Anti-Amyloid Fibrils (OC)

Anti-Amyloid Fibrils (OC) Antibody was purified by Protein A chromatography. A BLAST analysis was used to suggest cross-reactivity with Amyloid Fibrils (OC) from Human based on 100% homology with the immunizing sequence. Expected to detect in mouse and rat based on species homology. Recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrilllar oligomers or natively folded proteins. Cross-reactivity with Amyloid Fibrils (OC) from other sources has not been determined. Neuroscience research. 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]