Anti-APP / Amyloid beta, clone APP/9971R

1 mg/ml in 1X PBS, BSA free, sodium azide free. Proteolytic cleavage of the Amyloid protein precursor (APP) gives rise to the beta-Amyloid and Amyloid A4 proteins, which are present in human platelets. Amyloid deposition is associated with type II diabetes, Down syndrome and a variety of neurological disorders, including Alzheimer s disease. The Amyloid precursor protein (APP) undergoes alternative splicing, resulting in several isoforms. Proteolytic cleavage of APP leads to the formation of the 4 kDa Amyloid beta/A4 Amyloid protein. This protein is involved in the formation of neurofibrillary tangles and plaques that characterize the senile plaques of Alzheimer s patients. APLP1 (Amyloid precursor-like protein 1) and APLP2 are structurally similar to APP. Human APLP2 is a membrane-bound sperm protein that contains a region highly homologous to the transmembrane-cytoplasmic domains of APP found in brain plaques of Alzheimer s disease patients. Protein function: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis (PubMed:25122912). Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis- inducing pathways such as those mediated by G(o) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. By acting as a kinesin I membrane receptor, plays a role in axonal anterograde transport of cargo towards synapses in axons (PubMed:17062754, PubMed:23011729). Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons. Provides Cu(2+) ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. [The UniProt Consortium]