody, p70 S6K-alpha antibody, p70 S6KA antibody, p70 (S6K) alpha antibody, p70 (S6K) -alpha antibody, p70-alpha antibody, p70-S6K 1 antibody, p70-S6K antibody, P70S6K antibody, P70S6K1 antibody, p70S6Kb antibody, PS6K antibody, Ribosomal protein S6 kinase 70kDa polypeptide 1 antibody, Ribosomal protein S6 kinase beta 1 antibody, Ribosomal protein S6 kinase beta-1 antibody, Ribosomal protein S6 kinase I antibody, RPS6KB1 antibody, S6K antibody, S6K-beta-1 antibody, S6K1 antibody, Serine/threonine kinase 14 alpha antibody, Serine/threonine-protein kinase 14A antibody, STK14A antibody

E.coli-derived human PAWR recombinant protein (Position: R160-D255) . Human PAWR shares 82.3% and 81.2% amino acid (aa) sequence identity with mouse and rat PAWR, respectively.

Downstream effector of TOR signaling pathway involved in osmotic stress response. Could be involved in the control of plant growth and development. Phosphorylates the ribosomal proteins P14, P16 and S6. Functions as a repressor of cell proliferation and required for maintenance of chromosome stability and ploidy levels through the RBR1-E2F pathway.

1. Hirano, T., Kobayashi, N., Matsuhashi, T., Watanabe, D., Watanabe, T., Takasuga, A., Sugimoto, M., Sugimoto, Y. Mapping and exome sequencing identifies a mutation in the IARS gene as the cause of hereditary perinatal weak calf syndrome. PLoS One 8: e64036, 2013. Note: Electronic Article. 2. Kopajtich, R., Murayama, K., Janecke, A. R., Haack, T. B., Breuer, M., Knisely, A. S., Harting, I., Ohashi, T., Okazaki, Y., Watanabe, D., Tokuzawa, Y., Kotzaeridou, U., and 16 others. Biallelic IARS mutations cause growth retardation with prenatal onset, intellectual disability, muscular hypotonia, and infantile hepatopathy. Am. J. Hum. Genet. 99: 414-422, 2016. 3. 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.