In 2013, crystallographer and UAB Professor Dmitry Vassylyev was purifying proteins for crystallography studies when he began to develop the CL7/Im7 system. At the time, no single affinity chromatography system existed that could give him the desired ultra-high purity, tag-free protein with reasonable yield in a short amount of time.
This case study examines the Staley Lab’s success in using the CL7/Im7 system for their protein purification needs. Cody Hernandez, PhD candidate, shares his experience working with TriAltus’ methods to purify helicases, a mutant helicase, and several proteins.
Cas9 requires high purity in order to achieve high activity as a part of the CRISPR system for genetic modification. Due to a growing demand for Cas9 and an effort to improve its production, TriAltus conducted its own purification runs of Cas9 with success.
This blog post about pH in the context of protein purification is the third in a series about optimizing conditions for protein purification. Although pH is most commonly seen as an issue in ion-exchange chromatography, it also plays a critical role in affinity tag protein purification.
Using denaturing conditions is a way to coax insoluble proteins into solution by reducing hydrophobic effects and unfolding the aggregates. Denaturing agents are also useful for testing protein folding dynamics, protein elution from a column, and regenerating a resin column.