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Presenilin 1 antibody (PSEN1)

Details for Product anti-PSEN1 Antibody No. ABIN1003039, Supplier: Login to see
Antigen
  • pre1
  • psen
  • zfPS1
  • zf-PS1
  • ad3
  • fad
  • ps1
  • s182
  • X-PS-beta
  • X-PS-alpha
  • AD3
  • FAD
  • PS-1
  • PS1
  • S182
  • Ad3h
Alternatives
anti-Human Presenilin 1 antibody for Enzyme Immunoassay
Reactivity
Human, Mouse (Murine), Rat (Rattus)
234
80
59
26
11
4
4
4
2
Host
Rabbit
163
43
20
4
3
2
Clonality
Polyclonal
Conjugate
This Presenilin 1 antibody is un-conjugated
8
6
6
3
3
3
3
3
3
3
3
3
3
3
3
1
1
1
Application
Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
166
100
82
39
33
23
18
10
6
5
5
2
2
1
1
Supplier
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Immunogen Presenilin1 antibody was raised in rabbits against a 23 amino acid peptide from near the carboxy terminus of human presenilin1.
Blocking Peptide Blocking peptide for this product available: ABIN1004439
Isotype IgG
Purification Affinity chromatography purified via peptide column.
Alternative Name Presenilin1 (PSEN1 Antibody Abstract)
Background 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 g-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-a-converting enzyme (TACE) and the b-site cleavage enzyme (BACE) protease families, g-secretase will cleave the amyloid precursor protein (APP), but within the intramembrane region of APP, resulting in either the non-toxic p3 (from the a and g cleavage site) or the toxic Ab amyloid peptide (from the b and g cleavage site). It is thought that accumulation of the Ab peptide is the precursor to Alzheimer’s disease. Multiple isoforms of presenilin1 are known to exist. This antibody has no cross-reactivity to presenilin2.
Pathways Notch Signaling, EGFR Signaling Pathway
Application Notes Presenilin1 antibody can be used for detection of presenilin1 by Western blot at 0.5 – 1 µg/ml. (Optimal dilution should be determined by user). Antibody can also be used for immunohistochemistry and ELISA and might be suited for other applications not tested so far.
Restrictions For Research Use only
Format Liquid
Buffer Antibody is supplied in PBS containing 0.02% sodium azide.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Handling Advice Antibody can be stored at 4ºC, stable for 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. During shipment, small volumes of antibody will occasionally become entrapped in the seal of the product vial. For products with volumes of 200 myl or less, we recommend gently tapping the vial on a hard surface or briefly centrifuging the vial in a tabletop centrifuge to dislodge any liquid in the container’s cap.
Storage 4 °C
Expiry Date 12 months
Product cited in: Periz, Fortini: "Functional reconstitution of gamma-secretase through coordinated expression of presenilin, nicastrin, Aph-1, and Pen-2." in: Journal of neuroscience research, Vol. 77, Issue 3, pp. 309-22, 2004 (PubMed).

Weihofen, Martoglio: "Intramembrane-cleaving proteases: controlled liberation of proteins and bioactive peptides." in: Trends in cell biology, Vol. 13, Issue 2, pp. 71-8, 2003 (PubMed).

Selkoe: "The cell biology of beta-amyloid precursor protein and presenilin in Alzheimer's disease." in: Trends in cell biology, Vol. 8, Issue 11, pp. 447-53, 1999 (PubMed).

Background publications Sherrington, Rogaev, Liang et al.: "Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. ..." in: Nature, Vol. 375, Issue 6534, pp. 754-60, 1995 (PubMed).