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How it works:
The protein of interest fused to the SNAP-tag contained in cell lysate is rapidly labeled with a fluorophore or biotin prior to running it on an SDS-PAGE gel. After running the gel, the fluorescently labeled tagged protein is visualized by simply placing the gel on a UV transilluminator or in a fluorescent gel scanner. If the protein was biotinylated, it is detected after blotting using standard streptavidin conjugated detection reagents.
Advantages:
- Specific labeling eliminates need for antibodies.
- Very rapid protocol.
- Sensitivity with fluorophore and gel scanner similar to Western blot.
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| Expression of SNAP-cyclophilin A in E.coli strain BL21 A after arabinose induction. Direct visualization of labeled SNAP-tag fusion proteins in SDS-PAGE gel using a standard UV transilluminator. |
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