Overview
- Peptide (C)DSRPGPEDGENTAQWR, corresponding to amino acid residues 33-48 of rat Presenilin-2 (Accession O88777). Intracellular, N-terminus.
- Rat heart, mouse liver, human liver carcinoma HepG2 cell line and rat pheochromocytoma PC12 cell line (1:200-1:400).
- Western blot analysis of rat heart membrane:1. Anti-Presenilin-2 Antibody (#AIP-012), (1:400).
2. Anti-Presenilin-2 Antibody, preincubated with Presenilin-2 Blocking Peptide (#BLP-IP012).
Presenilin 2 (PS2) is the catalytic subunit of a tetrameric complex containing presenilin-1 or 2, anterior pharynx defective 1 (APH1), nicastrin, and PEN-21.
The presenilin complex is the founding member of a unique class of GXGD aspartyl proteases that catalyze the cleavage of the transmembrane domains of Type I membrane proteins including amyloid precursor protein (APP) and Notch1. Other members of this protease family include signal peptide peptidases (SPP) and a variety of archaeal homologs2.
PS1 and PS2 proteins have nine helical TM domains arranged with the hydrophilic, flexible N terminus in the cytosol and the C terminus protruding into the lumen or extracellular space3.
PS2 shares similarity with PS 1 and the crucial difference between them appears to be a “[DIE]xxxL/I/M” motif present only in PS2 which interacts in a phosphorylation dependent manner with AP-1 complexes and targets PS2 to the late endosome/lysosome complex. The absence of this sequence motif in PS1 allows for the wider subcellular location of PS1 in cell membranes4.
Presenilin mutations have been shown to be correlated with occurrence of familial Alzheimer's disease5.