A biotinylated and citrullinated α-enolase peptide
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Citrullinated α-Enolase (R8 + R14) (1-19)-biotin Peptide

Item No. 37627

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Synonyms
  • Citrullinated Enolase-1-biotin
  • α-Enolase Peptide (Citrulline Residues 8 + 14)
MW
2,381.5
Formulation (Request formulation change)
1 mg of lyophilized peptide
UniProt Accession №
P06733
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    1 mg

    $247

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    Cayman Chemical
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    Product Description

    Citrullinated α-Enolase (R8 + R14) (1-19)-biotin peptide is a biotinylated and citrullinated form of a 19-amino acid N-terminal peptide fragment of α-enolase, a glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate.1 α-Enolase also functions as a cell surface receptor for plasminogen on pathogens and activated immune cells, as an oxidative stress protein in endothelial cells, and as a chromatin binding partner to facilitate transcription.2,3,4 α-Enolase is an autoantigen in asthma, Hashimoto's encephalopathy, and rheumatoid arthritis, and has been found in the serum of pediatric patients with juvenile idiopathic arthritis.5,6,7,8 α-Enolase is also subject to citrullination by peptidyl arginine deiminases (PADs) and citrullinated α-enolase has been found in the synovial fluid of rheumatoid arthritis patients.7 Cayman’s Citrullinated α-Enolase (R8 + R14) (1-19)-biotin Peptide is intended for use in the detection of autoantibodies against α-enolase citrullinated at R8 and R13.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Zhu, X., Miao, X., Wu, Y., et al. ENO1 promotes tumor proliferation and cell adhesion mediated drug resistance (CAM-DR) in non-Hodgkin’s lymphomas. Exp. Cell Res. 335(2), 216-223 (2015).

    2. Song, Y., Luo, Q., Long, H., et al. Alpha-enolase as a potential cancer prognostic marker promotes cell growth, migration, and invasion in glioma. Mol. Cancer 13, 65 (2014).

    3. Subramanian, A., and Miller, D.M. Structural analysis of α-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene. The Journal of Biological Chemisty 275(8), 5958-5965 (2000).

    4. Hsiao, K.-C., Shih, N.-Y., Fang, H.-L., et al. Surface α-enolase promotes extracellular matrix degradation and tumor metastasis and represents a new therapeutic target. PLoS One 8(7), e69354 (2013).

    5. Nahm, D.-H., Lee, K.-H., Shin, J.-Y., et al. Identification of α-enolase as an autoantigen associated with severe asthma. J. Allergy Clin. Immunol. 118(2), 376-381 (2006).

    6. Moore, T.L., Gillian, B.E., Crespo-Pagnussat, S., et al. Measurement and evaluation of isotypes of anti-citrullinated fibrinogen and anti-citrullinated α-enolase antibodies in juvenile idiopathic arthritis. Clin. Exp. Rheumatol. 32(5), 740-746 (2014).

    7. Yoneda, M., Fujii, A., Ito, A., et al. High prevalence of serum autoantibodies against the amino terminal of α-enolase in Hashimoto’s encephalopathy. J. Neuroimmunol. 185(1-2), 195-200 (2007).

    8. Cong, Y., Wang, L., Peng, R., et al. Timosaponin AIII induces antiplatelet and antithrombotic activity via Gq-mediated signaling by the thromboxane A2 receptor. Sci. Rep. 6, 38757 (2016).