"It does everything we need when it comes to protein characterization"
The list of featured applications is long and ever growing. Here are some of the most used ones.
Labbot is not a tool to do just one thing. We offer a platform of core capabilities and the freedom to put them together to fit the experiment you want to do. We are excited to see what you will come up with.
Automation can be much more than a simple quality-of-life improvement. The enhanced reproducibility, precise control and freed-up time will also bring experiments that were previously too challenging into the realm of the possible.
Add new measurement techniques to your existing protocols? Take an old measurement and expand it across temperature or concentration? Automate a tedious procedure and multiply your output?
You deserve the best tools available for your science. We are excited to see what new possibilities you will unlock with your Labbot.
An early adopter since the first version, Sara and her group have put Labbot to work in projects ranging from calcium binding to the role of electrostatics in protein aggregation.
In an ongoing study she is following dissociation kinetics by rapidly diluting samples and recording a combination of FRET and light scattering. With Labbot it has been convenient to repeat the experiment at different temperatures to explore the thermodynamics of the system.
"One of the best features is that we can track the reaction with multiple readouts from the same sample. It really gives a few extra layers of insights."
This 2009 paper serves as the origin story of Labbot. Faced with the need to characterize the response of a pH sensitive probe with very high precision, Thom decided to automate the task. The device featured a CCD detector with the capacity to automatically record absorbance spectra as a set of computer controlled syringe pumps added small volumes of acid or base.It was clear already from the beginning that this method not only reduced the hassle of making these measurements, but also greatly improved the data density, quality and precision.
The authors identified and characterised peptide inhibitors of amyloid aggregation. The interactions between the inhibitors and amyloid fibrils are confirmed using several complementary methods, including Förster Resonance Energy Transfer (FRET). By labelling the interaction partners with FRET-compatible Alexa dyes and following their fluorescence intensities they could monitor the interactions throughout the entire reaction.
This paper focuses on the interplay between electrostatics and aggregation in an amyloid system. Rather than changing the pH by titration and recording the response, the authors follow a reaction in an unbuffered system and record the resulting pH change. They also follow the reaction using fluorescence readout and static light scattering in order the pH response to the aggregation reaction.
We are proud to work with our customers to facilitate great science. If you have any technical problems or have questions about how to make a specific application work, our small but dedicated team is here to help.
... I was a fresh Ph.D. student in Biochemistry, yearning to plunge into science. The goal of the project I was assigned was to understand what made a specific virus protein so important for the virus to spread.
The idea was to reconstitute the protein into artificial cell membranes and measure the flow of ions through it. Long story short, me and my supervisor Sindra decided to use a proton gradient as a driving force and a pH-sensitive dye as a reporter.
There was a tricky thing with this method. It would require me to perform an exact pH calibration of the dye for every batch of proteoliposomes we made. Although the principle of pH titration is quite simple, anyone who has made one manually knows it is difficult especially if you want equidistant data points.
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