Recombinant Rabbit monoclonal primary
Prion Protein(PrP) Recombinant Rabbit Monoclonal Antibody [SC57-05] (ET1610-27)
Rat brain tissue lysates, N2A, SHG-44, SH-SY5Y, rat brain tissue, mouse brain tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
Alternative prion protein; major prion protein antibody; AltPrP antibody; ASCR antibody; CD230 antibody; CD230 antigen antibody; CJD antibody; GSS antibody; KURU antibody; Major prion protein antibody; p27 30 antibody; PRIO_HUMAN antibody; Prion protein antibody; Prion related protein antibody; PRIP antibody; PRNP antibody; PrP antibody; PrP27 30 antibody; PrP27-30 antibody; PrP33-35C antibody; PrPC antibody; PrPSc antibody; Sinc antibody
Belongs to the prion family.
The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.
Golgi apparatus, Cell membrane.
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.