|Application ||WB, IHC-P|
|Reactivity||Human, Mouse, Rat|
|Dilution||IHC-P (5 µg/ml), WB (0.5-2 µg/ml),|
|Other Names||Presenilin-1, PS-1, 3.4.23.-, Protein S182, Presenilin-1 NTF subunit, Presenilin-1 CTF subunit, Presenilin-1 CTF12, PS1-CTF12, PSEN1, AD3, PS1, PSNL1|
|Target/Specificity||a 23 amino acid peptide from near the carboxy terminus of human presenilin1|
|Reconstitution & Storage||Short term 4°C, long term aliquot and store at -20°C, avoid freeze thaw cycles. Store undiluted.|
|Precautions||PSEN1 / Presenilin 1 Antibody (C-Terminus) 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.
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 (beta-amyloid 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. Stimulates cell-cell adhesion though its association with the E-cadherin/catenin complex. Under conditions of apoptosis or calcium influx, cleaves E-cadherin promoting the disassembly of the E-cadherin/catenin complex and increasing the pool of cytoplasmic beta-catenin, thus negatively regulating Wnt signaling. May also play a role in hematopoiesis.
Sherrington R.,et al.Nature 375:754-760(1995).
Sahara N.,et al.FEBS Lett. 381:7-11(1996).
Powell C.S.,et al.Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
Rowen L.,et al.Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
Kang L.,et al.Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
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