Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. The beta-amyloid protein precursor (APP) is cleaved by one of two beta-secretases (BACE and BACE2), producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the Alzheimer's disease patient's brains. Recently, Death Receptor 6 (DR6) was found to interact with an amino-terminal fragment of the beta-amyloid protein (N-APP) in neurons, activating a caspase 6-dependent apoptotic event leading to axonal degeneration and pruning during development, suggesting that these two proteins are involved in neural development and may possibly play a role in Alzheimer's disease.
- Recommended Dilutions: ELISA: 1:20,000; Immunohistochemsitry: 2 μg/mL; Immunofluorescence Microscopy: 20 μg/mL; Western Blot: 2 μg/mL; contains 0.02% (w/v) Sodium Azide
Type: Primary
Antigen: APP
Clonality: Polyclonal
Clone:
Conjugation: Unconjugated
Epitope: C-Terminal
Host: Rabbit
Isotype:
Reactivity: Human, Mouse, Rat