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Mouse Monoclonal to CD230 / Human Prion Protein (PrP)

EM-20 (IgG2a)

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Background

CD230 / Human prion protein (PrP), also known as PRNP, is a ubiquitously expressed GPI-anchored cell surface glycoprotein associating with lipid raft components and functioning as a signaling molecule. CD230 / PrP plays a role in apoptosis in a cell context-dependent manner, is involved in proliferation of epithelial cells and in distribution of junction-associated proteins in human enterocytes. Conversion of this normal cellular prion protein (PrPc) into an abnormal conformer (PrPSc) is the crucial step associated with triggering the pathogenesis of the prion neurodegenerative disorders, such as the Creutzfeld-Jakob disease (CJD). Whereas PrPc is rich in alpha-helices, the PrPSc form has higher content of beta-sheets and is resistant to proteinase K.

Specificity

The mouse monoclonal antibody EM-20 recognizes human prion protein (PrP). Diglycosylated form of PrP has ~ 40 kDa, monoglycosylated form ~ 30 kDa, and nonglycosylated form ~ 19-21 kDa. This antibody is suitable for discrimination between normal cellular prion protein (PrPc) and its conformationally changed form (PrPSc) prion protein.

Regulatory Status

Immunogen

Recombinant human prion protein

Species Reactivity:

  • Human

Negative Species:

Applications:

  • Western Blotting
    Recommended dilution: 0.5 μg/ml
    Note:Non-reducing conditions are essential
Usage note:
Indicated dilutions are recommended starting points for use of this product. Working concentrations should be determined by the investigator.

General references

  • *Wang X, Dong CF, Shi Q, Shi S, Wang GR, Lei YJ, Xu K, An R, Chen JM, Jiang HY, Tian C, Gao C, Zhao YJ, Han J, Dong XP: Cytosolic prion protein induces apoptosis in human neuronal cell SH-SY5Y via mitochondrial disruption pathway. BMB Rep. 2009 Jul 31;42(7):444-9. [Abstract] [Full Text]
  • *Segarra C, Lehmann S, Coste J: Prion protein expression and processing in human mononuclear cells: the impact of the codon 129 prion gene polymorphism. PLoS One. 2009 Jun 4;4(6):e5796. [Abstract] [Full Text]
  • *Yang Y, Chen L, Pan HZ, Kou Y, Xu CM: Glycosylation modification of human prion protein provokes apoptosis in HeLa cells in vitro. BMB Rep. 2009 Jun 30;42(6):331-7. [Abstract] [Full Text]
  • *Ermonval M, Baudry A, Baychelier F, Pradines E, Pietri M, Oda K, Schneider B, Mouillet-Richard S, Launay JM, Kellermann O: PLoS One. 2009 Aug 4;4(8):e6497. [Abstract] [Full Text]
  • *Li C, Yu S, Nakamura F, Yin S, Xu J, Petrolla AA, Singh N, Tartakoff A, Abbott DW, Xin W, Sy MS: Binding of pro-prion to filamin A disrupts cytoskeleton and correlates with poor prognosis in pancreatic cancer. J Clin Invest. 2009 Aug 17. pii: 39542. doi: 10.1172/JCI39542. [Epub ahead of print] [Abstract] [Full Text]
  • Product Specific References

  • *Dvorakova E, Vranac T, Janouskova O, Černilec M, Koren S, Lukan A, Nováková J, Matej R, Holada K, Čurin Šerbec V: Detection of the GPI-anchorless prion protein fragment PrP226* in human brain. BMC Neurol. 2013 Sep 25;13:126. [Abstract] [Full Text]
  • For research use only. Not for drug, diagnostic or other use.

    Example Data

    PrP
    Fig. 1.

    Fig. 1. Western blotting analysis of Creutzfeld-Jakob disease (CJD) negative (lane 1, 2) and CJD positive (lane 3, 4) human brain material using anti-PrP antibody (clone EM-20). CJD positive patient has proteinase K resistent prion protein.
    Lane 1, 4: Samples with proteinase K treatment
    Lane 2, 3: Samples without proteinase K treatment



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