It’s always nice to know that someone is reading your paper. It’s a sign that your research is interesting, useful and actually has an impact on the scientific community. We were thrilled to learn that papers published by Promega scientists made the top 10 most read papers of 2017 in the journal ACS Chemical Biology. In fact, Promega scientists authored five of the top six most read papers! Let’s take a look at what they are.
Publication Date (Web): September 11, 2017
This 2017 paper introduces our newest star: HiBiT, a tiny 11aa protein tag. To any scientist studying endogenous protein expression, the HiBiT Tagging System is your dream come true. It combines quantitative and highly sensitive luminescence-based measurement with a tiny-sized tag that can be easily inserted into endogenous protein via CRISPR/Cas9 gene editing with little impact on native protein function. The HiBiT Tagging System has been listed as a 2017 Top 10 Innovation by The Scientist, and it will drastically change how we study endogenous protein expression.
Publication Date (Web): May 25, 2015
Traditional methods for studying protein:protein interactions are commonly performed in vitro using protein fragments, but they don’t necessarily reflect what happens in a natural cellular environment. Then came NanoBRET™ PPI. The NanoBRET™ PPI system uses NanoLuc® Luciferase as a BRET energy donor and HaloTag® protein as the energy acceptor to measure the interaction of specific protein pairs. The improved spectral overlap, higher sensitivity, increased signal and lower background, provide researchers with a reproducible method for studying protein interactions expressed at physiologically relevant levels.
Publication Date (Web): August 15, 2012
In 2012, Promega scientists engineered a small luciferase subunit from the deep sea shrimp Oplophorus gracilirostris and developed a new substrate, furimazine. The new NanoLuc® luciferase produces luminescence ~150-fold brighter than firefly or Renilla luciferases. The brightness of NanoLuc® combined with its small size (19kDa), high thermal stability, activity over a broad pH range, lack of post-translational modifications and uniform cellular distribution make it an ideal tool for a wide variety of protein analyses. Since its launch, NanoLuc® luciferase has become a hallmark product of Promega and countless discoveries have been made with it!
Publication Date (Web): June 6, 2008
This HaloTag® paper was published back in 2008, but it’s still one of the most read papers in 2017! The HaloTag® protein is a 34kDa monomeric derivative of dehalogenase. It was engineered to enhance expression and solubility of recombinant proteins in E. coli and to provide efficient protein purification coupled with tag removal. When expressed as N-terminal HaloTag® fusions in E. coli, target proteins can be produced at higher levels with higher solubility compared to other fusion tags. Using the HaloTag® Protein Purification System, you can get protein of higher yield, purity and free of tag. It’s amazing that the technology developed ten years ago is still highly relevant today.
Publication Date (Web): November 16, 2015
The #1 most read Promega paper in 2017 announced the birth of NanoLuc® Binary Technology, or NanoBiT®, which is a structural complementation reporter based on NanoLuc® luciferase. The NanoLuc® luciferase was separated into two parts: a smaller 11aa peptide (SmBiT) and a larger 156aa subunit (LgBiT), and the two have low affinity for each other. This system is perfect for studying protein:protein interactions. When a target protein tagged with LgBiT interacts with a protein tagged with SmBiT, the two subunits will complement each other and form a bright, luminescent enzyme. Even better, the LgBiT:SmBiT interaction is reversible and can be detected in real time!
These publications are just a few examples of the exciting work done here at Promega. We hope the technology we develop will make your jobs as scientists easier and lead to more discoveries. What is your favorite Promega technology? Let us know!