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Fast and quantitative analysis of epigenetic interactions using MicroScale Thermophoresis
EP24026
Poster Title: Fast and quantitative analysis of epigenetic interactions using MicroScale Thermophoresis
Submitted on 23 May 2016
Author(s): Clemens Entzian, Corinna Kuttenberger, Tobias Mauerer, Lukas Kniep, Estefanía Muciño, Dr. Thomas Schubert
Affiliations: 2bind GmbH, Am Biopark 13, 93053, Regensburg, Germany
This poster was presented at Drug Discovery Forum, Munich
Poster Views: 1,248
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Poster Information
Abstract: Epigenetic regulation is based on specific molecular interactions between epigenetic reader, writer and eraser molecules and chromatin. Binding parameters of these interactions such as binding affinities, stoichiometries and thermodynamics are essential for the understanding of the establishment and maintenance of epigenetic networks. MicroScale Thermophoresis (MST) is a rapid and precise method to characterize epigenetic interactions in solution requiring low sample concentrations. The free choice of buffers during a MST measurement allows an analysis of molecular interactions in complex buffer systems, in serum and even in crude extracts. This robust and flexible technology offers the detection of affinities in a dynamic range from pM to mM. Integrated quality controls ensure high quality data. We present the characterization of molecular interactions between epigenetic proteins and their target from nucleotides to nucleosomes. Our optimized protocols assure highly sensitive cost- and time-efficient performance.Summary: Epigenetic regulation is based on specific molecular interactions between epigenetic reader, writer and eraser molecules and chromatin. Thermophoresis (MST) is a rapid and precise method to characterize epigenetic interactions in solution requiring low sample concentrations. We present the characterization of molecular interactions between epigenetic proteins and their target from nucleotides to nucleosomes. Our optimized protocols assure highly sensitive cost- and time-efficient performance.References: 1. Rothbart SB, Strahl BD (2014) Interpreting the language of histone and DNA modifications. Biochim Biophys Acta 1839: 627-643. CrossRef
2. Baylin SB, Jones PA (2011) A decade of exploring the cancer epigenome-biological and translational implications. Nat Rev Cancer 11: 726-734. CrossRef
3. Wu H, Zhang Y (2011) Mechanisms and functions of Tet protein-mediated 5-methylcytosine oxidation. Genes Dev 25: 2436-2452. CrossRef
4. Kouzarides T (2007) Chromatin modifications and their function. Cell 128: 693-705. CrossRef
5. Tan M, Luo H, Lee S, et al. (2011) Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146: 1016-1028. CrossRef
6. Zhang G, Pradhan S (2014) Mammalian epigenetic mechanisms. IUBMB Life 66: 240-256. CrossRef
7. Baaske P, Wienken CJ, Reineck P, et al. (2010) Optical thermophoresis for quantifying the buffer dependence of aptamer binding. Angew Chem Int Ed Engl 49: 22
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