Prion related neurodegenerative diseases, called transmissible spongiform encephalopathies, are observed in many animal species.
These diseases involve conversion of normal cellular prion protein (PrPc) into a form that is insoluble and resistant to proteases (PrPSc).
The protease resistant form can polymerize into fibrils which accumulate in infected tissues and cause cell death and tissue damage.
PrPs have an N-terminal signal sequence and a C-terminal linkage to glycosylphosphatidylinositol anchor.
The mature protein is a glycosylated protein that associates with cell membranes.
Phosphorylation of PrPC at Ser-43 by Cdk5 promotes proteinase K resistance, prion aggregation, and fibril formation in vitro.
In addition, Ser-43 phosphorylation is upregulated in scrapie-infected mouse brain relative to controls.
Thus, phosphorylation of Ser-43 may be an important mechanism leading conversion of PrPc to PrPSc and the onset of disease.
Applications:Suitable for use in ELISA, Western Blot, Immunoprecipitation, Immunohistochemistry.
Other applications not tested.
Recommended Dilution:Western Blot: 1:100Immunohistochemistry: 1:200-1:1000Immunoprecipitation: 1:100Optimal dilutions to be determined by the researcher.
Storage and Stability:Lyophilized powder may be stored at -20°C.
Stable for 12 months after receipt at -20°C.
Reconstitute with ddH2O.
Aliquot to avoid repeated freezing and thawing.
Store at -20°C.
Reconstituted product is stable for 12 months at -20°C.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Further dilutions can be made in assay buffer.
仕様
Size:50ul
Host:rabbit
Grade:Ascites
Purity:Ascites
Form:Supplied as a lyophilized powder. Reconstitute with 50ul sterile ddH2O.
Specificity:Recognizes Phospho Prion Protein (Ser43). Species Crossreactivity: Mammals