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Tris carboxyethyl phosphine

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Tris-carboxyethyl phosphine is a reducing agent commonly used in biochemical and cell biology applications. It is a water-soluble, odorless, and non-toxic compound that can be used to maintain a reducing environment for proteins and other biomolecules.

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Lab products found in correlation

Ultimate 3000 rslcnano hplc system, by Thermo Fisher Scientific (2 mentions) Orbitrap elite mass spectrometer, by Thermo Fisher Scientific (2 mentions) Endoproteinase gluc, by New England Biolabs (2 mentions) Glu c, by Roche (2 mentions) Endoproteinase asp n, by Roche (2 mentions)

2 protocols using tris carboxyethyl phosphine

1

Cross-Linking and Mass Spectrometry of Yfh1-Isu1 Complex

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These studies were carried out using procedures described previously.16 (link),17 (link) Briefly, [Yfh1]24·[Isu1LMW]24 complex (1 mL containing 4 mg total protein) was incubated with the cross-linker bis[sulfosuccinimidyl] suberate (BS3) (Thermo Scientific),88 (link),89 (link) at a protein/BS3 molar ratio of 1 : 100, and cross-linked protein was re-isolated via Sephacryl S300 size-exclusion chromatography and analyzed by SDS-PAGE. One preparation of cross-linked complex was incubated with endoproteinase GluC (New England BioLabs), and a second preparation was digested with both GluC and endoproteinase AspN (Roche/Sigma-Aldrich) and further treated with the reducing agent, tris-carboxyethyl phosphine (50 mM final concentration) (Hampton Research). Cross-linked peptides in each sample were identified at the Mayo Clinic Proteomics Core by nano-flow liquid chromatography electrospray tandem mass spectrometry (MS/MS) using an Orbitrap Elite mass spectrometer (Thermo Fisher Scientific) coupled to a Thermo Ultimate 3000 RSLCnano HPLC system as described previously.16 (link)
Galeano B.K., Ranatunga W., Gakh O., Smith DY I.V., Thompson J.R, & Isaya G. (2017). Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe–S cluster assembly centers †Electronic supplementary information (ESI) available: Fig. S1–S14; Tables S1 and S2. See DOI: 10.1039/c7mt00089h. Metallomics, 9(6), 773-801.
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2

Cross-linking analysis of Yfh1-Isu1 complex

Check if the same lab product or an alternative is used in the 5 most similar protocols
These studies were carried out using procedures described previously.16 (link), 17 (link) Briefly, [Yfh1]24•[Isu1LMW]24 complex (1 mL containing 4 mg total protein) was incubated with the cross-linker bis[sulfosuccinimidyl] suberate (BS3) (Thermo Scientific),88 (link), 89 (link) at a protein/BS3 molar ratio of 1:100, and cross-linked protein was re-isolated via Sephacryl S300 size-exclusion chromatography and analyzed by SDS-PAGE. One preparation of cross-linked complex was incubated with endoproteinase GluC (New England BioLabs), and a second preparation was digested with both GluC and endoproteinase AspN (Roche/Sigma-Aldrich) and further treated with the reducing agent, tris-carboxyethyl phosphine (50 mM final concentration) (Hampton Research). Cross-linked peptides in each sample were identified at the Mayo Clinic Proteomics Core by nano-flow liquid chromatography electrospray tandem mass spectrometry (MS/MS) using an Orbitrap Elite mass spectrometer (Thermo Fisher Scientific) coupled to a Thermo Ultimate 3000 RSLCnano HPLC system as described previously.16 (link)
Galeano B.K., Ranatunga W., Gakh O., Smith DY I.V., Thompson J.R, & Isaya G. (2017). Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe–S cluster assembly centers †Electronic supplementary information (ESI) available: Fig. S1–S14; Tables S1 and S2. See DOI: 10.1039/c7mt00089h. Metallomics, 9(6), 773-801.
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