I need to purify serum glycoprotein present in very low concentration (2-10 ng/mL). Current method (sepharose bound monoclonal antibodies with subsequent elution on a filter plate) works, but gives quite poor protein recovery. Any suggestions to optimise the protocol or of another approach?
Our laboratory has had excellent results in protein purification performance with affinity chromatography to immobilized metals such as nickel or cobalt, IMAC-Ni.
Whether you can write more specific information about your method ?
@Jaroslaw, thanks for your reply. The method goes: VHH mAbs are immobilised on sepharose beads, incubated with protein in-solution (2h), transferred to filter plate, washed (PBS 3 times, MQ 3 times), eluted with 100 mM formic acid, transferred to tubes, dried in SpeedVac.
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