Ligand Immobilization in Protein Interaction Studies — An Unattended Amine Coupling Protocol with Automatic Coinjection Activation
Amine coupling is the most commonly adopted technique to bind proteins to biosensor chips. Because of the possibility of the amine coupling reagents reacting with each other, these have to be premixed just before the injection and injected independently. Here are some tips to automatically coinject these reagents.
Novel Liposome-Capture Surface Chemistries to Analyze Drug-Lipid Interaction Using the ProteOn™ XPR36 System
Surface plasmon resonance (SPR) biosensors offer a label-free technique for profiling biomolecular interactions, including those between drugs and liposomes. Here we describe the novel surface chemistries that make capturing liposomes possible, and explore the application of the liposome capturing kit in analyzing liposome-small molecule interactions.
Building New Anti-HIV Molecules with Bio-Rad’s ProteOn™ XPR36 System
Can we construct molecules that will interfere with disease pathways? Dan Mitchell of the University of Warwick and his colleagues wanted to apply new synthesis techniques to interrupting HIV infection. Find out what they learned about the potential of these novel molecules using Bio-Rad’s ProteOn™ XPR36 System.
Immobilization of Active Kinases for Small Molecule Inhibition Studies
Surface plasmon resonance (SPR) is a well-established and important screening tool in the small molecule drug discovery workflow. Using the Bio-Rad SPR system ProteOn XPR36, rapid optimization of immobilization conditions for a kinase target was carried out in a fast workflow with a single sensor chip, showing the high performance of the ProteOn XPR36 system.
Video Tutorial for Analyzing Binding Interactions with Histidine-Tagged Proteins
Analyzing antibody binding to histidine-tagged proteins is not always easy because of inherent problems such as nonspecific binding and loss of analyte response associated with these tagged proteins. Optimization of these factors is key to precisely measuring the binding kinetics of these proteins.
Highly Efficient Lipoparticle Capture and SPR Binding Kinetics of a Membrane Protein Using the ProteOn™ XPR36 Protein Interaction Array System
The genes coding for membrane proteins, such as G-protein coupled receptors (GPCR), ion channels, and other membrane-bound enzymes make up 25–30% of the human genome and membrane proteins are estimated to represent 30–40% of the top drug targets. There is growing research, industrial, and commercial interest in the study of membrane proteins in general, and more specifically in immobilizing membrane proteins to various biosensor surfaces.
One Array, 36 Unique Protein Interactions
The ProteOn XPR36 protein interaction analysis system was introduced in 2006 to provide a novel array technology to researchers conducting label-free analysis of proteins. The ProteOn system is a high-throughput surface plasmon resonance-based screening tool for a wide range of applications from small-molecule drug discovery to antibody kinetic ranking, epitope binning, and epitope mapping.