GlnRS Antibody (F-4): sc-166241
- GlnRS Antibody (F-4) is a mouse monoclonal IgG2b κ provided at 200 µg/ml
- raised against amino acids 513-775 mapping at the C-terminus of GlnRS of human origin
- recommended for detection of GlnRS of human origin by WB, IP, IF, IHC(P) and ELISA
- m-IgG Fc BP-HRP, m-IgG2b BP-HRP and m-IgGκ BP-HRP are the preferred secondary detection reagents for GlnRS Antibody (F-4) for WB and IHC(P) applications. These reagents are now offered in bundles with GlnRS Antibody (F-4) (see ordering information below).
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GlnRS Antibody (F-4) is a mouse monoclonal IgG2b antibody that detects GlnRS in human samples through western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). GlnRS, or Glutaminyl-tRNA synthetase, is a crucial enzyme composed of 775 amino acids that plays a vital role in protein synthesis by catalyzing the aminoacylation of tRNA with L-glutamine. This process ensures accurate translation of genetic information into functional proteins by incorporating correct amino acids into the growing polypeptide chain during translation. GlnRS is localized in the cytoplasm and functions as a key component of a multi-protein complex containing nine aminoacyl-tRNA synthetases, each specific for a different amino acid. This complex facilitates efficient synthesis of Gln-tRNA(Gln) and demonstrates the intricate interplay between various aminoacyl-tRNA synthetases in maintaining cellular function and protein homeostasis. GlnRS′s ability to operate in both eukaryotic cells and prokaryotic systems, including mitochondria and chloroplasts, underscores evolutionary significance and adaptability in different biological contexts.
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GlnRS Antibody (F-4) References:
- A rationally engineered misacylating aminoacyl-tRNA synthetase. | Bullock, TL., et al. 2008. Proc Natl Acad Sci U S A. 105: 7428-33. PMID: 18477696
- The structure of yeast glutaminyl-tRNA synthetase and modeling of its interaction with tRNA. | Grant, TD., et al. 2013. J Mol Biol. 425: 2480-93. PMID: 23583912
- Evolutionary insights about bacterial GlxRS from whole genome analyses: is GluRS2 a chimera? | Dasgupta, S. and Basu, G. 2014. BMC Evol Biol. 14: 26. PMID: 24521160
- Structure of the ArgRS-GlnRS-AIMP1 complex and its implications for mammalian translation. | Fu, Y., et al. 2014. Proc Natl Acad Sci U S A. 111: 15084-9. PMID: 25288775
- The crystal structure of human GlnRS provides basis for the development of neurological disorders. | Ognjenović, J., et al. 2016. Nucleic Acids Res. 44: 3420-31. PMID: 26869582
- Aminoacyl-tRNA Synthetases in the Bacterial World. | Giegé, R. and Springer, M. 2016. EcoSal Plus. 7: PMID: 27223819
- A water-mediated and substrate-assisted aminoacylation mechanism in the discriminating aminoacyl-tRNA synthetase GlnRS and non-discriminating GluRS. | Aboelnga, MM., et al. 2017. Phys Chem Chem Phys. 19: 25598-25609. PMID: 28905057
- Aminoacyl-tRNA Synthetases: On Anti-Synthetase Syndrome and Beyond. | Galindo-Feria, AS., et al. 2022. Front Immunol. 13: 866087. PMID: 35634293
- Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase. | Rogers, MJ., et al. 1993. Biochimie. 75: 1083-90. PMID: 8199243
- Glutaminyl-tRNA synthetase: from genetics to molecular recognition. | Ibba, M., et al. 1996. Genes Cells. 1: 421-7. PMID: 9078373
Ordering Information
| Product Name | Catalog # | UNIT | Price | Qty | FAVORITES | |
GlnRS Antibody (F-4) | sc-166241 | 200 µg/ml | $322.00 | |||
GlnRS Antibody (F-4): m-IgG Fc BP-HRP Bundle | sc-537460 | 200 µg Ab; 10 µg BP | $361.00 | |||
GlnRS Antibody (F-4): m-IgGκ BP-HRP Bundle | sc-534734 | 200 µg Ab; 40 µg BP | $361.00 | |||
GlnRS Antibody (F-4): m-IgG2b BP-HRP Bundle | sc-549876 | 200 µg Ab; 10 µg BP | $361.00 |