Product category:
Genomics
News Release from: GE Healthcare | Subject: Ni Sepharose High Performance
Edited by the Laboratorytalk Editorial
Team on 20 January 2004
More reliable purification of
recombinant proteins
Purification of His-tagged recombinant proteins has been made more reliable with new affinity chromatography medium, said to offer the highest binding capacity on the market today
A new affinity chromatography medium announced by Amersham Biosciences offers optimised purification of His-tagged proteins Ni Sepharose High Performance provides better protein binding capacity, negligible Ni leakage and compatibility with a wide range of reducing agents, detergents, denaturants and other additives
This article was originally published on Laboratorytalk on 18 Apr 2003 at 8.00am (UK)
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The 34um bead matrix is said to offer the highest binding capacity available on the market today, to provide more concentrated samples, higher efficiency, time savings and increased yield.
With negligible Ni leakage, the medium minimises protein precipitation, and increases purity as well as yield.
Allan Simpson, vice president laboratory separations at Amersham Biosciences comments, "Ni Sepharose High Performance is optimised for the purification of His-tagged proteins.
"Scientists in industrial and academic labs utilising this new medium will have no difficulty translating its advantages into greater purity, higher yields and increased activity, as well as greater operational flexibility".
In addition to lab packs, Ni Sepharose High Performance is available as pre-packed HisTrap HP columns and HisTrap HP kit for convenience and time-saving advantages.
These HisTrap HP columns can be used with a syringe, a laboratory pump or chromatography systems.
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