Don’t fix it.
Ironically, SDS-PAGE (sodium dodecyl sulfate–polyacrylamide gel electrophoresis) has been around longer than the phrase.1 It’s hard to imagine a scientific process that has been relatively unchanged in more than fifty years; a process that predates the pocket calculator and man’s first steps on the moon. Nevertheless, this protein analysis procedure has been used for nearly five decades as a quick, cost-effective assay.
Since SDS-PAGE is covered in great detail in many other places, we’ll just share the short version with you. In brief, it is a process by which proteins are separated by their molecular weight for observation. The proteins are first denatured, or linearized, and given a negative charge. This is done using a buffer with sodium dodecyl sulfate (SDS). A buffer is added and then current is applied which draws the particles into bands of different sized particles. This can then be stained or further processed for assessment and analysis.
The fundamental principal, electrophoresis, dates back to the 1940s and Arne Tiselius who discovered it. For his work he was awarded the Nobel Prize in Chemistry.2 Ornstein and Davis further improved the separation, and thus clarity, in 1964 by employing the stacking effect. A year later, David Summers, working with poliovirus proteins, further improved the resolution and essentially defined what is today known as SDS-PAGE. Most commonly used methods today are derived from the discontinuous SDS-PAGE system described by Laemmli 1970.
Advanced Biotechnologies’ goal is to consistently deliver the purest viral reagents. SDS-PAGE is a tried and true QC we utilize to qualify many of our products. This assay, often one of many, is critical in determining the purity of the product we produce. It ensures you get the best we have to offer. Our eye is ever on the horizon for a process that matches the efficiency and cost-effectiveness of SDS-PAGE. But, until a replacement to this tried and true method is discovered, we’re ok going “old school”.