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Compound E

γ-Secretase inhibitor
ALX-270-415-C250 250 µg 118.00 USD
ALX-270-415-M001 1 mg 336.00 USD
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Cell permeable, potent, selective, non-transition state and non-competitive inhibitor of γ-secretase (IC50=0.3nM for total β-amyloid) and Notch processing, which ceases cell differentiation. At higher concentrations (20-400µM), only weakly affects the presenilase activity. Activity tested!

Product Specification

Alternative Name:(2S)-2-{[(3,5-Difluorophenyl)acetyl]amino}-N-[(3S)-1-methyl-2-oxo-5-phenyl-2,3-dihydro-1H-1,4-benzodiazepin-3-yl]propanamide, γ-Secretase Inhibitor, GSI
Purity:≥95% (HPLC)
Appearance:White to off-white powder.
Solubility:Soluble in DMSO.
Short Term Storage:+4°C
Long Term Storage:-20°C
Handling:Keep under inert gas.
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Product Literature References

Necrosis- and apoptosis-related Met cleavages have divergent functional consequences: R. Montagne, et al.; Cell Death Dis. 6, e1769 (2015), Application(s): Cell Culture, Abstract; Full Text
Gene deletion screen for cardiomyopathy in adult Drosophila identifies a new notch ligand: I.M. Kim, et al.; Circ. Res. 106, 1233 (2010), Abstract;
Down-regulation of the met receptor tyrosine kinase by presenilin-dependent regulated intramembrane proteolysis: B. Foveau, et al.; Mol. Biol. Cell 20, 2495 (2009), Abstract;
Synaptic activity prompts gamma-secretase-mediated cleavage of EphA4 and dendritic spine formation: E. Inoue, et al.; J. Cell. Biol. 185, 551 (2009), Abstract;
Determination of guinea-pig cortical gamma-secretase activity ex vivo following the systemic administration of a gamma-secretase inhibitor: S. Grimwood, et al.; Neuropharmacology 48, 1002 (2005), Abstract;
Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia: A.P. Weng, et al.; Science 306, 269 (2004), Abstract;
Identification of a new presenilin-dependent zeta-cleavage site within the transmembrane domain of amyloid precursor protein: G. Zhao, et al.; J. Biol. Chem. 279, 50647 (2004), Abstract; Full Text
Linking receptor-mediated endocytosis and cell signaling: evidence for regulated intramembrane proteolysis of megalin in proximal tubule: Z. Zou, et al.; J. Biol. Chem. 279, 34302 (2004), Abstract; Full Text
Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria: C.A. Hansson, et al.; J. Biol. Chem. 279, 51654 (2004), Abstract; Full Text
Presenilin-dependent gamma-secretase activity mediates the intramembranous cleavage of CD44: D. Murakami, et al.; Oncogene 22, 1511 (2003), Abstract;
Regulated intramembrane proteolysis of the p75 neurotrophin receptor modulates its association with the TrkA receptor: K.M. Jung, et al.; J. Biol. Chem. 278, 42161 (2003), Abstract; Full Text
aph-1 and pen-2 are required for Notch pathway signaling, gamma-secretase cleavage of betaAPP, and presenilin protein accumulation: R. Francis, et al.; Dev. Cell 3, 85 (2002), Abstract;
Linear non-competitive inhibition of solubilized human gamma-secretase by pepstatin A methylester, L685458, sulfonamides, and benzodiazepines: G. Tian, et al.; J. Biol. Chem. 277, 31499 (2002), Abstract; Full Text
Presenilin-dependent gamma-secretase-like intramembrane cleavage of ErbB4: H.J. Lee, et al.; J. Biol. Chem. 277, 6318 (2002), Abstract; Full Text
gamma -Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase: C.Y. Ni, et al.; Science 294, 2179 (2001), Abstract;
Pharmacological knock-down of the presenilin 1 heterodimer by a novel gamma -secretase inhibitor: implications for presenilin biology: D. Beher, et al.; J. Biol. Chem. 276, 45394 (2001), Abstract; Full Text
Presenilin-dependent gamma-secretase activity modulates thymocyte development: P. Doerfler, et al.; PNAS 98, 9312 (2001), Abstract; Full Text
Presenilin-1 and -2 are molecular targets for gamma-secretase inhibitors: D. Seiffert, et al.; J. Biol. Chem. 275, 34086 (2000), Abstract; Full Text

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