Chapter title |
VEGF Signaling
|
---|---|
Chapter number | 9 |
Book title |
VEGF Signaling
|
Published in |
Methods in molecular biology, January 2015
|
DOI | 10.1007/978-1-4939-2917-7_9 |
Pubmed ID | |
Book ISBNs |
978-1-4939-2916-0, 978-1-4939-2917-7
|
Authors |
Nithianandarajah-Jones, Gopika N, Cross, Michael J, Nithianandarajah-Jones, Gopika N., Cross, Michael J., Gopika N. Nithianandarajah-Jones, Michael J. Cross |
Abstract |
Extracellular signal-regulated kinase 5 (ERK5), also known as big MAPK (BMK1), is the most recently identified member of the mitogen-activated kinase pathway. It is ubiquitously expressed in mammalian cells and is activated by a number of growth factors. Gene knockout studies in mice have shown a critical role for ERK5 cardiovascular development and vascular integrity. Current methods to detect ERK5 activation in cells have relied on in vitro kinase assays and more recently phospho-specific antibodies. However, antibodies produced against phosphorylated proteins can often yield inconsistent data. Phos-tag™ Acrylamide is a reagent that enables specific tagging of phosphorylated proteins, resulting in retarded mobility and a distinct upward band shift from the non-phosphorylated protein following SDS-PAGE. Here, we describe the details of Phosphate affinity SDS-PAGE of ERK5 using acrylamide-pendant Phos-tag™. |
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