Prion diseases, or transmissible spongiform encephalopathies (TSEs), are manifested as genetic, infectious or sporadic, lethal neurodegenerative disorders involving alterations of the prion protein (PrP). Characteristic of prion diseases, cellular PrP (PrPc) is converted to the disease form, PrPSc, through alterations in the protein folding conformations. PrPc is constitutively expressed in normal adult brain and is sensitive to proteinase K digestion, while the altered PrPSc conformation is resistant to proteases, resulting in a distinct molecular mass after PK treatment. Consistent with the transient infection process of prion diseases, incubation of PrPc with PrPSc both in vitro and in vivo produces PrPc that is resistant to protease degradation. Infectious PrPSc is found at high levels in the brains of animals affected by TSEs, including scrapie in sheep, BSE in cattle and Cruetzfeldt-Jakob disease in humans.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of PrP of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine and bovine
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-253 representing full length prion protein
Tissue Specificity
epitope corresponding to amino acids 1-253 representing full length prion protein
Western blot analysis of PrP expression in rat brain (A) and mouse brain (B) tissue extracts.
Application Notes
recommended for detection of PrP of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine and bovine
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.