|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_056146, 23385|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||78411 Da|
|Application Notes||Nicastrin antibody can be used for detection of Nicastrin by Western blot at 0.5 - 1 μg/mL. Antibody can also be used for immunohistochemistry starting at 2.5 μg/mL. For immunofluorescence start at 20 μg/mL.|
|Other Names||Nicastrin Antibody: ATAG1874, KIAA0253, UNQ1874/PRO4317, Nicastrin, nicastrin|
|Target/Specificity||Nicastrin antibody was raised against a 18 amino acid synthetic peptide from near the center of human Nicastrin.|
The immunogen is located within amino acids 370 - 420 of Nicastrin.
|Reconstitution & Storage||Nicastrin 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||Nicastrin Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Essential 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). It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.|
|Cellular Location||Membrane; Single-pass type I membrane protein. Melanosome Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
|Tissue Location||Widely expressed.|
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Provided below are standard protocols that you may find useful for product applications.
Nicastrin Antibody: Nicastrin, in addition to presenilin, PEN2, and APH-1 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. Nicastrin is also thought to be involved in cell proliferation and signaling, especially in regards to activation of Notch receptors as loss of Nicastrin expression results in mouse embryonic lethality.
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.
Nguyen V, Hawkins C, Bergeron C, et al. Loss of nicastrin elicits an apoptotic phenotype in mouse embryos. Brain Res. 2006; 1086:76-84.
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