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Title:
Lipid-Binding Analysis Using a Fat Blot Assay | SpringerLink
Description:
Protein–lipid interactions play an important role in lipid metabolism, membrane trafficking and cell signaling by regulating protein localization, activation, and function. The Fat Blot assay is a relatively simple and inexpensive method to examine these...
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Schema {🗺️}

ScholarlyArticle:
      headline:Lipid-Binding Analysis Using a Fat Blot Assay
      pageEnd:259
      pageStart:253
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-62703-401-2.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Plant Lipid Signaling Protocols
         isbn:
            978-1-62703-401-2
            978-1-62703-400-5
         type:Book
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Teun Munnik
            affiliation:
                  name:University of Amsterdam
                  address:
                     name:Swammerdam Institute for Life Sciences, Section Plant Physiology, University of Amsterdam, Amsterdam, The Netherlands
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Magdalena Wierzchowiecka
            affiliation:
                  name:Adam Mickiewicz University
                  address:
                     name:Department of Molecular and Cellular Biology, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Polyphosphoinositides, Phosphatidic acid, Diacylglycerol, Inositol lipids, Lipid binding, Lipid targets, Lipid-binding domains, Lipid binding overlay, Protein–lipid interactions, FYVE, FAPP1, PLCδ1, Pleckstrin homology domain
      description:Protein–lipid interactions play an important role in lipid metabolism, membrane trafficking and cell signaling by regulating protein localization, activation, and function. The Fat Blot assay is a relatively simple and inexpensive method to examine these interactions using nitrocellulose membrane-immobilized lipids. The assay is adapted from the method by Dowler et al. (Sci STKE 129:pl6, 2002) and provides qualitative and quantitative information on the relative affinity with which a protein binds to a particular lipid. To perform a Fat Blot assay, serial dilutions of different phospholipids are spotted onto a nitrocellulose membrane. These membranes are then incubated with a lipid-binding protein possessing a GST (or other epitope) tag. The membranes are washed and the protein, which is bound to the membrane by virtue of its interaction with the lipid’s head group, is detected by immunoblotting with an antibody against GST (or other epitope). The procedure only requires a few micrograms of protein and is quick, simple and cheap to perform.
      datePublished:2013
      isAccessibleForFree:
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      context:https://schema.org
Book:
      name:Plant Lipid Signaling Protocols
      isbn:
         978-1-62703-401-2
         978-1-62703-400-5
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Amsterdam
      address:
         name:Swammerdam Institute for Life Sciences, Section Plant Physiology, University of Amsterdam, Amsterdam, The Netherlands
         type:PostalAddress
      name:Adam Mickiewicz University
      address:
         name:Department of Molecular and Cellular Biology, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Teun Munnik
      affiliation:
            name:University of Amsterdam
            address:
               name:Swammerdam Institute for Life Sciences, Section Plant Physiology, University of Amsterdam, Amsterdam, The Netherlands
               type:PostalAddress
            type:Organization
      name:Magdalena Wierzchowiecka
      affiliation:
            name:Adam Mickiewicz University
            address:
               name:Department of Molecular and Cellular Biology, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Swammerdam Institute for Life Sciences, Section Plant Physiology, University of Amsterdam, Amsterdam, The Netherlands
      name:Department of Molecular and Cellular Biology, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Poznan, Poland
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      isAccessibleForFree:
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