:: Posted by avi_wener on 03-16-2010
In order to be useful in proteomics applications, a fluorescent stain must be sensitive enough to visualize protein quantities down to 1 ng or less, exhibit minimal protein-to-protein variability in staining intensity and fully compatible with 2D electrophoresis and mass spectrometric fingerprinting.
In this study, the performance of Bio-Rad’s Oriole gel stain is characterized with respect to its spectral properties, detection sensitivity, protein-to-protein variability and compatibility with mass spectrometry. Furthermore, the study describes how Oriole may be imaged using UV light which is ideal considering that UV-based imaging equipment is relatively simple and inexpensive and tends to be more generally available to laboratory researchers.
Oriole Fluorescent Gel Stain: Characterization with SYPRO Ruby Gel Stain
:: Posted by avi_wener on 03-14-2010
Stanford chemists W. E. Moerner and Randall Goldsmith have recently published a paper in Nature Chemistry (Nature Chemistry 2, 179 - 186, 2010) describing a technique that enables scientists to examine protein behavior in solution without significantly altering the molecule through immobilization. As Louis Bergeron explains, “Observing molecules one at a time is valuable because it lets researchers get a clear picture of that molecule’s changing behavior over time, without the picture being confused by the presence of other molecules.” Bergeron goes on to quote Goldsmith who says that this is significant because “up until now, researchers have had to remove a molecule from its normal environment – typically a solution such as the bloodstream or the fluids inside a cell – and basically staple it to some surface such as a glass slide or a large plastic bead, or imbed it in a synthetic polymer to observe it.”
The machine used in the study is known as the Anti-Brownian Electrokinetic (ABEL) trap which works by cancelling out a molecule’s Brownian Motion (remember physics 101…those were the days!). There are only 3 ABEL traps in existence world-wide.
As I’ve discussed several times on the American Biotechnologist blog, I believe that a more holistic approach towards biological research such as the “omics” revolution is a healthier way of studying science and will lead to a richer set of observations over time. Protein chemistry can be a particularly difficult nut to crack as it is challenging to study the physical characteristics of proteins without removing them from their natural environment. This latest study is a feather in the cap of protein chemists and should be given recognition by fellow protein scientists interested in the “omics” revolution.
I’d love to see more of these types of studies. Wouldn’t you?
