Anti-PION

Anti-PION Antibody was affinity purified from monospecific antiserum by immunoaffinity purification. A BLAST analysis was used to suggest cross-reactivity with PION with Human, Rat and Mouse based on 100% homology with the immunizing sequence. Cross-reactivity with PION from other sources has not been determined. Multiple isoforms of PION are known to exist. PION antibody is predicted to not cross-react with other F-box protein family members. Pion antibody detects human PION. Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. The beta?amyloid protein precursor (APP) is cleaved by one of two beta?secretases (BACE and BACE2), producing a soluble derivative of the protein and a membrane anchored 99 -amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma?secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the Alzheimer's disease patients' brains. PION, or GSAP, selectively increases amyloid-beta production through a mechanism involving its interaction with both gamma-secretase and the APP C-terminal fragment, suggesting that PION may be a potential therapeutic target for the treatment of Alzheimer's disease. Anti-PION antibodies are ideal for investigators involved in neuroscience research.