A phospho-specific peptide corresponding to residues surrounding Serine 330 in human Presenilin-2 was used as an immunogen. The antibody only detects Presenilin-2 phosphorylated on Serine 330.
Buffer
Store at -20 C. Buffer: 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Presenilin 1 (PS1) and Presenilin 2 (PS2) are transmembrane proteins which belong to Presenilin family, and their mutations are associated with early onset familial Alzheimer's disease. Presenilins facilitate gamma-secretase cleavage of the beta-amyloid precursor protein and the intramembraneous cleavage of Notch1 (1). Phosphorylation of the PS2 C-terminal fragments at serine residues 327 and 330, located immediately adjacent to the caspase recognition sites, inhibits caspase-mediated cleavage of PS2 and can regulate apoptotic cleavage. PS2 is cleaved by caspases during apoptosis between aspartate 329 and serine 330 (2).
Related Pathway
Delta-Notch Signaling Pathway
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