DaRS Antibody (H-3): sc-393275

DaRS Antibody (H-3) is a mouse monoclonal IgG1 kappa light chain antibody that detects DaRS protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry, and enzyme-linked immunosorbent assay (ELISA). DaRS (H-3) antibody 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. DaRS protein, a member of the aminoacyl-tRNA synthetase family, plays a crucial role in protein biosynthesis by catalyzing the specific aminoacylation of cognate tRNA, which is essential for accurate translation of the genetic code into proteins. Notably, DaRS is part of a multisubunit complex that facilitates the transfer of Asp-tRNA to elongation factor alpha 1 (EF-1 α1), a key step in the elongation phase of protein synthesis. The N-terminus of DaRS in vertebrates features a unique structure that includes a putative amphiphilic helix, which varies among species. This N-terminal extension functions as a regulatory switch; when in an extended conformation, DaRS slows the dissociation of Asp-tRNA, allowing sufficient time for EF-1 α1 to engage with Asp-tRNA. This mechanism underscores the importance of the N-terminus in enhancing the catalytic efficiency of DaRS. Additionally, DaRS contains two phosphorylation sites, forms homodimers, and is primarily localized in the cytoplasm, further emphasizing its significance in cellular processes.

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DaRS Antibody (H-3) References:

1. Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex.  |  Sang Lee, J., et al. 2002. Biochem Biophys Res Commun. 291: 158-64. PMID: 11829477
2. Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function.  |  Cheong, HK., et al. 2003. Int J Biochem Cell Biol. 35: 1548-57. PMID: 12824064
3. Engineering mammalian aspartyl-tRNA synthetase to probe structural features mediating its association with the multisynthetase complex.  |  Mirande, M., et al. 1992. Eur J Biochem. 203: 459-66. PMID: 1735430
4. Development and validation of the Dimensional Anhedonia Rating Scale (DARS) in a community sample and individuals with major depression.  |  Rizvi, SJ., et al. 2015. Psychiatry Res. 229: 109-19. PMID: 26250147
5. cDNA sequence, predicted primary structure, and evolving amphiphilic helix of human aspartyl-tRNA synthetase.  |  Jacobo-Molina, A., et al. 1989. J Biol Chem. 264: 16608-12. PMID: 2674137
6. Properties of N-terminal truncated yeast aspartyl-tRNA synthetase and structural characteristics of the cleaved domain.  |  Lorber, B., et al. 1988. Eur J Biochem. 174: 155-61. PMID: 3286258
7. lncRNA DARS-AS1 Promoted Osteosarcoma Progression through Regulating miR-532-3p/CCR7.  |  Xue, Y., et al. 2022. Dis Markers. 2022: 4660217. PMID: 35422889
8. Dysphagia-optimised intensity-modulated radiotherapy versus standard intensity-modulated radiotherapy in patients with head and neck cancer (DARS): a phase 3, multicentre, randomised, controlled trial.  |  Nutting, C., et al. 2023. Lancet Oncol. 24: 868-880. PMID: 37423227
9. DARS-AS1: A Vital Oncogenic LncRNA Regulator with Potential for Cancer Prognosis and Therapy.  |  Shu, J., et al. 2024. Int J Med Sci. 21: 571-582. PMID: 38322590
10. LncRNA DARS-AS1 in human cancers: A comprehensive review of its potency as a biomarker and therapeutic target.  |  Dang, Q. 2024. Gene. 923: 148566. PMID: 38762015
11. Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix.  |  Escalante, C. and Yang, DC. 1993. J Biol Chem. 268: 6014-23. PMID: 8449960
12. Aspartyl-tRNA synthetase from rat: in vitro functional analysis of its assembly into the multisynthetase complex.  |  Agou, F. and Mirande, M. 1997. Eur J Biochem. 243: 259-67. PMID: 9030747

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-DaRS Antibody (H-3) has 2 citations in a variety of scientific publications.

Primary antibodies like Anti-DaRS Antibody (H-3) 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.

DaRS Antibody (H-3) Specifications

Alternate Product Name: DaRS

Product Clone Name: H-3

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG₁ kappa light chain

Amino Acids: 170-467

Epitope Target: DaRS

Epitope Species: human

Product Reactivity/Detection: DaRS

Species Reactivity/Detection: mouse, rat, human

Additional Mammalian Reactivity: N/A

Additional Non-Mammalian Reactivity: N/A

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

Vialing Information: Each vial contains 200 µg IgG₁ kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 2 citations in various scientific publications

Available Conjugates/Forms for DaRS Antibody (H-3): 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