Roche has announced the launch of its new cOmplete His-Tag Purification Column for researchers performing histidine-tagged protein purification from lysates.
The new column uses Roche’s proprietary nickel-chelate chemistry and is compatible with commonly used reducing agents (DTT), metalloproteinase inhibiting reagents such as EDTA, and different buffer and salt environments.
This allows researchers to choose optimal buffer conditions for the target protein in a convenient pre-packed format.
“We have received very positive feedback from pilot users who appreciate the flexibility of being able to purify proteins under protein protecting conditions,” said Ruedi Stoffel, Head of Biochemical Reagents & Custom Biotech.
Stoffel continued, “It enables our customers to apply any buffer required to obtain proteins of high purity, stability and function.”
Following the purification step, the new column does not require buffer exchange or resin recharging therefore avoiding a costly and time consuming process.
In addition, the resin’s minimized nickel ion leakage not only reduces toxic nickel waste, but also stabilizes the target protein by preventing nickel ions from catalyzing protein oxidation.
Thanks to the additional format, researchers can choose their preferred method of purification. The cOmplete His-Tag Purification Resin can be used for batch purification as well as on automated systems based on FPLC.
Pre-packed cOmplete His-Tag Purification Columns are available in two sizes (1 ml and 5 ml) and are compatible with standard instruments for protein purification.