Abcam, ab226296, Anti-GlnRS antibody - C-terminal

Size: 100µL
Rabbit Polyclonal GlnRS antibody. C-terminal. Suitable for IP, WB and reacts with Human, Mouse samples. Cited in 1 publication. Immunogen corresponding to Synthetic Peptide within Human QARS1 aa 700 to C-terminus.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Human,
Applications:WB, IPSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human QARS1 aa 700 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.P47897

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Purification notes-ab226296 was affinity purified using an epitope specific to GlnRS immobilized on solid support., Storage buffer-pH: 7 - 8Preservative: 0.09% Sodium azideConstituents: Tris citrate/phosphate, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Glutaminyl-tRNA synthetase (GlnRS) is an enzyme that catalyzes the attachment of glutamine to its corresponding tRNA molecule facilitating protein synthesis. Known also as QARS or GLNRS GlnRS has a molecular mass of approximately 75 kilodaltons. This enzyme is expressed in both prokaryotic and eukaryotic organisms indicating its fundamental role across diverse biological systems. In eukaryotes GlnRS is usually located in the cytoplasm where protein biosynthesis occurs. The structure of GlnRS includes an anticodon binding domain which allows it to recognize and bind specifically to tRNA^Gln.
Biological function summary
GlnRS ensures the correct translation of genetic information into proteins by attaching glutamine to the appropriate tRNA forming glutaminyl-tRNA^Gln. GlnRS operates as a monomer rather than being part of a larger protein complex. This activity is important for maintaining the fidelity of protein translation as it ensures that the amino acid sequence of the protein matches the codon sequence of the mRNA. Errors in tRNA charging can lead to the incorporation of incorrect amino acids potentially resulting in nonfunctional or deleterious proteins.
Pathways
GlnRS plays an important role in the aminoacyl-tRNA biosynthesis pathway which is integral for the translation of genetic information into functional proteins. This pathway is part of the larger translation machinery connecting genetic code with amino acid sequences. GlnRS is closely related to other aminoacyl-tRNA synthetases such as alanyl-tRNA synthetase (AlaRS) and leucyl-tRNA synthetase (LeuRS) which similarly charge their respective tRNAs. However each synthetase maintains particular specificity to ensure correct protein synthesis.
Disruptions in the function of GlnRS can relate to neurological disorders such as Charcot-Marie-Tooth disease due to its role in protein biosynthesis. Mutations in GlnRS or associated aminoacyl-tRNA synthetases like GlyRS have been documented in these disorders. Misregulation of GlnRS can lead to impaired protein synthesis and accumulation of misfolded proteins contributing to disease pathogenesis. Understanding the relationship between GlnRS and disease helps in developing potential therapeutic targets for related conditions.