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Membrane protein digestion - comparison of LPI HexaLane with traditional techniques.
Astra Zeneca.
Nanoxis AB.
Department of Chemistry, University of Gothenburg.
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2011 (English)In: Gel-free proteomics: Methods and Protocols / [ed] Kris Gevaert (ID1); Joël Vandekerckhove (ID2), Germany: Humana Press, 2011, 129-142 p.Chapter in book (Other academic)
Abstract [en]

Membrane protein profiling and characterization is of immense importance for the understanding of vital processes taking place across cellular membranes. Traditional techniques used for soluble proteins, such as 2D gel electrophoresis, are sometimes not entirely applicable to membrane protein targets, due to their low abundance and hydrophobic character. New tools have been developed that will accelerate research on membrane protein targets. Lipid-based protein immobilization (LPI) is the core technology in a new approach that enables immobilization and digestion of native membrane proteins inside a flow cell format. The presented method is described in the context of comparing the method to traditional approaches where the sample amount that is digested and analyzed is the same.

Place, publisher, year, edition, pages
Germany: Humana Press, 2011. 129-142 p.
, Methods in Molecular Biology, ISSN 1064-3745 ; 753
Keyword [en]
Membrane protein, immobilization, LPI, profiling, in-gel, in-solution, sequential digestion
National Category
Other Medical Sciences not elsewhere specified
Research subject
Analytical Chemistry
URN: urn:nbn:se:uu:diva-195912DOI: 10.1007/978-1-61779-148-2_9ISBN: 978-1-61779-148-2OAI: oai:DiVA.org:uu-195912DiVA: diva2:608683
Available from: 2013-02-28 Created: 2013-02-28 Last updated: 2013-03-26

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Sui, Ping
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