Overview
- Peptide (C)DSRPGPEDGENTAQWR, corresponding to amino acid residues 33-48 of rat Presenilin-2 (Accession O88777). Intracellular, N-terminus.
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).
Western blot analysis of mouse liver membrane:1. Anti-Presenilin-2 Antibody (#AIP-012), (1:200).
2. Anti-Presenilin-2 Antibody, preincubated with Presenilin-2 Blocking Peptide (#BLP-IP012).
Western blot analysis of human liver carcinoma HepG2 (lanes 1 and 3) and rat pheochromocytoma PC12 (lanes 2 and 4) cell lysates:1, 2. Anti-Presenilin-2 Antibody (#AIP-012), (1:200).
3, 4. Anti-Presenilin-2 Antibody, preincubated with Presenilin-2 Blocking Peptide (#BLP-IP012).
Expression of Presenilin-2 in mouse midbrainImmunohistochemical staining of perfusion-fixed frozen mouse brain sections with Anti-Presenilin-2 Antibody (#AIP-012), (1:200), followed by goat anti-rabbit-AlexaFluor-488. A. Presenilin-2 immunoreactivity (green) appears in neurons along the midline (horizontal arrows) and away from midline (vertical arrows). B. Pre-incubation of the antibody with Presenilin-2 Blocking Peptide (BLP-IP012), suppressed staining. Cell nuclei are stained with DAPI (blue).
- Johnson, D.S. et al. (2017) Cold Spring Harb. Perspect. Med. 7, a024067.
- Fluhrer, R. et al. (2009) J. Biol. Chem. 284, 13975.
- Wolfe, M.S. (2013) Biochim. Biophys. Acta 1828, 2886.
- Sannerud, R. et al (2016) Cell 166, 193.
- De Strooper, B. et al. (2012) Cold Spring Harb. Perspect. Med. 2, a006304.
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.
Anti-Presenilin-2 Antibody (#AIP-012) is a highly specific antibody directed against an epitope of the rat protein. The antibody can be used in western blot and immunohistochemistry applications. It has been designed to recognize PSEN2 from rat, mouse, and human samples.
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