GlyRS Antibody (D-10): sc-365311

GlyRS Antibody (D-10) is a mouse monoclonal IgG2b kappa light chain antibody that detects GlyRS protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). Anti-GlyRS antibody (D-10) is available in both non-conjugated and various conjugated forms, including agarose, horseradish peroxidase (HRP), phycoerythrin (PE), fluorescein isothiocyanate (FITC), and multiple Alexa Fluor® conjugates. Glycyl-tRNA synthetase (GlyRS) plays a crucial role in protein synthesis by catalyzing the attachment of glycine to corresponding tRNA, a process essential for accurate translation of genetic information into functional proteins. GlyRS (D-10) monoclonal antibody targets a class II aminoacyl-tRNA synthetase consisting of 739 amino acids, with widespread expression in tissues such as brain and spinal cord. Mutations in GlyRS have been linked to Charcot-Marie-Tooth disease type 2D (CMT2D), an autosomal dominant disorder characterized by muscle weakness and atrophy, particularly affecting upper extremities, as well as distal hereditary muscular neuropathy type V (HMN5), which presents with less severe sensory involvement. GlyRS′s role in ensuring protein synthesis fidelity underscores its significance in maintaining cellular function and overall organismal health, making anti-GlyRS antibody (D-10) a valuable research tool for studying these critical pathways.

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GlyRS Antibody (D-10) References:

1. Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.  |  Antonellis, A., et al. 2003. Am J Hum Genet. 72: 1293-9. PMID: 12690580
2. Inherited neuropathies: new genes don't fit old models.  |  Scherer, SS. 2006. Neuron. 51: 672-4. PMID: 16982409
3. An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model.  |  Seburn, KL., et al. 2006. Neuron. 51: 715-26. PMID: 16982418
4. Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons.  |  Antonellis, A., et al. 2006. J Neurosci. 26: 10397-406. PMID: 17035524
5. Severe childhood SMA and axonal CMT due to anticodon binding domain mutations in the GARS gene.  |  James, PA., et al. 2006. Neurology. 67: 1710-2. PMID: 17101916
6. Crystallization and preliminary X-ray diffraction analysis of an Escherichia coli tRNA(Gly) acceptor-stem microhelix.  |  Förster, C., et al. 2007. Acta Crystallogr Sect F Struct Biol Cryst Commun. 63: 46-8. PMID: 17183173
7. CMT2D neuropathy is linked to the neomorphic binding activity of glycyl-tRNA synthetase.  |  He, W., et al. 2015. Nature. 526: 710-4. PMID: 26503042
8. Large Conformational Changes of Insertion 3 in Human Glycyl-tRNA Synthetase (hGlyRS) during Catalysis.  |  Deng, X., et al. 2016. J Biol Chem. 291: 5740-5752. PMID: 26797133
9. Mutations in glycyl-tRNA synthetase impair mitochondrial metabolism in neurons.  |  Boczonadi, V., et al. 2018. Hum Mol Genet. 27: 2187-2204. PMID: 29648643
10. Glycyl-tRNA Synthetase (GARS) Expression Is Associated with Prostate Cancer Progression and Its Inhibition Decreases Migration, and Invasion In Vitro.  |  Khosh Kish, E., et al. 2023. Int J Mol Sci. 24: PMID: 36901698
11. Cloning, sequencing and bacterial expression of human glycine tRNA synthetase.  |  Williams, J., et al. 1995. Nucleic Acids Res. 23: 1307-10. PMID: 7753621
12. Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation.  |  Shiba, K., et al. 1994. J Biol Chem. 269: 30049-55. PMID: 7962006

Monoclonal antibodies for mammalian and non-mammalian protein targets represent essentially all targets covered by polyclonal antibodies. Over 8,300 of our antibodies are offered as ImmunoCruz^® conjugates which eliminates the need for a secondary antibody.

Santa Cruz Biotechnology antibodies have over 360,000 research citations. Anti-GlyRS Antibody (D-10) has 6 citations in a variety of scientific publications.

Primary antibodies like Anti-GlyRS Antibody (D-10) for mammalian target proteins are recommended for the detection of a range of mammalian species, primarily of mouse, rat and human species. Many mammalian antibodies are also ideal for veterinary research and reactive with ovine, porcine, caprine, feline, canine, bovine and equine protein targets. Santa Cruz Biotechnology primary monoclonal antibodies are suitable for laboratory research applications and are not intended for diagnostic or therapeutic use.

GlyRS Antibody (D-10) Specifications

Alternate Product Name: GlyRS

Product Clone Name: D-10

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG_2b kappa light chain

Amino Acids: 440-732

Epitope Target: GlyRS

Epitope Species: human

Product Reactivity/Detection: GlyRS

Species Reactivity/Detection: mouse, rat, human

Additional Mammalian Reactivity: equine, canine, bovine and porcine

Additional Non-Mammalian Reactivity: N/A

Applications: WB, IP, IF, IHC(P), ELISA

Vialing Information: Each vial contains 200 µg IgG_2b kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 6 citations in various scientific publications

Available Conjugates/Forms for GlyRS Antibody (D-10): AC: Agarose, AF488: Alexa Fluor^® 488, AF546: Alexa Fluor^® 546, AF594: Alexa Fluor^® 594, AF647: Alexa Fluor^® 647, AF680: Alexa Fluor^® 680, AF790: Alexa Fluor^® 790, FITC: Fluoroscein, HRP: Horseradish Peroxidase, PE: Phycoerythrin