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Molecular Diagnostics (MDx)
Tuesday, September 26, 2017
Christopher Eggers, PhD
Regulated protein abundance and surface expression are fundamental to normal cellular physiology and dysregulation underlies many disease states. Monitoring changes in protein abundance usually involves labor-intensive, antibody-based methods that yield only semi-quantitative results. This webinar will introduce a bioluminescent tagging system that can quantify proteins in minutes using simple, antibody-free methods. This system offers wide dynamic range and sensitivity compatible with detecting even endogenously expressed proteins when combined with CRISPR gene editing.
Tuesday, September 19, 2017
Ulrike Herbrand, PhD
In past years, the requirement for bioactivity testing changed from later phase lot release and stability testing to additional applications like biocomparability testing for follow-on biologics, accelerated stress condition testing and confirmation of successful production scale up. Therefore a suitable bioassay is needed at a very early time point. This webinar will look at a wide variety of therapeutic proteins and illustrate some best practices in method development that results in reliable, reproducible and precise assays, and discuss which assays may be best for your product and development program.
Tuesday, September 12, 2017
Donna Leippe, PhD
Metabolite detection technologies can pose challenges such as laborious sample preparation and the inability to assay numerous samples rapidly. Additionally, lack of sensitivity and dynamic range prevents detection of metabolites directly in cells in multi-well plates.
In this webinar, we describe new bioluminescent metabolite assays and sample processing strategies that enable rapid measurements of key energy metabolites in plate formats and show how the assays can be used to study cancer cell metabolism and activation of T cells.
Tuesday, June 13, 2017
Sergei Saveliev, PhD
Non-enzymatic post-translational modifications (PTMs) spontaneously occur in biotherapeutic proteins during manufacturing and storage. These modifications negatively affect efficacy and stability of biotherapeutic proteins. Major non-enzymatic PTMs are deamidation, disulfide bond scrambling and oxidation. These non-enzymatic PTMs are also introduced during protein preparation for peptide mapping and compromise the analysis. In the webinar recording Dr. Saveliev discusses sources of these artificial protein modifications as well as procedural optimizations to suppress these PTMs.
Tuesday, April 11, 2017
Hicham Zegzouti, PhD
Post-translational modifications (PTMs), the addition of functional groups to proteins, play a significant role in regulating cellular biology. Examples include phosphorylation, a common mechanism in regulating enzymatic activity, and the addition of carbohydrates to many eukaryotic proteins, which promotes proper folding, improves stability and serves in regulatory functions. A key objective of research and drug discovery surrounding PTMs is to study the regulation of these enzymes and find specific modulators of their activity. Although mass spectrometry, eastern and western blotting detection technologies have been used traditionally, none are amenable to high throughput or as sensitive as bioluminescent detection of nucleotide-based substrates for such enzymes.