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Dehydrolucidenic acid A, 20(21)-


  • Brand : BIOFRON

  • Catalogue Number : BD-P0104

  • Specification : 99.0%(HPLC)

  • CAS number : 852936-69-7

  • Formula : C27H36O6

  • Molecular Weight : 456.57

  • PUBCHEM ID : 122169316

  • Volume : 25mg

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4-[(7S,10S,13R,14R,17R)-7-hydroxy-4,4,10,13,14-pentamethyl-3,11,15-trioxo-1,2,5,6,7,12,16,17-octahydrocyclopenta[a]phenanthren-17-yl]pent-4-enoic acid


4-[(7S,10S,13R,14R,17R)-7-hydroxy-4,4,10,13,14-pentamethyl-3,11,15-trioxo-1,2,5,6,7,12,16,17-octahydrocyclopenta[a]phenanthren-17-yl]pent-4-enoic acid



Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.

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WGK Germany


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Personal Projective Equipment

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For Reference Standard and R&D, Not for Human Use Directly.

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provides coniferyl ferulate(CAS#:852936-69-7) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate

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Eukaryotic genomes are folded into loops. It is thought that these are formed by cohesin complexes via extrusion, either until loop expansion is arrested by CTCF or until cohesin is removed from DNA by WAPL. Although WAPL limits cohesin’s chromatin residence time to minutes, it has been reported that some loops exist for hours. How these loops can persist is unknown. We show that during G1-phase, mammalian cells contain acetylated cohesinSTAG1 which binds chromatin for hours, whereas cohesinSTAG2 binds chromatin for minutes. Our results indicate that CTCF and the acetyltransferase ESCO1 protect a subset of cohesinSTAG1 complexes from WAPL, thereby enable formation of long and presumably long-lived loops, and that ESCO1, like CTCF, contributes to boundary formation in chromatin looping. Our data are consistent with a model of nested loop extrusion, in which acetylated cohesinSTAG1 forms stable loops between CTCF sites, demarcating the boundaries of more transient cohesinSTAG2 extrusion activity.

Research organism: Human


ESCO1 and CTCF enable formation of long chromatin loops by protecting cohesinSTAG1 from WAPL


Gordana Wutz,1 Rene Ladurner,1† Brian Glenn St Hilaire,2,3,4 Roman R Stocsits,1 Kota Nagasaka,1 Benoit Pignard,1 Adrian Sanborn,2,5 Wen Tang,1 Csilla Varnai,6,7 Miroslav P Ivanov,1‡ Stefan Schoenfelder,6§ Petra van der Lelij,1 Xingfan Huang,2,8,9 Gerhard Durnberger,10# Elisabeth Roitinger,10 Karl Mechtler,1,10 Iain Finley Davidson,1 Peter Fraser,6,11 Erez Lieberman-Aiden,2,3,4,8,12,13 and Jan-Michael Peters1 Jeannie T Lee, Reviewing Editor and Kevin Struhl, Senior Editor Jeannie T Lee, Massachusetts General Hospital, United States; Contributor Information.

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Essential biological functions, such as mitosis, require tight coordination of hundreds of proteins in space and time. Localization, timing of interactions and changes in cellular structure are all crucial to ensure correct assembly, function and regulation of protein complexes1-4. Live cell imaging can reveal protein distributions and dynamics but experimental and theoretical challenges prevented its use to produce quantitative data and a model of mitosis that comprehensively integrates information and enables analysis of the dynamic interactions between the molecular parts of the mitotic machinery within changing cellular boundaries.

To address this, we generated a 4D image data-driven, canonical model of the morphological changes during mitotic progression of human cells. We used this model to integrate dynamic 3D concentration data of many fluorescently knocked-in mitotic proteins, imaged by fluorescence correlation spectroscopy-calibrated microscopy5. The approach taken here in the context of the MitoSys consortium to generate a dynamic protein atlas of human cell division is generic. It can be applied to systematically map and mine dynamic protein localization networks that drive cell division in different cell types and can be conceptually transferred to other cellular functions.


Experimental and computational framework for a dynamic protein atlas of human cell division


Yin Cai,1,3,* M. Julius Hossain,1,* Jean-Karim Heriche,1 Antonio Z. Politi,1 Nike Walther,1 Birgit Koch,1,4 Malte Wachsmuth,1,5 Bianca Nijmeijer,1 Moritz Kueblbeck,1 Marina Martinic Kavur,2,6 Rene Ladurner,2,7 Stephanie Alexander,1 Jan-Michael Peters,2 and Jan Ellenberg1

Publish date

2019 Jun 9.




Targeted cancer therapy is based on exploiting selective dependencies of tumor cells. By leveraging recent functional screening data of cancer cell lines we identify Werner syndrome helicase (WRN) as a novel specific vulnerability of microsatellite instability-high (MSI-H) cancer cells. MSI, caused by defective mismatch repair (MMR), occurs frequently in colorectal, endometrial and gastric cancers. We demonstrate that WRN inactivation selectively impairs the viability of MSI-H but not microsatellite stable (MSS) colorectal and endometrial cancer cell lines. In MSI-H cells, WRN loss results in severe genome integrity defects. ATP-binding deficient variants of WRN fail to rescue the viability phenotype of WRN-depleted MSI-H cancer cells. Reconstitution and depletion studies indicate that WRN dependence is not attributable to acute loss of MMR gene function but might arise during sustained MMR-deficiency. Our study suggests that pharmacological inhibition of WRN helicase function represents an opportunity to develop a novel targeted therapy for MSI-H cancers.

Research organism: Human


Werner syndrome helicase is a selective vulnerability of microsatellite instability-high tumor cells


Simone Lieb,#1,† Silvia Blaha-Ostermann,#1,† Elisabeth Kamper,1 Janine Rippka,1 Cornelia Schwarz,1 Katharina Ehrenhofer-Wolfer,1 Andreas Schlattl,1 Andreas Wernitznig,1 Jesse J Lipp,1 Kota Nagasaka,2 Petra van der Lelij,2 Gerd Bader,1 Minoru Koi,3 Ajay Goel,4 Ralph A Neumuller,1 Jan-Michael Peters,2 Norbert Kraut,1 Mark A Pearson,1 Mark Petronczki,1 and Simon Wohrle1 Wolf-Dietrich Heyer, Reviewing Editor and Jeffrey Settleman, Senior Editor Wolf-Dietrich Heyer, University of California, Davis, United States; Contributor Information.

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