GLPBio

Gamma Secretase

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Gamma secretase (γ-secretase), a member of the intramembrane cleaving protease (i-CLiP) family, is a promiscuous di-aspartyl protease that catalyzes the regulated intramembrane proteolysis (RIP), in which substrate proteins are cleaved within their membrane-spanning domain. A functional γ-secretase is a multi-protein complex consisting of the catalytic component, presenilin (PSEN), and three protein cofactors, including nicastrin (NCT), anterior-pharynx defective-1 (APH1) and PSEN enhancer-2 (PEN2). So far, 90 substrates of γ-secretase have been identified, which are type-I transmembrane proteins, except for glutamate receptor GluR3, polycystin-1 and glucosaminyltransferase (GnT-V), and appear to function as signaling proteins regulating a wide variety of cellular events, such as Notch signaling pathway.

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  • GC12659 structure
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  • GC12942 structure
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  • GC13099 structure
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  • GC13673 structure
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  • GC15645 structure
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  • GC15896 structure
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    potent gamma-Secretase inhibitor

  • GC15899 structure
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  • GC16197 structure
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  • GC16431 structure
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  • GC17671 structure
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  • GC17791 structure
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  • GC19290 structure
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    PF-3084014 (PF-3084014) is a reversible, orally bioavailable, noncompetitive, and selective γ-secretase inhibitor with an IC50 of 6.2 nM. Inhibition of Notch signaling by PF-3084014 while minimizing gastrointestinal toxicity presents a promising approach for research of Notch receptor-dependent cancers.

  • GC30427 structure
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    ELN 318463 racemate is the racemate of ELN318463.

  • GC30887 structure
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  • GC30954 structure
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  • GC31012 structure
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    Purity: >98%

    BMS 433796 is a γ-secretase inhibitor with Aβ lowering activity in a transgenic mouse model of Alzheimer's disease.