Anti-Nicastrin NCSTN 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-a-converting enzyme (TACE) and the b-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.

Nicastrin antibody was raised against a 17 amino acid synthetic peptide from near the carboxy terminus of human Nicastrin. The immunogen is located within amino acids 630 - 680 of Nicastrin.

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 (amyloid-beta precursor protein) (PubMed:10993067, PubMed:12679784, PubMed:25043039, PubMed:26280335) . The gamma- secretase complex 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.

Nicastrin antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.