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Top 5 Luciferase Reporter Vectors You Didn’t Know You Needed (But Now Can’t Live Without) 

Posted on by Simon Moe

Ever spent your Friday night troubleshooting a cloning reaction that just won’t work? 

We’ve been there. So have thousands of other scientists. That’s why Promega and Addgene teamed up to create something game-changing: a curated collection of 600+ luciferase reporter vectors, designed to help you skip the cloning and get straight to the data. 

Addgene, the nonprofit plasmid-sharing platform trusted by researchers worldwide, and Promega, a global leader in luminescent assay technologies, have joined forces to make your gene expression, pathway analysis, and cell signaling experiments faster, easier, and reproducible. 

In this post, we’re spotlighting 5 standout vectors from the new collection that are making life in the lab a whole lot better. 

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One Health in Action: Integrated Solutions for Animal Health Pathogens

Posted on by Promega

For research use only

Introduction: Diagnostic Innovation for Zoonotic Threats

When a veterinarian detects influenza A in pigs, they’re not just protecting a herd; they’re helping safeguard public health through broad ongoing surveillance.

To support rapid, biosafe detection of Influenza A viruses (H5N1, H3N2, H1N1) in animal populations, Promega and Longhorn Vaccines and Diagnostics have partnered to create a workflow that doesn’t require BSL-3 containment. It’s scalable, field-ready, and designed with One Health in mind.

This work is part of our broader commitment to enabling real-time disease surveillance—across species and borders. Together with Longhorn, we’re building molecular diagnostics that meet the moment, and the future.

Want the technical details? Read the press release. 

Why It Matters: Influenza A and Diagnostic Bottlenecks

Influenza A viruses—including highly pathogenic strains like H5N1—pose a dual threat to animal health and human safety. Yet despite the urgency, many surveillance and research efforts stall at the lab bench. Why? Because working with zoonotic pathogens often requires high-containment (BSL-3) facilities—especially when dealing with real-world samples like cow milk, poultry swabs, or pig oral fluids.

To help overcome this barrier, Promega and Longhorn set out to design a complete diagnostic workflow that does more than just detect. It needed to:

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What Drives Muscle Fiber Shifts in Obesity and Type ll Diabetes?

Posted on by Kari Kenefick

Skeletal muscle is the body’s main consumer of glucose derived from food.

Muscle Fiber Types
Skeletal muscle is composed of two types of muscle fiber: Type I (slow-twitch) and Type II (fast-twitch).
Type I fibers contract slowly and can maintain contraction over long periods of time. They are rich in mitochondria and myoglobin and are well vascularized. These fibers rely mostly on aerobic metabolism to make the ATP that fuels cells. Type I muscle fibers are fatigue-resistant and efficient—great for supporting posture, distance running, cycling and any activity that needs steady output.

Type II fibers contract quickly, produce more force and power, but also fatigue more quickly. They have fewer mitochondria and less vasculature and rely more on anaerobic pathways like glycolysis (using glucose without oxygen).

Type I muscle fibers are smaller in diameter and generate less peak force but excel at endurance and heat management. Type II fibers are typically larger, produce more force and speed and handle explosive tasks like sprinting, jumping or heavy lifting.

Most muscles are a mix of fiber types, and genetics sets the starting ratio of Type l to Type ll, but fibers are adaptable. With aging and disuse, Type II fibers tend to atrophy more, which is one reason that power declines faster than endurance.

Another distinction important for this story: Type I fibers are more insulin-sensitive than Type II fibers. Additionally, these fiber types differ in different body types.

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Measure Engagement to Target Proteins within Complexes: Why Context Matters

Posted on by Promega

This blog was written by guest contributor Tian Yang, Associate Product Manager, Promega, in collaboration with Kristin Huwiler, Manager, Small Molecule Drug Discovery, Promega.

For target-based drug discovery programs, biochemical assays using purified target proteins are often run for initial hit discovery, as these assays are target-specific, quantitative and amenable for high-throughput screens, allowing for precise characterization of target-compound interactions. However, proteins do not act in isolation inside the cells. Instead, proteins form complexes with other cellular components to drive cellular processes, signaling cascades, and metabolic pathways. Just as the interactions between a target protein and its binding partners can influence the target function, compound engagement with target proteins can vary depending on the protein complex formed.

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At the Forefront of Biologics Characterization: Insights from Promega R&D Scientists 

Posted on by Tera Madigan Ogorazalek

As biologics grow more complex, so do the tools required to understand, validate, and ensure their quality. From monoclonal antibody cocktails to antibody-drug conjugates (ADCs) and cell therapies, developers are navigating new frontiers in potency, purity, and functional characterization. 

Promega’s R&D scientists have been actively contributing to this evolving dialogue through respected industry platforms like BioCompare and BEBPA. Through ongoing collaboration with industry experts, Promega scientists are developing innovative assays and strategies that address the complex challenges of biologics development and quality assurance. 

This article highlights key takeaways from five recent publications featuring Promega experts and collaborators, with insights spanning from early research to quality assurance in manufacturing. 

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Cellular Selectivity Profiling: Unveiling Novel Interactions and More Accurate Compound Specificity

Posted on by Promega

This blog was written by guest contributor Tian Yang, Associate Product Manager, Promega, in collaboration with Kristin Huwiler, Manager, Small Molecule Drug Discovery, Promega.

Determining the selectivity of a compound is critical during chemical probe or drug development. In the case of chemical probes, having a clearly defined mechanism of action and specific on-target activity are needed for a chemical probe to be useful in delineating the function of a biological target of interest in cells. Similarly, optimizing a drug candidate for on-target potency and reducing off-target interactions is important in the drug development process (1,2). A thorough understanding of the selectivity profile of a drug can facilitate drug repurposing, by enabling approved therapeutics to be applied to new indications (3). Interestingly, small molecule drugs do not necessarily require the same selectivity as a chemical probe, since some drugs may benefit from polypharmacology to achieve their desired clinical outcome.

Selectivity profiling panels based on biochemical methods have commonly been used to assess compound specificity for established target classes in drug discovery and chemical probe development. Biochemical assays are target-specific and often quantitative, enabling direct measurements of compound affinities for targets of interest and facilitate comparison of compound engagement to a panel of targets. As an example, several providers offer kinase selectivity profiling services using different assay formats and kinase panels comprised of 100 to 400 kinases (4). However, just as biochemical target engagement does not always translate to cellular activity, selectivity profiles based on biochemical platforms may not reflect compound selectivity in live cells (5).

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Is Your Lab Environment Messing with Your Results? How to Spot the Signs Early

Posted on by Promega

This blog was contributed by guest Avi Aggarwal, 2025 summer intern at Promega.

If you’ve ever scratched your head over inconsistent experimental results, especially ones that seem to fluctuate for no obvious reason—you’re not alone. Sometimes the problem isn’t your pipetting, your reagents, or even your protocol. It might be the room itself.

Changes in temperature, humidity, or even invisible dust particles can quietly throw off your results. Something as simple as moving your thermocycler under an air vent or setting up a plate reader where sunlight hits it in the afternoon could cause subtle but significant issues.

Scientist removes samples from liquid nitrogen tank, affecting the immediate laboratory environment.
Any number of things can affect the laboratory environment, from opening a cryo tank to moving an instrument under an air vent.

Our Project to Learn How Subtle Environmental Changes Can Affect Sensitive Lab Equipment

We spent some time developing an environmental anomaly detection framework aimed at helping scientists understand how subtle environmental changes can affect sensitive lab equipment and experimental results. Our team set out to monitor real-world lab conditions using temperature and humidity sensors, including live testing with a GloMax® Discover platform and Sensirion SHT45 sensors. We also worked with open-source environmental datasets to simulate a variety of lab-like conditions, such as daily cycles, sudden temperature spikes, and slow humidity drifts.

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Unlocking the Power of Live-Cell Kinetics in Degrader Development

Posted on by Kelly Grooms

In targeted protein degradation (TPD), timing is everything. Understanding not just whether a degrader works—but how fast, how thoroughly and how sustainably—can dramatically influence early discovery decisions. Dr. Kristin Riching (Promega) dove into the real-time world of degradation kinetics in the webinar: Degradation in Motion: How Live-Cell Kinetics Drive Degrader Optimization, sharing how dynamic data provides a clearer view of degrader performance than traditional endpoint assays.

Whether you’re exploring your first PROTAC or optimizing a molecular glue series, the expertise offered in Dr. Riching’s presentation gives you actionable insights that will help you connect kinetic data to better therapeutic design.

3D visualization of a protein structure within a live-cell environment, highlighting the interaction site relevant to targeted protein degradation, set against a dark cellular background to emphasize kinetic dynamics.
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How Thalidomide and Molecular Glues Are Redefining Drug Discovery

Posted on by Kari Kenefick

Targeted protein degradation (TPD) is a strategy used to selectively remove proteins from cells, rather than simply blocking their activity. Traditional small-molecule drugs work by binding to a protein and inhibiting its function, leaving the protein intact. In contrast, TPD harnesses the cell waste-disposal system—in particular, the ubiquitin-proteasome pathway—to tag the target protein for destruction. Once tagged, the protein is chopped up and recycled by the proteasome, eliminating it from the cell.

Perhaps the best known TPD approach uses PROTACs (proteolysis-targeting chimeras), which are bifunctional molecules: one end binds the protein of interest, and the other recruits an E3 ubiquitin ligase. By bringing the protein and ligase together, the PROTAC triggers ubiquitin tagging and subsequent degradation.

How NanoBRET works image.

Molecular glues achieve the same end result—selective protein destruction—in a different way. Instead of acting as a physical bridge between the protein and the E3 ligase, molecular glues bind to one protein (often the ligase) and subtly change its shape or surface properties, improving interaction with the target protein. This induced fit causes the target protein to be ubiquitinated without a large, two-part molecule like a PROTAC.

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ATP-Powered Proteins Beyond Kinases – and Why Helicases Are Stealing the Spotlight

Posted on by Kari Kenefick

This blog was written by guest author Michael Curtin, Senior Product Manager, Small Molecule Drug Discovery.

ATP is the universal energy currency of cells, and thousands of proteins outside the kinase family “spend” it to move cargo, remodel nucleic acids, pump ions, or fold proteins. These ATP-hydrolyzing enzymes—collectively known as ATPases—span functional classes including motor proteins, transporters, chaperones, chromatin remodelers, ligases, and, crucially for genome stability, helicases.

From DNA replication to RNA processing, helicases are essential players. DNA/RNA helicases such as MCM, XPB/XPD, WRN, and members of the DDX family sit alongside AAA+ unfoldases, ABC transporters, and V-ATPases—all drawing on ATP to power their molecular work.

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