beta-Amyloid Precursor Protein, CT (APP), Purified

Amyloid Precursor Protein (APP) is an integral membrane protein with a large ectodomain, a transmembrane domain, and a short cytoplasmic tail. APP is proteolytically cleaved by b-secretase (BACE) to generate the APP N-terminal fragment (sbAPP) with Mr100kD and a C-terminal fragment (C99) with Mr12kD. The smaller 12kD fragment can be further cleaved by g-secretase, an enzyme activity recently attributed to presenilin-2. This second cleavage produces the insoluble b-amyloid (Ab), a peptide of ~4kD. The accumulation of b-amyloid in intracellular neurofibrillary tangles and extracellular plaques is observed in the brains of Alzheimer's disease patients and Downs's Syndrome patients. In Alzheimer's disease, this protein is broken down and releases the 12 amino acid beta-amyloid protein that is found in senile plaques and vessels. The amyloid precursor protein is currently investigationed to determine how this protein is broken down abnormally in Alzheimer's disease to give rise to the beta-amyloid protein which is present in senile plaques and vessels. , Source: Synthetic, sequence 681GYENPTYKFFEQMQN695 (linear), Storage and Stability: Lyophilized powder may be stored at 4°C for short-term only. Stable for 12 months at -20°C. Reconstitute to nominal volume (see reconstitution instructions for peptides) and store at -20°C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer. . ,