Ni Sepharose excel media
His Mag- and Ni Sepharose excel are immobilized metal ion affinity chromatography (IMAC) media (resins) designed for capture and purification of histidine-tagged proteins secreted into eukaryotic cell culture supernatants.
Nickel ions are very strongly bound to both media, enabling direct loading of large sample volumes without removing agents that normally would cause metal ion stripping. Both media significantly simplify and speed up the workflow and are excellent choices when working with purification of histidine-tagged proteins secreted from eukaryotic cells.
- Load eukaryotic cell culture samples containing secreted histidine-tagged proteins directly with retained binding capacity
- Increase target protein yield and decrease degradation through reduced and simplified sample handling
- Choose between several different formats for screening and preparative purification of histidine-tagged proteins
IMAC purification of histidine-tagged proteins secreted into eukaryotic cell culture supernatants has traditionally been challenging because of incompatibility between the IMAC medium and the cell culture medium. The cell culture medium strips the immobilized metal ions from the IMAC medium during sample loading, resulting in low or no binding of the target protein. The purification has been further complicated by the fact that the target protein concentration is often low. This requires the use of large sample volumes, which in turn might lead to increased metal ion stripping. Considerable sample pretreatment has been required to overcome these problems, an example being buffer exchange by diafiltration in combination with concentration procedures. Such pretreatment is time consuming, potentially harmful to sensitive proteins, and can cause unnecessary loss of target protein.
GE Healthcare Europe GmbH
Andrea Löhndorf, PhD, MBA
Regional Marketing Manager
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