Catalog Number:

RA18013

Product Type:

Affinity Purified Antibody

Immunogen Sequence:

synthetic phosphopeptide (KLH coupled) corresponding to residues surrounding Thr668 of human APP695. Antibodies are purified by protein A and peptide affinity chromatography

Host:

Rabbit

Reactivity:

Human, Mouse and Rat

Applications:

Immunocytochemistry on PFA fixed cells, Immunohistochemistry on paraffin sections, Western Blot, Immunoprecipitation

Description:

Amyloid precursor protein (APP), a widely expressed cell surface protein, is cleaved in the transmembrane region by gamma-secretase. Gamma-cleavage of APP produces the extracellular amyloid beta peptide of Alzheimer disease and releases an intracellular tail fragment. The cytoplasmic tail of APP forms a multimeric complex with the nuclear adaptor protein Fe65 and the histone acetyltransferase TIP60. This complex potently stimulates transcription via heterologous Gal4 or LexA DNA binding domains, suggesting that release of the cytoplasmic tail of APP by gamma-cleavage may function in gene expression.

The phosphorylation status of amyloid precursor protein (APP) at Thr668 is suggested to play a critical role in the proteolytic cleavage of APP, which generates either soluble APP(beta) (sAPP(beta)) and beta-amyloid peptide (Abeta), the major component of senile plaques in patient brains inflicted with Alzheimer's disease (AD), or soluble APP(alpha) (sAPP(alpha)) and a peptide smaller than Abeta.

Reference:

Liu F, Su Y, Li B, Zhou Y, Ryder J, Gonzalez-DeWhitt P, May PC, Ni B. Regulation of amyloid precursor protein (APP) phosphorylation and processing by p35/Cdk5 and p25/Cdk5. FEBS Lett. 2003 Jul 17;547(1-3):193-6.