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The complex was run on a SDS denaturing gel.
Briefly, the equal amounts of sample were resolved on a SDS polyacrylamide gel and transferred to a polyvinylidene difluoride membrane.
Equal amounts of purified recombinant salivary proteins (100 ng), were electrophoresed on a SDS 12% polyacrylamide gel and transferred to nitrocellulose membranes.
The immunoprecipitated mixture or 20 µg total lysates were separated on a SDS polyacrylamide gel, and transferred to a polyvinylidene difluoride membrane (PVDF) (BioRad).
All three fractions were loaded on a SDS polyacrylamide gel and bands were identified MALDI-TOF.
Finally beads were boiled in 12 μl SDS sample buffer and the supernatant loaded on a SDS PAGE.
Similar(52)
After washing five times, the beads were boiled in SDS loading buffer and separated on a SDS-PAGE gel.
(C) Visualization of hENT1 on a SDS-PAGE gel.
The identity and purity of the expressed rCMEPX was analyzed on a SDS PAGE.
The samples were run on a SDS-PAGE gel and tryptically digested before analysis by HPLC MS-MS.
The remaining ZGs were lyzed and separated on a SDS-PAGE gel in triplicate lanes (80 μg proteins per lane).
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