Anti-Abeta40

Abeta derives from APP via proteolytic cleavage by proteases called alpha-, beta- and gamma-secretase. The alpha-secretase cleavage precludes the formation of Abeta, while the beta- and gamma-cleavages generate APP components with amyloidogenic features. Amyloid beta A4 precursor protein(APP), encoded by APP gene which locate on human chromosome 21q, is a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. APP expressed in all fetal tissues and is pronounced in brain, kidney, heart and spleen, but weak in liver. Defects in APP are the cause of Alzheimer disease type 1 (AD1). This antibody can recogniaze the N-terminus of human APP: Soluble APP-alpha and Soluble APP-beta. 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. 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. 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]