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Purification of Plant Receptor Kinases from Plant Plasma Membranes.
- Source :
-
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2017; Vol. 1621, pp. 47-56. - Publication Year :
- 2017
-
Abstract
- Receptor kinases play a central role in various biological processes, but due to their low abundance and highly hydrophobic and dynamic nature, only a few of them have been functionally characterized, and their partners and ligands remain unidentified. Receptor protein extraction and purification from plant tissues is one of the most challenging steps for the success of various biochemical analyses to characterize their function. Immunoprecipitation is a widely used and selective method for enriching or purifying a specific protein. Here we describe two different optimized protein purification protocols, batch and on-chip immunoprecipitation, which efficiently isolate plant membrane receptor kinases for functional analysis.
- Subjects :
- Agrobacterium genetics
Agrobacterium metabolism
Arabidopsis enzymology
Arabidopsis genetics
Arabidopsis Proteins biosynthesis
Arabidopsis Proteins genetics
Biosensing Techniques instrumentation
Biosensing Techniques methods
Cell Membrane enzymology
Chromatography, Affinity instrumentation
Gene Expression
Immunoprecipitation methods
Ligands
Microsomes chemistry
Plant Leaves enzymology
Plant Leaves genetics
Protein Array Analysis instrumentation
Protein Array Analysis methods
Protein Serine-Threonine Kinases biosynthesis
Protein Serine-Threonine Kinases genetics
Receptors, Cell Surface biosynthesis
Receptors, Cell Surface genetics
Nicotiana enzymology
Nicotiana genetics
Arabidopsis chemistry
Arabidopsis Proteins isolation & purification
Cell Membrane chemistry
Chromatography, Affinity methods
Protein Serine-Threonine Kinases isolation & purification
Receptors, Cell Surface isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 1940-6029
- Volume :
- 1621
- Database :
- MEDLINE
- Journal :
- Methods in molecular biology (Clifton, N.J.)
- Publication Type :
- Academic Journal
- Accession number :
- 28567642
- Full Text :
- https://doi.org/10.1007/978-1-4939-7063-6_5