Ex 26

• Supplier: Tocris Bioscience
• Catalog: 0845
• Prices: $159.00, $669.00
• Sizes: 10 mg, 50 mg
• Function Type: Antagonist
• Cas Number: 1233332-37-0
• Chemical Name: 1-[[[5'-[[1-(4-Chloro-3-methylphenyl)ethyl]amino]-2'-fluoro-3,5-dimethyl[1,1'-biphenyl]-4-yl]carbonyl]amino]-cyclopropanecarboxylicacid
• Formula: C28H28ClFN2O3
• Molecular Weight: 494.98
• Purity: >98 %
• Description: Potent and selective S1P 1 receptor antagonist (IC 50 = 0.93 nM). Exhibits > 3,000-fold selectivity for S1P 1 over S1P 2 , S1P 3 , S1P 4 and S1P 5 . Induces lymphocyte sequestration in peripheral lymph nodes and upregulates S1P 1 receptor expression. Reduces disease severity in mice with EAE. Increases IFN- α production in stimulated dendritic cells in vivo .

Product References

Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1. - Discovery of indoles as potent and selective inhibitors of the deacetylase SIRT1.

Napper AD, Hixon J, McDonagh T, Keavey K, Pons JF, Barker J, Yau WT, Amouzegh P, Flegg A, Hamelin E, Thomas RJ, Kates M, Jones S, Navia MA, Saunders JO, DiStefano PS, Curtis R. J Med Chem. 2005 Dec 15;48(25):8045-54.

Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not - Inhibition of SIRT1 catalytic activity increases p53 acetylation but does not

Solomon JM, Pasupuleti R, Xu L, McDonagh T, Curtis R, DiStefano PS, Huber LJ. Mol Cell Biol. 2006 Jan;26(1):28-38.

The 2.5 A crystal structure of the SIRT1 catalytic domain bound to nicotinamide - The 2.5 A crystal structure of the SIRT1 catalytic domain bound to nicotinamide

Zhao X, Allison D, Condon B, Zhang F, Gheyi T, Zhang A, Ashok S, Russell M, MacEwan I, Qian Y, Jamison JA, Luz JG. J Med Chem. 2013 Feb 14;56(3):963-9.