Show simple item record

dc.contributor.authorReusch, Sebastian  Concept link
dc.contributor.authorBiswas, Abin  Concept link
dc.contributor.authorHirst, William G.  Concept link
dc.contributor.authorReber, Simone  Concept link
dc.date.accessioned2021-03-16T20:55:01Z
dc.date.available2021-03-16T20:55:01Z
dc.date.issued2020-12-18
dc.identifier.citationReusch, S., Biswas, A., Hirst, W. G., & Reber, S. (2020). Affinity purification of label-free tubulins from xenopus egg extracts. STAR Protocols, 1(3), 100151.en_US
dc.identifier.urihttps://hdl.handle.net/1912/26818
dc.description© The Author(s), 2020. This article is distributed under the terms of the Creative Commons Attribution License. The definitive version was published in Reusch, S., Biswas, A., Hirst, W. G., & Reber, S. Affinity purification of label-free tubulins from xenopus egg extracts. STAR Protocols, 1(3), (2020): 100151, doi:10.1016/j.xpro.2020.100151.en_US
dc.description.abstractCytoplasmic extracts from unfertilized Xenopus eggs have made important contributions to our understanding of microtubule dynamics, spindle assembly, and scaling. Until recently, these in vitro studies relied on the use of heterologous tubulin. This protocol allows for the purification of physiologically relevant Xenopus tubulins in milligram yield, which are a complex mixture of isoforms with various post-translational modifications. The protocol is applicable to any cell or tissue of interest. For complete details on the use and execution of this protocol, please refer to Hirst et al. (2020).en_US
dc.description.sponsorshipThis article was prompted by our stay at the Marine Biological Laboratory (MBL), Woods Hole, MA, in the summer of 2016 funded by the Princeton-Humboldt Strategic Partnership Grant together with the lab of Sabine Petry (Princeton University). We are grateful to the National Xenopus Resource (NXR) for supplying frogs. For mass spectrometry, we would like to acknowledge the assistance of Benno Kuropka and Chris Weise from the Core Facility BioSupraMol supported by the Deutsche Forschungsgemeinschaft (DFG). We thank the Protein Expression Purification and Characterization (PEPC) facility at the MPI-CBG; in particular, we thank Aliona Bogdanova and Barbara Borgonovo. We thank all former and current members of the Reber lab for discussions and helpful advice, in particular Christoph Hentschel and Soma Zsoter for technical assistance. S.R. acknowledges funding from the IRI Life Sciences (Humboldt-Universität zu Berlin, Excellence Initiative/DFG). W.H. was supported by the Alliance Berlin Canberra co-funded by a grant from the Deutsche Forschungsgemeinschaft (DFG) for the International Research Training Group (IRTG) 2290 and the Australian National University.en_US
dc.publisherCell Pressen_US
dc.relation.urihttps://doi.org/10.1016/j.xpro.2020.100151
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.titleAffinity purification of label-free tubulins from xenopus egg extractsen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/j.xpro.2020.100151


Files in this item

Thumbnail
Thumbnail

This item appears in the following Collection(s)

Show simple item record

Attribution-NonCommercial-NoDerivatives 4.0 International
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivatives 4.0 International