The beta-amyloid peptide (beta A4), proteolytically released from the amyloid precursor protein (APP), provides the principal component of senile plaques in Alzheimer's disease. Cleavage of APP by alpha-secretase or alternatively by beta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, respectively, and the retention of corresponding membrane-anchored C-terminal fragments, C83 and C99. Subsequent processing of C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is nonamyloidogenic. Alternatively, presenilin/ nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59).
- For ELISA, Flow Cytometry, Immunocytochemistry, Western Blot
Recognizes human amyloid beta A4 (CT, 40/42). Cross-reacts with APP. Detects a band of ~4kDa by Western blot.
Reconstitute with 1ml water (15 minutes at room temperature).
Type: Primary
Antigen: APP
Clonality: Monoclonal
Clone:
Conjugation:
Epitope:
Host: Mouse
Isotype: IgG1
Reactivity: Human