|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_000012, 4506163|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||52668 Da|
|Application Notes||Presenilin1 antibody can be used for detection of presenilin1 by Western blot at 0.5 - 2 µg/mL. Antibody can also be used for immunohistochemistry starting at 2.5 µg/mL. For immunofluorescence start at 20 µg/mL.|
|Other Names||Presenilin1 Antibody: AD3, FAD, PS1, PS-1, S182, AD3, PSNL1, Presenilin-1, Protein S182, presenilin 1|
|Reconstitution & Storage||Presenilin1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||Presenilin1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||AD3, PS1, PSNL1|
|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 (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.|
|Cellular Location||Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Cell surface. Cell membrane. Note=Bound to NOTCH1 also at the cell surface. Colocalizes with CDH1/2 at sites of cell-cell contact. Colocalizes with CTNNB1 in the endoplasmic reticulum and the proximity of the plasma membrane. Also present in azurophil granules of neutrophils. Colocalizes with UBQLN1 in the cell membrane and in cytoplasmic juxtanuclear structures called aggresomes (PubMed:21143716).|
|Tissue Location||Expressed in a wide range of tissues including various regions of the brain, liver, spleen and lymph nodes|
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Provided below are standard protocols that you may find useful for product applications.
Presenilin1 Antibody: Presenilin1 was initially identified a marker of susceptibility to early-onset Alzheimer's disease. In addition to PEN2, nicastrin and APH-1, Presenilin1 forms the gamma-secretase protein complex, a membrane-bound aspartyl protease that can cleave certain proteins at peptide bonds buried within the hydrophobic environment of the lipid bilayer. This cleavage is responsible for a key step in signaling from several cell-surface receptors and is thought to be required for the generation of the neurotoxic amyloid peptides that are central to the pathogenesis of Alzheimer's disease. Like the tumor necrosis factor-alpha-converting enzyme (TACE) and the beta-site cleavage enzyme (BACE) protease families, gamma-secretase will cleave the amyloid precursor protein (APP), but within the intramembrane region of APP, resulting in either the non-toxic p3 (from the alpha and gamma cleavage site) or the toxic Abeta amyloid peptide (from the beta and gamma cleavage site). It is thought that accumulation of the Abeta peptide is the precursor to Alzheimer's disease. Multiple isoforms of presenilin1 are known to exist. This antibody has no cross-reactivity to presenilin2.
Sherrington R, Rogaev EI, Liang Y, et al. Cloning of a gene bearing missense mutations in early-onset familial Alzheimer’s disease. Nature1995; 375:754-60.
Weihofen A and Martoglio B. Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides. Trends Cell Biol.2003; 13:71-8.
Periz G and Fortini ME. Functional reconstitution of g-secretase through coordinated expression of presenilin, nicastrin, aph-1, and pen-2. J. Neurosci. Res.2004; 77:309-22.
Selkoe DJ. The cell biology of b-amyloid precursor protein and presenilin in Alzheimer’s disease. Trends Cell Biol.1998; 8:447-53.
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