Dieser Maus Monoklonal Antikörper detektiert spezifisch Prion Prpsc in IA, IHC (p) und WB. Es zeigt Reaktivität gegenüber Proben von Chemical. Es wurde in 2+ Publikationen zitiert.
For immunohistochemistry, and Western blotting, dilutions to be used depend on detection system applied. It is recommended that users test the reagent and determine their own optimal dilutions. The typical starting working dilution is 1:50. 1
Beschränkungen
Nur für Forschungszwecke einsetzbar
Buffer
PBS, containing 0.1 % bovine serum albumin and 0.02 % sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C
Informationen zur Lagerung
Product should be stored at 4 °C. Under recommended storage conditions, product is stable for at least one year. The exact expiry date is indicated on the label.
Cordes, Bergström, Ohm, Laursen, Heegaard: "Characterisation of new monoclonal antibodies reacting with prions from both human and animal brain tissues." in: Journal of immunological methods, Vol. 337, Issue 2, pp. 106-20, (2008) (PubMed).
Bergström, Jensen, Heegaard, Cordes, Hansen, Laursen, Lind: "Short-term study of the uptake of PrP(Sc) by the Peyer's patches in hamsters after oral exposure to scrapie." in: Journal of comparative pathology, Vol. 134, Issue 2-3, pp. 126-33, (2006) (PubMed).
Target
Prion Prpsc
Substanzklasse
Chemical
Hintergrund
The monoclonal antibody 1.5D7 recognizes the disease associated isoform of the prion protein Sc termed PrP . Prion diseases, also known as spongiform encephalopathies, are a group of neurodegenerative diseases that include BSE (bovine spongiform encephalopathy) in cattle, scrapie in sheep and CJD (Creutzfeldt-Jakob disease) in humans. The normal cellular form of the prion C protein is denoted as PrP and is a constitutively expressed glycosylphosphatidylinositol anchored C protein that has been shown to play a role in myelin formation. PrP has an unstructured N-terminal part and a C-terminal part consisting of three α -helices and two short β strands. Refolding of the Sc normal prion protein results in PrP , which has a tightly packed C-terminal part enriched in beta sheets which is insoluble and resistant to digestion by proteases. Prion diseases are characterized by Sc the deposition of highly structured aggregates of PrP , astrocytosis, neuronal cell death and spongiform structures in the brain. These diseases can be sporadically (unknown cause), be inherited due to polymorphisms or mutations in the prion protein gene or be transmitted by an infectious particle Sc Sc which is believed to consist of PrP only. In order to study prion diseases the detection of PrP and the ability to discriminate between the normal and disease associated PrP is of pivotal importance. The monoclonal antibody 1.5D7 can be used for the specific identification and characterization of Sc PrP in tissue sections by immunohistochemistry and PET-blot. Aliases Spongiform encephalopathies Immunogen BoPrP153-165 (GSDYEDRYYRENM)