One of the advancements in protein purification has been to tag the protein of interest with a short sequence that can bind to an immobilized matrix and aid purification. Bio-Rad’s new IMAC resin offers a host of advantages for the purification of histidine-tagged proteins. Learn more about this resin and see how it can enhance the efficiency of your protein purification workflow.
Modern Improvements to Classic Technologies: Innovating Electrophoresis and Chromatography Upstream of Protein Characterization to Speed Up Research
When testing new drug therapies, it is essential to know the identity of the protein being tested. Chromatography is a commonly used technique to separate complex biological mixtures and isolate proteins of interest prior to downstream characterization. Learn more about how automating chromatography and stain-free technology are helping to save time and effort in protein purification.
A well-designed multidimensional (Multi-D) chromatography process, which utilizes optimized individual column methods, can help automate multistep protein purification processes. This can help you save time and increase productivity. See how you can use Multi-D chromatography to expedite the purification of polyhistidine-tagged proteins when using a typical capture, intermediate, and polish purification workflow.
A biomolecule protein purification workflow requires more than one resin. The trick is to find the combination of resins that provides the highest purity in the least number of steps and at the lowest cost. Here are some guides to select the optimal resins for the purification of monoclonal antibodies, native and recombinant proteins, Ig G and mammalian and adenovirus, and for removing aggregates and endotoxins.
Producing highly purified proteins in large quantities is a challenge and requires modification of methods and protocols to attain high efficiency. Dr Murat Kasap from Kocaeli University, Turkey, has overcome these difficulties by taking advantage of the modularity of the NGC Chromatography System and successfully synthesized and purified cardiac troponin-I protein.
Protein purification becomes a challenging step for applications requiring high protein concentrations (such as structural biology studies). This is also true for researchers purifying integral membranes proteins and untagged proteins from native sources. Here we provide some useful tips for selecting the proper resins, optimizing conditions and developing effective strategies to tackle the challenges associated with such difficult-to-purify proteins.
Multicolumn purifications are tedious and the manual operations during this process introduce variabilities, affecting the success of purification and reproducibility of results. This whiteboard animation explains how an automated multi-dimensional chromatography method can make this an easier process with very high success rates.
Mixed-Mode Chromatography for mAb S Aggregate Removal: Comparison of CHT™ Ceramic Hydroxyapatite, Capto adhere, and Capto adhere ImpRes
The separation of monomers from product-related impurities is quite challenging in process separations. It requires a thorough screening and an efficient resin to get efficiency in the purification process. Review the performance data of Bio-Rad’s mixed mode CHT™ Ceramic Hydroxapatite in achieving process separation efficiency and how it compares with various Capto media.
The best chromatography media should yield high protein purity and product recovery as well as be versatile enough to purify difficult samples. Bio-Rad’s CHT™ Ceramic Hydroxyapatite achieves this by virtue of being able to interact with the proteins through multiple modes, making the process extremely efficient. The whiteboard animation describes the mode of action of CHT.
What can chromatography peaks tell us? From the quality of column packing to the purity of separated proteins, a lot can be gleaned from the peaks. Here are some definitions that can help decipher what chromatography peaks can tell us.