Anti-Prion Protein (Ser-43), Phosphospecific Antibody

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.

Our Prion Protein (Ser-43) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat Prion Protein (Ser-43) and is antigen affinity purified. It is great for use in WB.

Prion Protein (Ser-43) antibody was generated from a phospho-peptide that included amino acids surrounding Serine 43 in human prion protein. This sequence has high homology to the conserved site in rat, mouse, and bovine prion protein.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.

The antibody detects a human recombinant Prion protein after phosphorylation by Cdk5/p25 complex. In addition, the antibody may detect aggregrated forms of prion in human PC3 cells treated with Calyculin A.