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ML115 Sale

(Synonyms: CID 6619100, SID 14735210) 目录号 : GC44213

A cell-permeable STAT3 activator

ML115 Chemical Structure

Cas No.:912798-42-6

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5mg
¥2,610.00
现货
10mg
¥4,140.00
现货

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Sample solution is provided at 25 µL, 10mM.

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产品描述

Signal transducer and activator of transcription 3 (STAT3) is a cytokine-inducible transcription factor with roles in inflammation and cancer. ML115 is an isoxazole carboxamide that acts as a cell-permeable STAT3 activator (EC50 = 2 nM) and is more than 28,000-fold selective for STAT3 over STAT1 and NF-κB. It shows no cytotoxicity against HT-1080 or NIH-3T3 cells. ML115 increases the expression of BCL3, a known STAT3-dependent oncogene, and enhances STAT3 activation by the pro-inflammatory cytokine IL-6. As the maintenance of pluripotency in mouse embryonic stem cells requires continued activation of STAT3, ML115 may be useful in maintaining embryonic stem cells in an undifferentiated state.

Chemical Properties

Cas No. 912798-42-6 SDF
别名 CID 6619100, SID 14735210
Canonical SMILES COC1=CC(NC(C2=NOC(C3CC3)=C2)=O)=C(OC)C=C1Cl
分子式 C15H15ClN2O4 分子量 322.7
溶解度 DMF: 25 mg/ml,DMSO: 16 mg/ml,Ethanol: 0.1 mg/ml 储存条件 Store at -20°C
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1 mg 5 mg 10 mg
1 mM 3.0989 mL 15.4943 mL 30.9885 mL
5 mM 0.6198 mL 3.0989 mL 6.1977 mL
10 mM 0.3099 mL 1.5494 mL 3.0989 mL
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Research Update

Effect of acetate formation pathway and long chain fatty acid CoA-ligase on the free fatty acid production in E. coli expressing acy-ACP thioesterase from Ricinus communis

Metab Eng 2012 Jul;14(4):380-7.PMID:22480945DOI:10.1016/j.ymben.2012.03.007.

Microbial biosynthesis of fatty acid like chemicals from renewable carbon sources has attracted significant attention in recent years. Free fatty acids can be used as precursors for the production of fuels or chemicals. Wild type E. coli strains produce fatty acids mainly for the biosynthesis of lipids and cell membranes and do not accumulate free fatty acids as intermediates in lipid biosynthesis. However, free fatty acids can be produced by breaking the fatty acid elongation through the overexpression of an acyl-ACP thioesterase. Since acetyl-CoA might be an important factor for fatty acid synthesis (acetate formation pathways are the main competitive pathways in consuming acetyl-CoA or pyruvate, a precursor of acetyl-CoA), and the long chain fatty acid CoA-ligase (FadD) plays a pivotal role in the transport and activation of exogenous fatty acids prior to their subsequent degradation, we examined the composition and the secretion of the free fatty acids in four different strains including the wild type MG1655, a mutant strain with inactivation of the fatty acid beta-oxidation pathway (fadD mutant (ML103)), and mutant strains with inactivation of the two major acetate production pathways (an ack-pta (acetate kinase/phosphotransacetylase), poxB (pyruvate oxidase) double mutant (ML112)) and a fadD, ack-pta, poxB triple mutant (ML115). The engineered E. coli cells expressing acyl-ACP thioesterase with glucose yield is higher than 40% of theoretical yield. Compared to MG1655(pXZ18) and ML103(pXZ18), acetate forming pathway deletion strains such as ML112(pXZ18) and ML115(pXZ18) produced similar quantity of total free fatty acids, which indicated that acetyl-CoA availability does not appear to be limiting factor for fatty acid production in these strains. However, these strains did show significant differences in the composition of free fatty acids. Different from MG1655(pXZ18) and ML103(pXZ18), acetate formation pathway deletion strains such as ML112(pXZ18) and ML115(pXZ18) produced similar level of C14, C16:1 and C16 free fatty acids, and the free fatty acid compositions of both strains did not change significantly with time. In addition, the strains bearing the fadD mutation showed significant differences in the quantities of free fatty acids found in the broth. Finally, we examined two potential screening methods for selecting and isolating high free fatty acids producing cells.