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Accumulation of neurotoxic amyloid-beta is a major hallmark of Alzheimer disease (AD\\\\; MIM 104300). Additionally we are shipping Pigeon Homolog (Drosophila) Antibodies (18) and Pigeon Homolog (Drosophila) Proteins (6) and many more products for this protein.
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GSAP cleavage via caspase-3 (show CASP3 ELISA Kits) is regulated and depend upon the availability of 5-Lipoxygenase (show ALOX5 ELISA Kits) in Alzheimer's disease.
gamma-secretase activating protein (GSAP) and imatinib have roles in the regulation of gamma-secretase activity and amyloid-beta generation
Protocols for recombinant bacterial expression and purification of potentially important protein GSAP are not successful in generating soluble forms of GSAP that contain well-ordered and homogeneous tertiary structure.
Aberrant regulation of gamma-secretase activating protein expression plays a key role in acceleration of gamma-cleavage of beta-secretase-cleaved C-terminal fragment of amyloid precursor protein (show APP ELISA Kits) and accumulation of Abeta (show APP ELISA Kits) in AD brains
A gamma-secretase activating protein (GSAP) that selectively increases amyloid-beta production via interactions with both gamma-secretase and its substrate, the amyloid precursor protein carboxy-terminal fragment.
Study reports discovery of a novel gamma-secretase activating protein (GSAP) that selectively increases amyloid-beta production through interactions with gamma-secretase and its substrate, the amyloid precursor protein (show APP ELISA Kits) carboxy-terminal fragment.
Accumulation of neurotoxic amyloid-beta is a major hallmark of Alzheimer disease (AD\; MIM 104300). Formation of amyloid-beta is catalyzed by gamma-secretase (see PSEN1\; MIM 104311), a protease with numerous substrates. PION, or GSAP, selectively increases amyloid-beta production through a mechanism involving its interaction with both gamma-secretase and its substrate, the amyloid-beta precursor protein (APP\; MIM 104760) C-terminal fragment (APP-CTF) (He et al., 2010
, pigeon homolog
, protein pigeon homolog