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Anti-Prion Protein Antibody

     
  •  - Anti-Prion Protein Antibody AN1918
    Western blot of GST recombinant human full-length prion protein that was untreated (lanes 1 and 3) or phosphorylated with Cdk5/p25 (lanes 2 & 4). Endogenous prion phosphorylation was examined in human PC3 cells untreated (lanes 5 & 7) or treated with Calyculin A (100 nM) for 30 min (lanes 6 & 8). The blots were probed with anti-Prion protein (3F4) (lanes 1, 2, 5, & 6) or anti-Prion protein (Ser-43) (lanes 3, 4, 7, & 8).
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immuno electron microscopy
  • EIA=Enzyme Immunoassay
WB
Primary Accession P04156
Host Mouse
Clonality Mouse Monoclonal
Isotype IgG2a
Clone Names 3F4
Calculated MW 27661 Da
Additional Information
Gene ID 5621
Other Names PrP, PrPsc, PrPc
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-Prion Protein Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
ShippingBlue Ice
Research Areas
Citations (0)
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Background

Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species. These diseases involve conversion of normal cellular prion protein (PrPc) into a form that is insoluble and resistant to proteases (PrPSc). The protease resistant form can polymerize into fibrils which accumulate in infected tissues and cause cell death and tissue damage. PrPs have an N-terminal signal sequence and a C-terminal linkage to glycosylphosphatidylinositol anchor. The mature protein is a glycosylated protein that associates with cell membranes. Phosphorylation of PrPC at Ser-43 by Cdk5 promotes proteinase K resistance, prion aggregation, and fibril formation in vitro. In addition, Ser-43 phosphorylation is upregulated in scrapie-infected mouse brain relative to controls. Thus, phosphorylation of Ser-43 may be an important mechanism leading conversion of PrPc to PrPSc and the onset of disease.

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$ 275.00
Cat# AN1918
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