Date published: 2026-2-14

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Cysteine Antibody (3A4): sc-69954

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Datasheets
  • Cysteine Antibody (3A4) is a mouse monoclonal IgG2a Cysteine antibody provided at 100 µg/ml
  • raised against Cysteine
  • recommended for detection of Cysteine by WB, IP and FCM
  • At present, we have not yet completed the identification of the preferred secondary detection reagent(s) for Cysteine Antibody (3A4). This work is in progress.
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    Cysteine Antibody (3A4) is a mouse monoclonal IgG2a antibody that detects the Cysteine protein of various species by western blotting (WB), immunoprecipitation (IP), and flow cytometry (FCM). Anti-Cysteine antibody (3A4) is available as a non-conjugated format. Cysteine is a non-essential α-amino acid characterized by its free thiol (-SH) side chain, which plays a crucial role in the structure and function of numerous proteins. This amino acid is found abundantly in dietary sources such as eggs, milk, pork, oats, onions, and garlic, and is recognized for antioxidant properties and ability to bind metal ions, making Cysteine valuable in pharmaceutical, food, and personal care industries. Notably, Cysteine is the most chemically reactive amino acid under physiological conditions, readily oxidizing to form cystine, a dimer linked by a disulfide bond. The significance of Cysteine extends to post-translational modifications, particularly cysteinylation, which involves the addition of a cysteine residue to a peptide. This modification is one of the most prevalent in cellular processes and can serve as a biomarker for various physiological states, including inflammation and oxidative stress, highlighting Cysteine′s importance in maintaining cellular health and responding to environmental 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

    Cysteine Antibody (3A4) References:

    1. Modification of cysteine residues in vitro and in vivo affects the immunogenicity and antigenicity of major histocompatibility complex class I-restricted viral determinants.  |  Chen, W., et al. 1999. J Exp Med. 189: 1757-64. PMID: 10359579
    2. Cysteinylation of MHC class II ligands: peptide endocytosis and reduction within APC influences T cell recognition.  |  Haque, MA., et al. 2001. J Immunol. 166: 4543-51. PMID: 11254711
    3. PKC isozyme S-cysteinylation by cystine stimulates the pro-apoptotic isozyme PKC delta and inactivates the oncogenic isozyme PKC epsilon.  |  Chu, F., et al. 2003. Carcinogenesis. 24: 317-25. PMID: 12584183
    4. Cysteinylation of maternal plasma albumin and its association with intrauterine growth restriction.  |  Bar-Or, D., et al. 2005. Prenat Diagn. 25: 245-9. PMID: 15791656
    5. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms.  |  Lill, R. and Mühlenhoff, U. 2006. Annu Rev Cell Dev Biol. 22: 457-86. PMID: 16824008
    6. S-cysteinylation is a general mechanism for thiol protection of Bacillus subtilis proteins after oxidative stress.  |  Hochgräfe, F., et al. 2007. J Biol Chem. 282: 25981-5. PMID: 17611193
    7. Removal of cysteinylation from an unpaired sulfhydryl in the variable region of a recombinant monoclonal IgG1 antibody improves homogeneity, stability, and biological activity.  |  Banks, DD., et al. 2008. J Pharm Sci. 97: 775-90. PMID: 17786988
    8. Structure-based Approaches Targeting Parasite Cysteine Proteases.  |  Vieira, RP., et al. 2019. Curr Med Chem. 26: 4435-4453. PMID: 28799498
    9. Pharmacologic role of cysteine in ameliorating or exacerbating mineral toxicities.  |  Baker, DH. and Czarnecki-Maulden, GL. 1987. J Nutr. 117: 1003-10. PMID: 3298579
    10. Cysteine and related aminothiols in cardiovascular disease, obesity and insulin resistance.  |  Pavão, ML., et al. 2022. Adv Clin Chem. 109: 75-127. PMID: 35953129
    11. Diversity and roles of cysteine desulfurases in photosynthetic organisms.  |  Caubrière, D., et al. 2023. J Exp Bot. 74: 3345-3360. PMID: 36861318
    12. Protective action of sulfur compounds against aldehyde toxicants of cigarette smoke.  |  Sprince, H. 1985. Eur J Respir Dis Suppl. 139: 102-12. PMID: 3862602

    Ordering Information

    Product NameCatalog #UNITPriceQtyFAVORITES

    Cysteine Antibody (3A4)

    sc-69954
    100 µg/ml
    $322.00