(second article below)
Why our SCB scientists think using insect cells (sf9) to express Ubiquitin is a good idea
Behind every functional ubiquitin enzyme lies a careful choice: how and where it’s expressed.
Our scientists know that expression systems matter:
- E. coli offers speed, but many ubiquitin enzymes misfold, aggregate, or form inclusion bodies.
- Insect cells (like Sf9) provide a eukaryotic environment, enabling proper folding, post-translational modifications, and stability.
Equally important is the choice of purification tag (His, GST, or others) because ubiquitin-like proteins are small and easily misfolded if not handled properly.
By refining these details, SCB ensures that every enzyme we deliver is active, validated, and research-ready. It’s a subtle but critical part of our craft, turning complexity into reliability for scientists pushing the boundaries of ubiquitin research.
At SignalChem Biotech, our work with ubiquitin enzymes is about more than proteins. It’s about engineering clarity into a complex system.
The ubiquitin cascade works like a relay race: E1 activates ubiquitin, E2 carries it, and E3 attaches it to a target protein. Each step is essential, but how do you know if each handoff works?
That’s where assay design comes in. By tagging each step of the cascade, our scientists can:
– Validate enzyme function independently
– Pinpoint where a reaction stalls
– Tailor assays for E1s, E2s, or E3s based on research goals
Accelerate screening for inhibitors or activators at specific stages
This modular approach transforms a hidden molecular process into something measurable and engineerable, making the “invisible” visible for researchers worldwide.
