Anti-beta-Amyloid Precursor Protein (APP)

Amyloid-beta precursor protein (APP) is the source of the amyloid-beta (Ab) peptide found in neuritic plaques of Alzheimer's disease (AD) patients. APP is aglycosylated transmembrane protein with a long extracellular N-terminal domain, a short intracellular C-terminal domain, and an Abeta-segment of intermediate length shared between the intra- and extracellular regions. APP is cleaved by alpha-secretase immediately before or after reaching the cell surface, releasing the nonamyloidogenic secreted form of the N-terminal soluble APP fragment (sAPPa). APP molecules that are not cleaved by alpha-secretase are internalized, and subjected to beta-site cleavage by beta-secretase, leaving behind a membrane-bound C-terminal stub. This terminal stub is the substrate for gamma-secretase, which cleaves the molecule at gamma-site(s) to release the 40aa, 42aa, or 43aa -long Ab peptides. Applications: Suitable for use in Western Blot, Immunoprecipitation and Immunohistochemistry. Other applications have not been tested. Recommended Dilutions: Western Blot (Mouse): 1-3ug/ml. Detects a band representing the full-length protein at ~ 100kD, and a band at ~ 10-12kD representing the C99 C-terminal cleavage fragment. A major non-specific band has been observed at ~50kD in mouse brain homogenates., Immunoprecipitation (Mouse): 7ug/reaction, Immunohistochemistry (FFPE, Human): 1-2ug/ml. Digestion with trypsin prior to staining is required., Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.