The Protein Man's Blog | A Discussion of Protein Research

Gel electrophoresis is a simple, rapid and highly sensitive tool that can be used to separate proteins based on their physical properties (e.g. molecular weight and native charge or isoelectric point) prior to downstream detection or analysis. The separation of proteins by electrophoresis can be explained by the fact that charged molecules will travel through a gel matrix when an electrical current is applied. Proteins are commonly separated in this manner using polyacrylamide gel electrophoresis (PAGE) to identify individual proteins in complex samples or to examine multiple proteins within a single sample.

As you probably know, biotechnology has grown tremendously over the past decade. What you may not know, however, it is now being taught in some high school classes. This post will explore why biotech is being taught as early as high school and how this is paving the way for a new generation of biotech experts.

Since accurate protein quantitation is essential to all experiments related to protein studies, different methods have been developed to measure the concentration of proteins in a given assay. Some of the more traditional methods of total protein quantitation include the measurement of UV absorbance at 280 nm (A₂₈₀), Bicinchoninic acid (BCA) and Bradford assays, and other alternative methods such as Lowry and other novel assays.

While detergents can be used to extract, solubilize, and manipulate (disrupt or form) membrane proteins from biological membranes for subsequent biochemical and physical characterization, and are useful in controlling protein crystallization and preventing nonspecific binding in affinity purification and immunoassay procedures, they can also be one of your greatest foes in the laboratory.