Amyloid precursor protein (APP) is a type I transmembrane protein that has a central role in the pathogenesis of Alzheimer’s disease, as well as additional roles in brain development, neuronal plasticity, and memory.1 APP is cleaved by β-secretase (BACE) in neuronal endosomes during amyloidogenic processing of APP, generating the C-terminal C99 fragment, which is localized to the endoplasmic membrane.2,3 C99 is further cleaved by γ-secretase, liberating the APP intracellular domain (AICD) and generating amyloid-β (Aβ) peptides of various lengths, including Aβ40 (Item No. 21617) and Aβ42 (Item No. 20574), which are hallmarks of Alzheimer's disease. APP can also be cleaved by α-secretase during non-amyloidogenic processing of APP, which occurs at the neuronal plasma membrane and generates the neuroprotective soluble APP fragment sAPPα, as well as a variety of other fragments, including the C47 fragment.1,4 Transgenic mice expressing mutant forms of APP exhibit extracellular Aβ deposits in the brain, as well as cognitive dysfunction, and are widely used models of Alzheimer’s disease.5 Intraneuronal C99 levels are increased in the transgenic APPE693Q mouse model of Alzheimer’s disease, as well as postmortem frontal cortex from patients with sporadic Alzheimer's disease.3,6 Cayman's APP (C99 Fragment) (C-Term) Polyclonal Antibody can be used for ELISA and Western blot (WB) applications. The antibody recognizes the C-terminal region corresponding to the C99 fragment to detect intact APP, as well as the C47 APP fragment, at 18 kDa and 9 kDa, respectively, from human samples.WARNING This product is not for human or veterinary use.
