Ligand-capture approaches using biotin as an affinity tag are often utilized in biomolecular interaction analyses with surface plasmon resonance (SPR) biosensors. However, a drawback to using biotin is that it makes surface regeneration of SPR sensor chips difficult. Here is a strategy that facilitates surface regeneration when using biotinylated ligand-capture approaches to SPR analysis.

The Fraser Laboratory in the Dept. of Molecular and Cellular Biology at UC Davis studies protein translation mechanisms by purifying diverse ribosomal proteins and reconstructing the translation complex in vitro. The lab utilized Bio-Rad’s NGC system to overcome specific purification difficulties with their protein while beta-testing the equipment. The NGC system enabled the group to increase their throughput by 25% and also saved substantial training time.

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.

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.

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.

The HTE sensor chip is designed for label-free biomolecular interaction analysis with polyhistidine-tagged proteins. It features a novel tris-NTA (3-NTA) surface for excellent performance of polyhistidine-tagged protein capture, providing high binding stability and regeneracy. It is an ideal choice for the applications of protein-small molecule and other protein interactions requiring high sensitivity.

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.