Purification of PP2A Holoenzymes by Sequential Immunoprecipitation with Anti-Peptide Antibodies View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2006-11-15

AUTHORS

Moorhead Greg , Gernot Walter , Jin Zhou , Ralf Ruediger

ABSTRACT

Understanding the multiple functions of protein phosphatase 2A (PP2A) rests on elucidating the enzymatic properties of over 50 different possible forms of the PP2A holoenzyme. We describe a procedure for highly purifying each one of these forms. This procedure is based on coexpressing in 293 cells one scaffolding A subunit, one regulatory B subunit, and one catalytic C subunit, each tagged with a different sequence, and purifying the trimeric holoenzyme by three consecutive immunoprecipitations with antibodies against the tags. In a few hours and from a small number of cells, sufficient enzyme can be purified for enzymatic studies. Purification of six different holoenzymes in parallel can easily be accomplished. More... »

PAGES

113-126

Book

TITLE

Protein Phosphatase Protocols

ISBN

1-59745-267-X

Identifiers

URI

http://scigraph.springernature.com/pub.10.1385/1-59745-267-x:113

DOI

http://dx.doi.org/10.1385/1-59745-267-x:113

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025782921


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