Render Target: STATIC
Render Timestamp: 2024-12-13T10:57:00.359Z
Commit: 611277b6de3cd1bb065350b6ef8d63df412b7185
XML generation date: 2024-09-30 01:53:59.580
Product last modified at: 2024-10-17T12:00:37.397Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

PRNP (D3Q5C) Rabbit mAb #14025

Filter:
  • WB
  • IP
  • IF

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 20-40
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50
    Immunofluorescence (Immunocytochemistry) 1:200

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    PRNP (D3Q5C) Rabbit mAb recognizes endogenous levels of total PRNP protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser222 of human PRNP protein.

    Background

    The PRNP gene encodes the major prion protein (PrP, CD230), a widely-expressed glycoprotein expressed at high levels in the central nervous system (1). While the typical cellular function of PrP is not well defined, it is a putative antioxidant and a metal-binding protein that may be involved in signal transduction (2). Prion proteins can adopt different conformations; the cellular PrPc prion protein may be converted following translation into the β-sheet-rich scrapie isoform (PrPsc) responsible for several prion diseases, including bovine spongiform encephalopathy and human Creutzfeldt-Jakob disease (3). Unlike most neurodegenerative diseases, prion diseases are infectious as prions are capable of propagating by conferring an abnormally folded state onto properly folded cellular proteins (3). In addition, the cellular PrPc has may be involved in β-amyloid peptide oligomerization and synaptic toxicity (4).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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