GlyRS Antibody (H-1): sc-271778

GlyRS Antibody (H-1) is a mouse monoclonal IgG1 antibody that detects GlyRS in mouse, rat, and human samples through applications such as western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), and enzyme-linked immunosorbent assay (ELISA). GlyRS, or Glycyl-tRNA synthetase, is a crucial enzyme composed of 739 amino acids that plays a vital role in protein synthesis by catalyzing the attachment of glycine to its corresponding tRNA, thereby ensuring the accurate translation of genetic information into functional proteins. This process is essential for maintaining cellular function and integrity, as any errors in protein synthesis can lead to severe consequences, including neurodegenerative diseases. Notably, defects in the GlyRS gene are linked to Charcot-Marie-Tooth disease type 2D (CMT2D), an autosomal dominant disorder characterized by significant muscle weakness and atrophy, particularly affecting the upper extremities. Additionally, mutations in the GlyRS gene are implicated in distal hereditary muscular neuropathy type V (HMN5), which presents with similar symptoms but typically with less severe sensory involvement. Anti-GlyRS antibody (H-1) is therefore an invaluable tool for researchers studying these conditions and the fundamental processes of protein synthesis.

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GlyRS Antibody (H-1) References:

1. Cocrystal structures of glycyl-tRNA synthetase in complex with tRNA suggest multiple conformational states in glycylation.  |  Qin, X., et al. 2014. J Biol Chem. 289: 20359-69. PMID: 24898252
2. Vanderwaltozyma polyspora possesses two glycyl-tRNA synthetase genes: one constitutive and one inducible.  |  Chien, CI., et al. 2015. Fungal Genet Biol. 76: 47-56. PMID: 25683380
3. Neddylation requires glycyl-tRNA synthetase to protect activated E2.  |  Mo, Z., et al. 2016. Nat Struct Mol Biol. 23: 730-7. PMID: 27348078
4. Glycyl-tRNA synthetase from Nanoarchaeum equitans: The first crystal structure of archaeal GlyRS and analysis of its tRNA glycylation.  |  Fujisawa, A., et al. 2019. Biochem Biophys Res Commun. 511: 228-233. PMID: 30771900
5. Associations between Neurological Diseases and Mutations in the Human Glycyl-tRNA Synthetase.  |  Vinogradova, ES., et al. 2021. Biochemistry (Mosc). 86: S12-S23. PMID: 33827397
6. The binding mode of orphan glycyl-tRNA synthetase with tRNA supports the synthetase classification and reveals large domain movements.  |  Han, L., et al. 2023. Sci Adv. 9: eadf1027. PMID: 36753552
7. Structural basis of a two-step tRNA recognition mechanism for plastid glycyl-tRNA synthetase.  |  Yu, Z., et al. 2023. Nucleic Acids Res. 51: 4000-4011. PMID: 36912079
8. Glycyl-tRNA Synthetase Induces Psoriasis-Like Skin by Facilitating Skin Inflammation and Vascular Endothelial Cell Angiogenesis.  |  Zheng, YX., et al. 2024. J Invest Dermatol. 144: 774-785.e10. PMID: 37827278
9. Common evolutionary origins of the bacterial glycyl tRNA synthetase and alanyl tRNA synthetase.  |  Alvarez-Carreño, C., et al. 2023. Protein Sci. 33: e4844. PMID: 38009704
10. The polyphyletic origins of glycyl-tRNA synthetase and lysyl-tRNA synthetase and their implications.  |  Di Giulio, M. 2024. Biosystems. 244: 105287. PMID: 39127441

The preferred GlyRS antibody is GlyRS Antibody (D-10): sc-365311.