Date published: 2025-12-18

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FARSLA Antibody (L-8): sc-100987

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Datasheets
  • FARSLA Antibody (L-8) is a mouse monoclonal IgG1 κ FARSLA antibody, cited in 1 publications, provided at 100 µg/ml
  • raised against recombinant FARSLA of human origin
  • recommended for detection of FARSLA of human origin by WB, IP and ELISA
  • At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for FARSLA Antibody (L-8). This work is in progress.

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FARSLA Antibody (L-8) is a mouse monoclonal IgG1 kappa light chain antibody that detects the FARSLA protein of human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-FARSLA antibody (L-8) is available as the non-conjugated form. FARSLA, also known as FRSA, CML33, FARSL, or phenylalanyl-tRNA synthetase alpha subunit (PheHA), plays a crucial role in protein synthesis as a member of the class-II aminoacyl-tRNA synthetase family. FARSLA (L-8) antibody recognizes a protein primarily located in the cytoplasm, where FARSLA functions as a heterodimer composed of a catalytic α-subunit and a regulatory β-subunit. The α-subunit is essential for forming the amino acid binding pocket, mediating ATP/aminoacyl adenylate binding, and interacting with the acceptor stem of tRNA, which is vital for accurate translation of genetic information into proteins. FARSLA is highly expressed in proliferating cells of the bone marrow and operates in a cell cycle-dependent and differentiation-dependent manner, underscoring its importance in cellular growth and development. FARSLA′s ability to ensure correct aminoacylation of tRNA is critical for maintaining protein synthesis fidelity, which is fundamental for cellular function and response to physiological changes.

For Research Use Only. Not Intended for Diagnostic or Therapeutic Use.

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

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

FARSLA Antibody (L-8) References:

  1. Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells.  |  Rodova, M., et al. 1999. Biochem Biophys Res Commun. 255: 765-73. PMID: 10049785
  2. Cloning of the cDNA encoding phenylalanyl tRNA synthetase regulatory alpha-subunit-like protein whose expression is down-regulated during differentiation.  |  Zhou, X., et al. 1999. Gene. 233: 13-9. PMID: 10375616
  3. Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes.  |  Moor, N., et al. 2002. Protein Expr Purif. 24: 260-7. PMID: 11858721
  4. Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end.  |  Moor, N., et al. 2003. Biochemistry. 42: 10697-708. PMID: 12962494
  5. Phenylalanyl-tRNA synthetase contains a dispensable RNA-binding domain that contributes to the editing of noncognate aminoacyl-tRNA.  |  Roy, H. and Ibba, M. 2006. Biochemistry. 45: 9156-62. PMID: 16866361
  6. The crystal structure of the ternary complex of phenylalanyl-tRNA synthetase with tRNAPhe and a phenylalanyl-adenylate analogue reveals a conformational switch of the CCA end.  |  Moor, N., et al. 2006. Biochemistry. 45: 10572-83. PMID: 16939209
  7. FrsA functions as a cofactor-independent decarboxylase to control metabolic flux.  |  Lee, KJ., et al. 2011. Nat Chem Biol. 7: 434-6. PMID: 21623357
  8. Computational, structural, and kinetic evidence that Vibrio vulnificus FrsA is not a cofactor-independent pyruvate decarboxylase.  |  Kellett, WF., et al. 2013. Biochemistry. 52: 1842-4. PMID: 23452154
  9. Caroline Drummond MBE, Hon DSc, NSch, FRAgS, FIAgM, FRSA, FSB, CEnv, BSc (Hons) Agric.  |  Dennis, C. 2022. Nutr Bull. 47: 374-375. PMID: 36045108
  10. Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase.  |  Ibba, M., et al. 1995. FEBS Lett. 358: 293-6. PMID: 7843418
  11. Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site.  |  Aphasizhev, R., et al. 1996. Biochemistry. 35: 117-23. PMID: 8555164
  12. Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent.  |  Sen, S., et al. 1997. Proc Natl Acad Sci U S A. 94: 6164-9. PMID: 9177188

Ordering Information

Product NameCatalog #UNITPriceQtyFAVORITES

FARSLA Antibody (L-8)

sc-100987
100 µg/ml
$333.00

For Western Blot, is it recommended to use denatured or non-denatured conditions with FARSLA (L-8): sc-100987 antibody?

Asked by: cjMara
Thank you for your question. We recommend this antibody for use in denatured Western Blot conditions. It has not been validated for use in non-denatured conditions. Please contact our Technical Service Department for further details or inquiries.
Answered by: Technical Support
Date published: 2017-03-27
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Rated 5 out of 5 by from Good for ELISA assayAntibody has been used to detect FARSLA by ELISA in published research. -SCBT QC
Date published: 2023-09-14
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FARSLA Antibody (L-8) is rated 4.0 out of 5 by 2.
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