Presenilin1 Antibody

Presenilin1 Antibody: 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. This antibody has no cross-reactivity to presenilin2.

Presenilin1 antibody can be stored at 4˚ C for three months and -20˚ C, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.

Sherrington R, Rogaev EI, Liang Y, et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature1995; 375:754-60.

Weihofen A and Martoglio B. Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides. Trends Cell Biol.2003; 13:71-8.

Periz G and Fortini ME. Functional reconstitution of g-secretase through coordinated expression of presenilin, nicastrin, aph-1, and pen-2. J. Neurosci. Res.2004; 77:309-22.