|Reactivity||Human, Mouse, Rat|
|Calculated MW||50140 Da|
|Other Names||Presenilin-2, PS-2, 3423-, AD3LP, AD5, E5-1, STM-2, Presenilin-2 NTF subunit, Presenilin-2 CTF subunit, PSEN2, AD4, PS2, PSNL2, STM2|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding serine 327 of human Presenilin 2 was used as an immunogen. This antibody detects Presenilin 2 phosphorylated on serine 327.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Presenilin-2 Antibody Phospho (pS327) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||AD4, PS2, PSNL2, STM2|
|Function||Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors and APP (amyloid-beta precursor protein). Requires the other members of the gamma-secretase complex to have a protease activity. May play a role in intracellular signaling and gene expression or in linking chromatin to the nuclear membrane. May function in the cytoplasmic partitioning of proteins.|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein|
|Tissue Location||Isoform 1 is seen in the placenta, skeletal muscle and heart while isoform 2 is seen in the heart, brain, placenta, liver, skeletal muscle and kidney|
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Provided below are standard protocols that you may find useful for product applications.
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).
1. Steiner H, et al. J Biol Chem. 274(40):28669-73, 1999.
2. Walter J, et al. Proc Natl Acad Sci U S A 96:1391-6, 1999.
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