January 11th, 2017
•We report and demonstrate an optimized nitrocellulose binding assay that can be used to quantify autophosphorylation of purified bacterial histidine kinases. Our method has several advantages over traditional SDS-PAGE based techniques, providing a valuable alternative for characterizing these important proteins.
Related Videos
Assaying Protein Kinase Activity with Radiolabeled ATP
Measuring Protein Binding to F-actin by Co-sedimentation
Rab10 Phosphorylation Detection by LRRK2 Activity Using SDS-PAGE with a Phosphate-binding Tag
Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain
Detection of Small GTPase Prenylation and GTP Binding Using Membrane Fractionation and GTPase-linked Immunosorbent Assay
Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator
Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
Quantification of Protein Interaction Network Dynamics using Multiplexed Co-Immunoprecipitation