Prion is a cell surface glycoprotein present in two isoform- PrPc (a cellular isoform) and PrPsc (a disease associated isoform). Monoclonal anti-prion protein antibody is useful for the treatment of prion disease, by inhibiting the abnormal isoform PrPsc . This antibody can also be used for passive immunization of animals to protect them from prion infection. Anti prion protein antibody may be used to inhibit abnormal prion protein accumulation in cultured scrapie-infected neuroblastoma cells. The antibody reacts specifically with amino acids 145-180 of human prion. It also has specificity for monkey, cow, sheep, deer, squirrel, hamster, mouse and rat.
Synonyms: Monoclonal Anti-Prion Protein antibody produced in mouse; Anti-AA960666; Anti-CD230; Anti-PRIP; Anti-PrP; Anti-PrP; Anti-PrPSc; Anti-Prn-i; Anti-RP23-401J24.1; Anti-Sinc
MDL Number: MFCD01865558
Storage: -20C
Application: Anti-Prion Protein antibody, mouse monoclonal may be used in:
•immunoblotting
•flow cytometry
•immunocytochemistry
•immunoprecipitation
•immunoelectron microscopy
•immunohistochemistry
•enzyme linked immunosorbent assay
Biochem Physiol Actions: Prion-related diseases are fatal neurodegenerative disorders also known as transmissible spongiform encephalopathies (TSEs). Prion plaques are of three types: unicentric (single, compact core), multicentric (two or more cores and definite border), and diffuse plaques without a definite central core. Disease-associated prion protein specifically inhibits the proteolytic β-subunits of the 26S proteasome. This may clarify the mechanism of cell death by the prion protein. Prion protein may be involved in copper utilization, serving to buffer copper at the synaptic cleft or to mediate re-uptake of copper into the presynapse. Alternatively, bound copper may influence PrP binding characteristics. The PrP-copper complex may be crucial for synaptic homeostasis as a result of its antioxidant activity.
RIDADR: NONH for all modes of transport
WGK Germany: 3