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Most problems with misaligned printouts on the printer supplied with the TC20 and TC10 cell counters can be solved by cleaning the print heads. In this short video, find out the fast, easy, and effective way to clean these print heads so you can get back to your research!
Good data processing practice ensures that protein interaction experiments using a surface plasmon resonance (SPR) system will yield the clearest possible results. Here we present tips for understanding and processing SPR sensorgrams when using Bio-Rad’s ProteOn™ XPR36 protein interaction array system.
Analyzing protein interaction data using a surface plasmon resonance (SPR) system can be complicated. This user guide describes how to analyze SPR data to obtain kinetic and equilibrium constants, as well as sample concentrations.
This appendix to “Guide to SPR Data Analysis on the Proteon™ XPR36 System” gives information on the data set export using ProteOn Manager™ Software.
Using Bio-Rad’s PDQuest Software to Generate a Match Rate between 2-D Electrophoresis and Western Blotting
2-D electrophoresis followed by immunodetection of protein spots using western blotting is adopted commonly in proteomics studies. Here we present step-by-step instructions for obtaining accurate overlaps between the gel and the blot using the PDQuest 2-D gel analysis software.
A Novel Biotinylated Ligand-Capture Method with Surface Regeneration Capability for Label-Free Biomolecular Interaction Analysis
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.
Analyzing Binding Kinetics with Surface Plasmon Resonance Complemented with Direct Mass Spectrometry on the Same Sensor Chip
Surface Plasmon Resonance (SPR) is an optical phenomenon that is used for the label-free analysis of the binding of any two molecules in real-time.
Learning to use analysis software can be time-consuming and following a manual can be challenging.
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.
Today many researchers are considering changing their western blot detection method from chemiluminescence to multiplex fluorescence. There are several drivers behind this trend. Most significantly, fluorescent detection allows users to multiplex their western blots, enabling simultaneous detection of several target proteins at once, reducing or eliminating the need to strip and re-probe. Other benefits of fluorescence include better dynamic range, more quantitative results, and better signal stability over time.