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PopCulture® Reagent* is a detergent-based concentrate that can be added directly to cultures of E. coli to effectively extract proteins without the need for cell harvest. Recombinant proteins can be directly screened in the crude extract or purified by adding an affinity matrix, washing the matrix-target protein complex to remove spent culture medium and cellular contaminants, and eluting the purified protein from the matrix. The entire culturing, extraction, and purification process can be performed in the original culture tube or multiwell plate. This “in-media” protein screening or purification procedure can be adapted to high-throughput robotic processing of samples
for proteomics research and any application that would benefit from the increased speed and convenience it provides. Successful purification of intact fusion proteins from total culture extracts has been demonstrated using His•Bind® and GST•Bind™ Resins (Grabski 2001). The use of His•Mag™ or GST•Mag™ Agarose Beads enables the entire procedure to be carried out in a single tube without the need for columns or centrifugation. Addition of rLysozyme™ Solution or the use of pLysS hosts increases the efficiency of protein xtraction with the procedure. Benzonase® Nuclease may also be added to reduce the viscosity of the extract.
PopCulture Reagent is supplied as a ready-to-use Tris-buffered liquid concentrate that is stable at room temperature.
Features:
• No separation of cells from culture medium
• No mechanical disruption of cells
• No clarification of cell extracts prior to purification
• Direct affinity adsorption of target proteins to resin from the total culture extract
• Ability to rapidly perform the entire cell growth and purification process in a single
tube or well
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