I am encountering an issue when using A/G magnetic beads for eluting membrane proteins from my samples. It seems that the proteins tend to aggregate during the elution process, which is hindering my results.
Could anyone provide recommendations or strategies to improve the elution of these membrane proteins? Are there specific buffers, conditions, or methods that could help prevent aggregation? Your expertise and suggestions would be greatly appreciated!
Lucian Miles
Acidic elution can be used, or 50-100 mM L-arginine can be added to reduce aggregation by shielding the hydrophobic surface of the antibody. Adding 50-150 mM NaCl can increase the ionic strength and neutralize the surface charge, thereby reducing aggregation caused by electrostatic interaction between antibodies. At the same time, attention should be paid to the isoelectric point of the eluted protein, and the buffer pH should avoid this isoelectric point.
Marine Ma ,
The answer to this question comes from MedChemExpress (MCE) Technical Support.
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