When I need to assay the expresssion of a certain membrane-bound protein on cell surface, I usually perform Western blot of the membrane proteins extracted by detergents such as NP40 or Brij, using a protein extraction kit like the Promega mem per plus membrane protein extraction kit. However, recently I learned from literatures that you can also perform cell surface biotinylation, lyse the cells, collect the biotin-bound proteins by streptavidin beads, and then subject the collected proteins to standard WB. I am just curious which approach (detergent extraction or cell surface biotinylation) would be more convienient and efficient to isolate cell surface protein? And what are the advabtages of each approach?
Depends on the purpose of your experiment: Surface labelling is a method you use when you need to distinguish between membrane protein that are actually accessible on the surface of the cells as opposed to proteins embedded in internal membranes, such as ER, Golgi, nuclear membrane ... It is also needed when you study the trafficking of membrane proteins in response to ligand stimulation: internalisation and recycling of receptors.
https://plueckthun.bioc.uzh.ch/wp-content/uploads/Publications/APpub0452.pdf
In this context, you try to distinguish between the population of membrane proteins actually on the surface vs. the same proteins localised in internal membrane compartments.
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