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35s methione and cysteine

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35S-methionine and cysteine is a radioactive labeling reagent used in protein synthesis studies. It provides a means to incorporate radioactive sulfur atoms into newly synthesized proteins, allowing researchers to track and analyze protein production and turnover.

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Lab products found in correlation

Ni nta, by Qiagen (2 mentions)

2 protocols using 35s methione and cysteine

1

Recombinant Protein Interaction Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
GST-tagged recombinant proteins were purified using glutathione sepharose following the manufacture’s protocol (GE healthcare). Coupled in vitro transcription and translation reactions were used to generate SMN and delta-Tudor SMN proteins with 35S-methione and cysteine (Promega). Purified GST and GST-FUS (500 ng) were incubated with SMN and delta-Tudor SMN together with 20 μl of glutathione-sepharose at 4°C for 1 hour. The beads were subsequently washed three times with wash buffer (50 mM HEPES, pH 7.5, 150 mM KCl, 1 mM MgCl2, 0.1% NP-40, 10% glycerol). The associated proteins were eluted with 15 mM glutathione and analyzed with autoradiography. 6xHis-tag recombinant proteins were expressed in bacteria and purified with Ni-NTA (Qiagen) according the manufacturer’s manual. In vitro GST-pull-down assay using GST, GST-FUS, and GST-TDP-43 with equal amount of recombinant SMN proteins performed as described above. The associated proteins were eluted with 15 mM glutathione and analyzed with immunoblots.
Sun S., Ling S.C., Qiu J., Albuquerque C.P., Zhou Y., Tokunaga S., Li H., Qiu H., Bui A., Yeo G.W., Huang E.J., Eggan K., Zhou H., Fu X.D., Lagier-Tourenne C, & Cleveland D.W. (2015). ALS-causative mutations in FUS/TLS confer gain- and loss-of-function by altered association with SMN and U1-snRNP. Nature communications, 6, 6171.
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2

Recombinant Protein Interaction Analysis

Check if the same lab product or an alternative is used in the 5 most similar protocols
GST-tagged recombinant proteins were purified using glutathione sepharose following the manufacture’s protocol (GE healthcare). Coupled in vitro transcription and translation reactions were used to generate SMN and delta-Tudor SMN proteins with 35S-methione and cysteine (Promega). Purified GST and GST-FUS (500 ng) were incubated with SMN and delta-Tudor SMN together with 20 μl of glutathione-sepharose at 4°C for 1 hour. The beads were subsequently washed three times with wash buffer (50 mM HEPES, pH 7.5, 150 mM KCl, 1 mM MgCl2, 0.1% NP-40, 10% glycerol). The associated proteins were eluted with 15 mM glutathione and analyzed with autoradiography. 6xHis-tag recombinant proteins were expressed in bacteria and purified with Ni-NTA (Qiagen) according the manufacturer’s manual. In vitro GST-pull-down assay using GST, GST-FUS, and GST-TDP-43 with equal amount of recombinant SMN proteins performed as described above. The associated proteins were eluted with 15 mM glutathione and analyzed with immunoblots.
Sun S., Ling S.C., Qiu J., Albuquerque C.P., Zhou Y., Tokunaga S., Li H., Qiu H., Bui A., Yeo G.W., Huang E.J., Eggan K., Zhou H., Fu X.D., Lagier-Tourenne C, & Cleveland D.W. (2015). ALS-causative mutations in FUS/TLS confer gain- and loss-of-function by altered association with SMN and U1-snRNP. Nature communications, 6, 6171.
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