I have read the following article, but was not successful in extracting the protein.
Article Mass Spectrometry of Whole Proteins Eluted from Sodium Dodec...
One possibility would be electroelution using GPR-800 (https://proteabio.com/products/GPR-800).
Could you indicate which is your intended downstream application after elution of the protein from the gel?
Additionally, some information about your protein (size, isoelectric point etc.) may help to better address your question.
I know, that there are protocols for preparing gels, which can be resolved after the electrophoresis, but unfortunately I have no literatur on that.
Do visit SERVA ELECTROPHORESIS. They offer different kits and products that might be compatible to what your are looking for. Best of luck!
For successful extraction of intact proteins from SDS-PAGE gels, protein bands should not be fixed, as crosslinking them with formaldehyde will trap proteins in gels, and will lead to a poor extraction efficiency.
An easy way is to run proteins in parallel lanes. Cut out and separate 2 lanes. Fix and stain one lane. Cut band from the second lane by comparing against the first lane. Electroelute or extract from the cut lband.
Alternatively, after running a gel, and prior to staining hte gel, perfom electrotransfer to a PVDF membrane. You may then stain the PVDF membrane, and cut out the protein band of interest. You may elute or extract this cut band.
where did your protein come from? animal, cells, or plant? because the resources of the protein usually effact the SDS -PAGE gel too. Just make sure the protein is pure before subject to SDS-gel
Thank you for the suggestions. Yongmei, the proteins are expressed in E. coli and are usually pure. In this case the protein is displaying two bands in SDS-PAGE however the smaller MW band is not showing in mass spec.
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