Presenilin 1 Monoclonal Antibody (APS 11), Invitrogen™

Description

MA1-751 detects presenilin 1 protein (PS1) from mouse, rat, human, and nonhuman primate samples. No cross-reactivity is seen with presenilin 2. MA1-751 has successfully been used immunofluorescence, immunocytochemistry, immunohistochemistry, Western blot , and ELISA procedures. By Western blot, this antibody detects an ∽28 kDa protein representing PS1 N-terminus cleavage product from ST15 cell lysate transfected with human PS1. In formalin-fixed, paraffin embedded sections of human brain, this antibody showed strong staining of both the plaque core and dystrophic neurites. The MA1-751 immunogen is a synthetic peptide corresponding to residues C H(21) L S N T V R S Q N D N R E(34) of human PS1.

Presenilin1 was initially identified a marker of susceptibility to early-onset Alzheimer's disease. In addition to PEN2, nicastrin and APH-1, Presenilin1 forms the -gamma-secretase protein complex, a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer. This cleavage is responsible for a key step in signaling from several cell-surface receptors and is thought to be required for the generation of the neurotoxic amyloid peptides that are central to the pathogenesis of Alzheimer's disease. Like the tumor necrosis factor-alpha-converting enzyme (TACE) and the beta-site cleavage enzyme (BACE) protease families, -gamma-secretase will cleave the amyloid precursor protein (APP), but within the intramembrane region of APP, resulting in either the non-toxic p3 (from the alpha and -gamma cleavage site) or the toxic Abeta amyloid peptide (from the beta and -gamma cleavage site). It is thought that accumulation of the Abeta peptide is the precursor to Alzheimer's disease. Multiple isoforms of presenilin1 are known to exist.