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The success of the expression of (recombinant) proteins for protein structure analysis depends on many factors, one of which is the consistent and controlled growth of the cell line used.

 

Digilab HiGro® offers high-capacity incubation and shaking for accelerated sample growth in microwell plates. This uniquely engineered instrument combines a small shaking orbital, gas flow and temperature control system in a user-friendly, compact layout. Plate-holding cassettes allow for easy loading and unloading.

 

PROTEIN STRUCTURE

SAMPLE. SCIENCE. SOLUTIONS.

In proteomics-based biomarker and drug discovery using 2D electrophoresis, after an experiment is concluded the gels are analyzed for differentially expressed proteins. In many cases the next step is the excision of proteins of interest from the gel and in-gel proteolytic digestion for further identification using mass spectrometry. Manual excision might be an inexpensive solution for very low throughput and gels with just a few spots. However, automated spot excision is an indispensable tool for higher throughput and for complex gels adding a level of accuracy, precision, and reliability that can not be achieved otherwise.

 

Digilab has improved the ProPic II™ protein gel picking technology with the addition of a high resolution line scanning imaging system and utilization of their market leading benchtop microarraying platform to provide the highest possible XYZ picking accuracy. The result is accurate and reliable picking of the smallest and most closely spaced protein features. Digilab ProPic II™ offers third generation imaging and picking integrated on a single platform, small footprint, 16-bit imaging, 10x improvement in picking accuracy over the ProPic with direct imaging and picking from gels stained with all commonly used fluorescent and visible stains, and seamless integration with 2D DIGE.

Counter diffusion offers several advantages over other crystallization methods. As the protein and precipitant solutions diffuse against each other within the capillary, a continuum of potential crystallization conditions is created resulting in the equivalent of several vapor diffusion experiments within each capillary. Additionally, crystals are often larger and of improved quality resulting in enhanced X-ray diffraction data. By scanning down the length of each capillary, the quality of the crystals can be evaluated while maintaining their environmental integrity (eliminating the need for manual crystal manipulation). Additives such as ligands or heavy atom derivatives can also be slowly diffused into the protein crystallization process for further biochemical and crystallographic requirements.