Anti-Beta Amyloid 9

Anti-Beta Amyloid 9 was affinity purified from monospecific antiserum by immunoaffinity chromatography. A BLAST analysis was used to suggest no cross-reactivity with other species based on 100% sequence homology. Cross-reactivity with Beta Amyloid 9 from other sources has not been determined. Beta Amyloid 9 functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. It is expressed in all fetal tissues with the highest levels located in the brain, kidney, heart and spleen tissue. It is involved in cell mobility, transcription regulation via protein-protein interactions and copper homeostasis/oxidative stress through copper ion reduction. The copper-metallated APP induces neuronal death directly in vitro, or is potentiated through Cu2+ mediated low-density lipoprotein oxidation. It has binding capabilities via its C-terminus for transient metals such as copper, zinc and iron. It binds APBB1-KAT5 to promote transcription activation and inhibits Notch signaling through interaction with Numb. It also promotes tau aggregation and TPK II-mediated phosphorylation. Anti-Beta Amyloid regulates neurite outgrowth by binding components in the cellular matrix such as heparin, collagen I and amyloid-beta peptide, leading to mitochondrial dysfunction in cultured cortical neurons. Defects in APP cause Alzheimer disease type 1 and cerebral amyloid angiopathy. This antibody is ideal for researchers interested in Cancer or Neuroscience research.