CHRONECT | Workstation Proteomics
Automated sample preparation in the proteomics lab to optimize throughput and avoid handling errors.
The mass spectrometric identification and quantification of proteins requires a prior cleavage of the proteins into peptides. This cleavage is called protein digestion. It takes place with the help of enzymes such as the protease trypsin or the endopeptidase Lys-C.
Proteins can be analyzed using mass spectrometry methods either with proteins in solution or with proteins that have been separated on SDS gel electrophoresis. The sample preparation consists of several steps. After denaturing and washing the sample, the first step is the reduction and subsequent alkylation of the sulfhydryl groups of the proteins. The reagents TCEP and CAA are used for this. This is followed by the actual enzymatic digestion and the subsequent extraction of the newly formed peptides, which can then be analyzed by mass spectrometry.
- High sample throughput
- High degree of automation
- Flexible, easily customizable
- Based on the experience of a large proteomics research center
- Ideal for laboratories with medium sample throughput
- No risk of contamination
- Excellent reproducibility
- investment security
Automation is performed based on the reli-able Pal samplers and the software plat-form CHRONOS. The application system consists of the following components:
- Vacuum tray for In-gel digest with a vacuum pump
- CHRONOS Software with pre-in-stalled methods
- Data system for controlling
- SOP generated by the Max-Delbrück-Centrum for molecular medicine
- Accessories and consumables
- Briefing, commissioning, training and suppor