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35s methione and cysteine

Manufactured by Promega

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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2 protocols using 35s methione and cysteine

1

Recombinant Protein Interaction Analysis

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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.
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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.
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