AspRS Antibody (C-6): sc-166535

AspRS Antibody (C-6) is a mouse monoclonal IgG2a kappa light chain antibody that detects AspRS protein of human origin by western blotting (WB), immunoprecipitation (IP), immunofluorescence (IF), immunohistochemistry with paraffin-embedded sections (IHCP), and enzyme-linked immunosorbent assay (ELISA). anti-AspRS antibody (C-6) 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. AspRS, or mitochondrial aspartyl-tRNA synthetase, is a crucial 645 amino acid protein that plays a vital role in protein synthesis by aminoacylating tRNA with aspartic acid, which is essential for the accurate translation of mRNA into proteins. AspRS is localized in the mitochondrial matrix, where AspRS exists as a homodimer and is responsible for ensuring that the correct amino acid is attached to its corresponding tRNA, thereby maintaining the fidelity of protein synthesis. A 47 amino acid mitochondrial targeting signal is critical for AspRS localization, while conserved residues facilitate ATP binding, tRNA binding, and aspartic acid recognition. The gene encoding AspRS is located on chromosome 1q25.1, and mutations in this gene can lead to leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation (LBSL), an autosomal recessive disorder characterized by symptoms such as cerebellar ataxia, spasticity, and dorsal column dysfunction, which may also include mild cognitive deficits.

Alexa Fluor^® is a trademark of Molecular Probes Inc., OR., USA

LI-COR^® and Odyssey^® are registered trademarks of LI-COR Biosciences

AspRS Antibody (C-6) References:

1. Magnesium ion-mediated binding to tRNA by an amino-terminal peptide of a class II tRNA synthetase.  |  Hammamieh, R. and Yang, DC. 2001. J Biol Chem. 276: 428-33. PMID: 11035022
2. Loss of a primordial identity element for a mammalian mitochondrial aminoacylation system.  |  Fender, A., et al. 2006. J Biol Chem. 281: 15980-6. PMID: 16597625
3. Molecular dynamics simulations show that bound Mg2+ contributes to amino acid and aminoacyl adenylate binding specificity in aspartyl-tRNA synthetase through long range electrostatic interactions.  |  Thompson, D. and Simonson, T. 2006. J Biol Chem. 281: 23792-803. PMID: 16774919
4. A non-discriminating aspartyl-tRNA synthetase from Halobacterium salinarum.  |  Cardoso, AM., et al. 2006. RNA Biol. 3: 110-4. PMID: 17114946
5. Amino acid residues required for maturation, cell uptake, and processing of translation inhibitor microcin C.  |  Kazakov, T., et al. 2007. J Bacteriol. 189: 2114-8. PMID: 17158672
6. Inhibition by L-aspartol adenylate of a nondiscriminating aspartyl-tRNA synthetase reveals differences between the interactions of its active site with tRNA(Asp) and tRNA(Asn).  |  Bernard, D., et al. 2007. J Enzyme Inhib Med Chem. 22: 77-82. PMID: 17373551
7. Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation.  |  Scheper, GC., et al. 2007. Nat Genet. 39: 534-9. PMID: 17384640
8. Peculiar inhibition of human mitochondrial aspartyl-tRNA synthetase by adenylate analogs.  |  Messmer, M., et al. 2009. Biochimie. 91: 596-603. PMID: 19254750
9. Dual targeting of a tRNAAsp requires two different aspartyl-tRNA synthetases in Trypanosoma brucei.  |  Charrière, F., et al. 2009. J Biol Chem. 284: 16210-16217. PMID: 19386587
10. Plasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparum.  |  Bour, T., et al. 2009. J Biol Chem. 284: 18893-903. PMID: 19443655
11. Template-based structure prediction and molecular dynamics simulation study of two mammalian Aspartyl-tRNA synthetases.  |  Ul-Haq, Z., et al. 2010. J Mol Graph Model. 28: 401-12. PMID: 19896876
12. Service and unity: the 1997 ASPRS presidential address. American Society of Plastic and Reconstructive Surgeons.  |  Iverson, RE. 1998. Plast Reconstr Surg. 101: 1386-8. PMID: 9529231

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-AspRS Antibody (C-6) has 0 citations in a variety of scientific publications.

Primary antibodies like Anti-AspRS Antibody (C-6) 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.

AspRS Antibody (C-6) Specifications

Alternate Product Name: AspRS

Product Clone Name: C-6

Classification: Primary Antibody

Clonality: Monoclonal Antibody

Antibody Isotype: IgG_2a kappa light chain

Amino Acids: 346-645

Epitope Target: AspRS

Epitope Species: human

Product Reactivity/Detection: AspRS

Species Reactivity/Detection: 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 IgG_2a kappa light chain in 1.0 ml of PBS with < 0.1% sodium azide and 0.1% gelatin

Research Citations: 0 citations in various scientific publications

Available Conjugates/Forms for AspRS Antibody (C-6): 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