Background:  The Presenilin 1 (PS1) and Presenilin 2 (PS2) transmembrane proteins are components of high molecular weight complexes. These complexes mediate proteolytic cleavage within the transmembrane domain of several proteins, including the β-Amyloid precursor protein (βAPP) and Notch. Missense mutations in the genes encoding the Presenilin proteins increase the proteolysis of βAPP and results in the overproduction of the neurotoxic β-Amyloid peptide, which results in a condition associated with Familial Alzheimer’s disease (FAD). A novel component of the presenilin complex, nicastrin, is a type I transmembrane glycoprotein that is involved in mediating Notch/GLP-1 signaling. In addition, nicastrin contributes to the processing of βAPP, which makes nicastrin an attractive potential target for modulating the production of β-Amyloid in patients with Alzheimer’s disease. Originally purified from immunoprecipitated PS1 complexes from HEK293 cells, nicastrin contains hydrophilic amino and carboxy-terminal domains, a short, hydrophobic transmembrane domain and potential N-myristoylation and phosphorylation sites.

Description: Rabbit polyclonal to Nicastrin

Immunogen: KLH conjugated synthetic peptide derived from Nicastrin

Specificity:  ·Reacts with Human, Mouse and Rat.

·Isotype: IgG

Application:  ·Western blotting: 1/100-500. Predicted Mol wt: 78 kDa;

·Immunohistochemistry (Paraffin/frozen tissue section): 1/50-200;

·Immunocytochemistry/Immunofluorescence: 1/100;

·Immunoprecipitation: 1/50;

·ELISA: 1/500;

·Optimal working dilutions must be determined by the end user.