|Calculated MW||52668 Da|
|Other Names||Presenilin-1, PS-1, 3423-, Protein S182, Presenilin-1 NTF subunit, Presenilin-1 CTF subunit, Presenilin-1 CTF12, PS1-CTF12, PSEN1, AD3, PS1, PSNL1|
|Target/Specificity||A phospho specific peptide corresponding to residues surrounding serine 310 of human Presenilin 1 was used as an immunogen. This antibody detects Presenilin 1 phosphorylated on serine 310|
|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-1 Antibody Phospho (pS310) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||AD3, PS1, PSNL1|
|Function||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) (PubMed:15274632, PubMed:10545183, PubMed:10593990, PubMed:10206644, PubMed:10899933, PubMed:10811883, PubMed:12679784, PubMed:12740439, PubMed:25043039, PubMed:26280335). Requires the presence of the other members of the gamma-secretase complex for protease activity (PubMed:15274632, PubMed:25043039, PubMed:26280335). Plays a role in Notch and Wnt signaling cascades and regulation of downstream processes via its role in processing key regulatory proteins, and by regulating cytosolic CTNNB1 levels (PubMed:9738936, PubMed:10593990, PubMed:10899933, PubMed:10811883). Stimulates cell-cell adhesion via its interaction with CDH1; this stabilizes the complexes between CDH1 (E-cadherin) and its interaction partners CTNNB1 (beta-catenin), CTNND1 and JUP (gamma-catenin) (PubMed:11953314). Under conditions of apoptosis or calcium influx, cleaves CDH1 (PubMed:11953314). This promotes the disassembly of the complexes between CDH1 and CTNND1, JUP and CTNNB1, increases the pool of cytoplasmic CTNNB1, and thereby negatively regulates Wnt signaling (PubMed:9738936, PubMed:11953314). Required for normal embryonic brain and skeleton development, and for normal angiogenesis (By similarity).|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein Cytoplasmic granule. Cell membrane Note=Translocates with bound NOTCH1 from the endoplasmic reticulum and/or Golgi to the cell surface (PubMed:10593990). Colocalizes with CDH1/2 at sites of cell-cell contact. Colocalizes with CTNNB1 in the endoplasmic reticulum and the proximity of the plasma membrane (PubMed:9738936). Also present in azurophil granules of neutrophils (PubMed:11987239). Colocalizes with UBQLN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes (PubMed:21143716).|
|Tissue Location||Detected in azurophile granules in neutrophils and in platelet cytoplasmic granules (at protein level) (PubMed:11987239). Expressed in a wide range of tissues including various regions of the brain, liver, spleen and lymph nodes (PubMed:7596406, PubMed:8641442, PubMed:8574969)|
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Provided below are standard protocols that you may find useful for product applications.
Presenilin (PS) facilitates gamma-secretase cleavage of the beta-amyloid precursor protein and the intramembraneous cleavage of Notch1 (1). Presenilin (PS) is essential for the gamma-cleavage required for the generation of the C terminus of amyloid beta-protein (Abeta). The discovery that a deficiency of presenilin 1 (PS1) decreases the production of amyloid beta-protein (Abeta) identified the presenilins as important mediators of the gamma-secretase cleavage of beta-amyloid precursor protein (APP). It has been shown that two conserved transmembrane (TM) aspartates in PS1 are critical for Abeta production, providing evidence that PS either functions as a required diaspartyl cofactor for gamma-secretase or is itself gamma-secretase. Presenilin 2 (PS2) shares substantial sequence and possibly functional homology with PS1. It has been shown that the two TM aspartates in PS2 are also critical for gamma-secretase activity, providing further evidence that PS2 is functionally homologous to PS1 (2). Phosphorylation at serine 310 by PKACa has been linked to its proteolytic processing and apoptosis regulation (3). Heterogenous proteolytic processing generates N-terminal (NTF) and C-terminal (CTF) fragments of 35 kDa and 20 kDa respectively. During apoptosis, CTF is further cleaved by caspase-3 to produce PSI-CTF12 fragment.
1. Steiner H, et al. J Biol Chem. 274(40):28669-73, 1999.
2. Kimberly WT, et al. J Biol Chem 275(5):3173-8, 2000.
3. Fluhrer R, et al., J Biol Chem 279:1585-1593, 2004
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