A number of mutations, identified in the gene encoding the β-amyloid precursor protein (βAPP), have been linked to early-onset Familial Alzheimers Disease. βAPP is cleaved sequentially by the proteolytic enzymes β-secretase and γ-secretase to produce β-amyloid (Aβ) peptides with the Aβ1-42(43) and the Aβ1-40 forms being the most prevalent. Secreted Aβ peptides can bind to scavenger receptors and the receptor for advanced glycation end products. Aβ peptides are degraded either via a reuptake mechanism followed by endosomal degradation or by an extracellular insulin-degrading enzyme. Extracellular accumulation of Aβ leads to formation of aggregates, fibrils, and eventually amyloid deposits called neuritic plaques, a hallmark of Alzheimer’s disease. β-amyloid antibodies and peptides have been developed as tools for elucidating the biology of Alzheimers disease. GenScript Human β-Amyloid 1-42 Antibody (2C2G5), mAb, Mouse is produced from the hybridoma resulting from fusion of Sp2/0 myeloma and B-lymphocytes obtained from mouse immunized with a synthetic peptide corresponding to amino acids 36-42 of human β-Amyloid conjugated to KLH (Swiss Prot: P05067).