was supplemented with CaCl
2 to a final
concentration of 6 mM, then digested at room temperature with a catalytic ratio
of thrombin: CBP-FLAG-JNK. To evaluate the extent of digestion over time, the
reaction was terminated at various time points (0, 1, and 18 hours). The degree
of digestion by thrombin was evaluated by performing SDS-PAGE. 20 l of each
time point sample was boiled, then electrophoresed on a 12% Tris-glycine
acrylamide gel, and then stained with Coomassie Blue (not shown).
To confirm recognition of FLAG-JNK by anti-FLAG M2 antibody, western
blot analysis was performed on the thrombin digest time points. 10-l
(~1 g) of sample was subjected to SDS-PAGE, as described above. Samples
were electroblotted onto a nitrocellulose filter and detected with anti-FLAG
M2 antibody using standard procedures (Figure
4).
Immunoaffinity Pull-Down of c-Jun with FLAG-JNK
It has been shown that transcriptional activity of c-Jun is greatly enhanced
in response to phosphorylation.7 JNK binds to the c-Jun
transactivation domain and phosphorylates Ser-63, Ser-73, and some secondary
sites. To demonstrate the utility of a FLAG-fusion protein with the CBP tag
removed, we performed an immunoaffinity pull-down of c-Jun from HeLa cell
nuclear extract with immobilized FLAG-JNK.
JNK gel was prepared by immobilizing FLAG-JNK on anti-FLAG M2 affinity
gel. JNK gel was equilibrated in binding buffer and subsequently incubated
with HeLa extract. The affinity gel was pelleted by low-speed centrifugation
and washed extensively with binding buffer. The washed gel pellet was
boiled in sample buffer then subjected to SDS-PAGE. Duplicate gels were
performed. One gel was stained with Coomassie Blue protein stain, the
other gel was electroblotte
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Page: All 1 2 3 4 5 6 7 8 Related biology technology :1.
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