Laboratory Products
Simplifies Solubilisation and Purification of Membrane Proteins
Jan 04 2011
GE Healthcare’s Membrane Protein Purification Kit is designed for rapid and easy detergent screening of histidinetagged membrane proteins, enabling simultaneous evaluation of solubilization and purification efficiency. Analysis and evaluation can be performed by a number of methods such as Western blot, gel filtration, or light scattering.
The Kit contains seven detergents in ready-to-use solution (purity ≥ 99% by HPLC analysis), His Mag Sepharose™ Ni, buffer stock solutions, and an easy-to-follow protocol, and is sufficient for two complete screening experiments.
Integral membrane proteins play major roles in fundamental biological processes, and are common targets in the development of pharmaceuticals. To be studied, these proteins must be dispersed in an aqueous solution. To avoid protein loss and deactivation during solubilization and concomitant purification of integral membrane proteins, the choice of detergent is a key factor. Therefore, a detergent screen is often necessary to determine the optimal detergent for each protein
and purpose.
His Mag Sepharose Ni are magnetic beads designed for rapid, small-scale purification and screening of histidine-tagged proteins from different sources. The high density beads allow rapid capture by magnetic devices, while the visibility of the beads permits reliable collection of the bound histidine-tagged membrane proteins in the screening and purification procedure. Purification of target membrane proteins for a number of analytical or other downstream applications can be achieved within a few hours.
Digital Edition
Lab Asia 31.4 August 2024
August 2024
Chromatography Articles - HPLC gradient validation using non-invasive flowmeters Mass Spectrometry & Spectroscopy Articles - MS detection of Alzheimer’s blood-based biomarkers Labo...
View all digital editions
Events
Sep 11 2024 Bangkok, Thailand
Sep 11 2024 Bangkok, Thailand
Sep 11 2024 Singapore
Sep 18 2024 Lausanne, Switzerland
Sep 19 2024 Shanghai, China