Anti-QRSL1 Antibody Picoband® APC-vervoeging

Contributes to glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity. Involved in glutaminyl-tRNAGln biosynthesis via transamidation and mitochondrial translation. Located in mitochondrion. Part of glutamyl-tRNA (Gln) amidotransferase complex. Implicated in combined oxidative phosphorylation deficiency 40.

QRSL1; Glutamyl-tRNA (Gln amidotransferase subunit A, mitochondrial; Glu-AdT subunit A; EC 6.3.5.7; Glutaminyl-tRNA synthase-like protein 1

QRSL1

55278

Q9H0R6

Human, Mouse, Rat

No cross-reactivity with other proteins

E.coli-derived human QRSL1 recombinant protein (Position: M1-Q528) . Human QRSL1 shares 88.1% and 87% amino acid (aa) sequence identity with mouse and rat QRSL1, respectively.

Flow Cytometry

Immunogen affinity purified.

Liquid

1. Friederich, M. W., Timal, S., Powell, C. A., Dallabona, C., Kurolap, A., Palacios-Zambrano, S., Bratkovic, D., Derks, T. G. J., Bick, D., Bouman, K., Chatfield, K. C., Damouny-Naoum, N., and 41 others. Pathogenic variants in glutamyl-tRNA (Gln) amidotransferase subunits cause a lethal mitochondrial cardiomyopathy disorder. Nature Commun. 9: 4065, 2018. Note: Electronic Article. 2. Hartz, P. A. Personal Communication. Baltimore, Md. 11/16/2016. 3. Kamps, R., Szklarczyk, R., Theunissen, T. E., Hellebrekers, D. M. E. I., Sallevelt, S. C. E. H., Boesten, I. B., de Koning, B., van den Bosch, B. J., Salomons, G. S., Simas-Mendes, M., Verdijk, R., Schoonderwoerd, K., de Coo, I. F. M., Vanoevelen, J. M., Smeets, H. J. M. Genetic defects in mtDNA-encoded protein translation cause pediatric, mitochondrial cardiomyopathy with early-onset brain disease. Europ. J. Hum. Genet. 26: 537-551, 2018.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

57 kDa

6

Glutaminyl-tRNA amidotransferase subunit QRSL1

Glutamyl-tRNA (Gln) amidotransferase subunit A, mitochondrial

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.