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Compound E

γ-Secretase inhibitor
ALX-270-415-C250 250 µg 159.00 USD
ALX-270-415-M001 1 mg 458.00 USD
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  • Cell-permeable, potent, and non-competitive selective inhibitor of γ-secretase and Notch pathway
  • Inducer of neuronal differentiation
  • Active in vitro and in vivo
γ-Secretase is a multimeric and transmembrane aspartyl protease constituted of four subunits: presenilin, nicastrin, Aph-1, and Pen-2. Presenilin is the catalytic subunit of γ-secretase. The carboxyl-terminal fragments (CTFs) of Amyloid precursor protein (APP) and of Notch are two well-known substrates of γ-secretase. Aberrant cleavage of these substrates by γ-secretase is associated with Alzheimer's disease and cancer, respectively. g-Secretase is, therefore, a promising drug target. Compound E is a cell permeable, potent, selective, and non-competitive inhibitor of γ-secretase. It inhibits the cleavage of both APP and Notch CTFs (IC50=0.3nM for total β-amyloid). At higher concentrations (20-400µM), It only weakly affects the activity of presenilin. Compound E was shown to impede ovarian folliculogenesis, promotes neuronal differentiation, and down-regulate thymocyte development.

Product Details

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)
Identity:Identity determined by MS and NMR.
Appearance:White to off-white powder.
Solubility:Soluble in DMSO (50 mg/ml).
Shipping:Ambient Temperature
Short Term Storage:+4°C
Long Term Storage:-20°C
Use/Stability:Stock solutions in DMSO are stable for at least 1 month when stored at -20°C.
Handling:Keep under inert gas.
Regulatory Status:RUO - Research Use Only
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Product Literature References

A hotspot mutation targeting the R-RAS2 GTPase acts as a potent oncogenic driver in a wide spectrum of tumors: I. Fernandez-Pisonero, et al.; Cell Rep. 38, 110552 (2022), Abstract;
Endothelial Notch signaling directly regulates the small GTPase RND1 to facilitate Notch suppression of endothelial migration: B. Swaminathan, et al.; Sci. Rep. 12, 1655 (2022), Abstract;
Protein aggregation and calcium dysregulation are hallmarks of familial Parkinson’s disease in midbrain dopaminergic neurons: G.S. Virdi, et al.; NPJ Parkinsons Dis. 8, 162 (2022), Abstract;
A non-toxic concentration of telomerase inhibitor BIBR1532 fails to reduce TERT expression in a feeder-free induced pluripotent stem cell model of human motor neurogenesis: V.A. Pandya, et al.; Int. J. Mol. Sci. 22, 3256 (2021), Abstract; Full Text
Cancer-associated mutations in VAV1 trigger variegated signaling outputs and T-cell lymphomagenesis: J.R. Valero, et al.; EMBO J. 40, e108125 (2021), Abstract;
Comparative structural, biophysical, and receptor binding study of true type and wild type AAV2: A. Bennett, et al.; J. Struct. Biol. 213, 107795 (2021), Abstract;
Leukemia-specific delivery of mutant NOTCH1 targeted therapy.: G. Roti, et al.; J. Exp. Med. 215, 197 (2018), Abstract; Full Text
A Paradoxical Tumor-Suppressor Role for the Rac1 Exchange Factor Vav1 in T Cell Acute Lymphoblastic Leukemia: J. Robles-Valero, et al.; Cancer Cell 32, 608 (2017), Abstract; Full Text
Mechanism of BMP9 promotes growth of osteosarcoma mediated by the Notch signaling pathway: P. Liu, et al.; Oncol. Lett. 11, 1367 (2016), Application(s): Notch Inhibition in Cell Culture, Abstract; Full Text
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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