Positive Control: NIH/3T3 cell lysate, Raji cell lysate, MCF-7 cell lysate, Daudi cell lysate, mouse liver tissue lysate, rat liver tissue lysate, MCF-7, human small intestine tissue, mouse testis tissue.
Subcellular Location: Endoplasmic reticulum, Endoplasmic reticulum membrane, Golgi apparatus membrane, Cell membrane, Early endosome, Early endosome membrane, Cytoplasmic granule, growth cone, neuron projection, axon, synapse.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Alzheimer Disease 3; Minilin; Presenilin-1; Presenilin-1 CTF subunit; Presenilin-1 CTF12; Presenilin-1 NTF subunit; presenilin1; Protein S182; PS-1; PS1-CTF12; S182 protein; Senilin 1
Gene Aliases: AD3; Ad3h; FAD; PS-1; PS1; PSEN1; PSNL1; S182
Molecular Function: aspartic protease