Top Stories of 2012

The McCarroll laboratory studies the biological effects of human genome polymorphism, seeking to define how genome variation influences gene expression and risk of disease.

Bio-Rad has long demonstrated innovation in imaging, with the introduction of the stain-free gel electrophoresis workflow, which was rapidly followed by the launch of the Gel Doc™ EZ imager. Now, this progression continues with the release of the ChemiDoc™ MP imaging system.

Hexapeptide libraries, such as Bio-Rad’s ProteoMiner™ protein enrichment technology, can significantly increase sensitivity of shotgun proteomics analyses of diverse complex samples. Underlying this increased sensitivity is the partial removal of high-abundance proteins leading to an increased representation of low-abundance proteins — a phenomenon described as dynamic range compression. Currently, hexapeptide libraries have been mostly used to increase proteomic detection in fluid samples (eg: saliva, plasma, etc.), but not in cellular lysates.

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.

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.