|Tested species reactivity||Sheep|
|Published species reactivity||Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic Peptide: G(90) Q G G G T H N Q W N K P(102) G G C|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS with 1mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunohistochemistry (Frozen) (IHC (F))||1:20|
|Immunoprecipitation (IP)||Assay dependent|
|Western Blot (WB)||1:1,000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
|Immunoprecipitation (IP)||See 1 publications below|
PA1-750 detects prion protein (PrP) from sheep tissues.
PA1-750 has been successfully used in Western blot, immunoprecipitation and immunohistochemistry procedures. By Western blot, this antibody detects a 33-35 kDa protein representing PrPC and a 27-30 kDa protein representing PrPSc from sheep normal and infected brains. Immunohistochemical staining of PrP in formalin-fixed infected sheep brain with PA1-750 results in intense staining of PrP plaques which are known to exhibit an abnormally high concentration of PrP.
PA1-750 immunizing peptide corresponds to amino acid residues 90-102 from hamster PrP. PA1-750 immunizing peptide (Cat. # PEP-034) is available for use in neutralization and control experiments.
Cellular prion protein (PrPC) is a highly conserved, 33-35 kDa protease-sensitive, sialoglycoprotein of unknown function which is endogenously expressed in brain. Studies have shown this protein to be anchored to the external surface of the cell membrane by glycosyl phosphatidylinositol. A post-translationally altered, protease-resistant PrPC isoform ( PrP-Scrapie or PrPSc) of 27-30 kDa is found in association with several fatal neurodegenerative disorders collectively termed transmissible spongiform encephalopathies (TSEs). Deposition of PrPSc in the central nervous system is a reliable indication of a TSE. Prion diseases include scrapie in sheep and goats, bovine spongiform encephalopathy or "Mad Cow disease", and chronic wasting disease (CWD) in deer and elk. PrP is responsible for Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker (GSS) disease, Fatal Familial Insomnia (FFI), and Kuru in humans.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Lipid rafts act as specialized domains for tetanus toxin binding and internalization into neurons.
PA1-750 was used in immunoprecipitation to study the mechanism of tetanus toxin binding and internalization.
|Herreros J,Ng T,Schiavo G||Molecular biology of the cell (12:2947)||2001|