DAPT

DAPT (208255-80-5) is an inhibitor of γ-secretase (IC50 in human primary neurons = 115 nM for total Aβ or 200 nM for Aβ42 specifically).1?Oral administration of DAPT has been shown to reduce levels of Aβ in brain extract, cerebrospinal fluid and plasma from mice and rats.2,3?DAPT blocks Notch signaling which promotes neuronal differentiation of precursor cells.4?Enhances iPS cells without oncogenes KLF4 and CMYC5. Cell permeable.

A potent and specific inhibitor of γ-secretase.

DAPT is used in the study of β-amyloid formation. DAPT has been shown to inhibit Notch signaling in studies of autoimmune and lymphoproliferative diseases, such as ALPS and lupus erythematosus, as well as in cancer cell growth, angiogenesis, and differentiation of human induced pluripotent stem cells.

DAPT (GSI-IX) is a novel γ-secretase inhibitor, which inhibits Aβ production with IC50 of 20 nM in HEK 293 cells

ChEBI: DAPT is a dipeptide consisting of alanylphenylglycine derivatised as a 3,5-difluorophenylacetamide at the amino terminal and a tert-butyl ester at the carboxy terminal. A gamma-secretase inhibitor. It has a role as an EC 3.4.23.46 (memapsin 2) inhibitor. It is a dipeptide, a difluorobenzene, a carboxylic ester and a tert-butyl ester.

Inhibitor of γ -secretase; causes a reduction in A β 40 and A β 42 levels in human primary neuronal cultures (IC 50 values are 115 and 200 nM for total A β and A β 42 respectively) and in brain extract, cerebrospinal fluid and plasma in vivo . Does not effect APP α and APP β levels. Blocks Notch signaling in hybrid human-mouse foetal thymus organ culture (FTOC). Activity causes neural cells to commit to neuronal differentiation.

DAPT is a γ-secretase inhibitor and indirectly an inhibitor of Notch, a γ-secretase substrate. Other γ-secretase substrates include LDL receptor-related protein, E-cadherin and ErbB-4. As an inhibitor of γ-secretase, DAPT may be useful in the study of β-amyloid (Aβ) formation. DAPT has been shown to inhibit Notch signaling in studies of autoimmune and lymphoproliferative diseases, such as ALPS and lupus erythematosus (SLE), as well as in cancer cell growth, angiogenesis, and differentiation of human induced pluripotent stem cells (hIPSC).

+4°C

[1] H. F. DOVEY. Functional gamma-secretase inhibitors reduce beta-amyloid peptide levels in brain[J]. Journal of Neurochemistry, 2009, 76 1: 173-181. DOI:10.1046/j.1471-4159.2001.00012.x
[2] Effects of γ-secretase inhibition on the amyloid β isoform pattern in a mouse model of Alzheimer’s disease
[3] MOHAMMED EL MOUEDDEN. Reduction of Abeta levels in the Sprague Dawley rat after oral administration of the functional gamma-secretase inhibitor, DAPT: a novel non-transgenic model for Abeta production inhibitors.[J]. Current pharmaceutical design, 2006, 12 6: 671-676. DOI:10.2174/138161206775474233
[4] MAGDA DE SMEDT. Different thresholds of Notch signaling bias human precursor cells toward B-, NK-, monocytic/dendritic-, or T-cell lineage in thymus microenvironment.[J]. Blood, 2005, 106 10: 3498-3506. DOI:10.1182/blood-2005-02-0496
[5] JUSTIN K ICHIDA. Notch inhibition allows oncogene-independent generation of iPS cells[J]. Nature chemical biology, 2014, 10 8: 632-639. DOI:10.1038/nchembio.1552