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Dithriothreitol

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Dithriothreitol (DTT) is a reducing agent commonly used in biochemical and molecular biology applications. It functions by maintaining the reduced state of sulfhydryl groups in proteins and other biomolecules.

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Lab products found in correlation

C18 column, by Merck Group (2 mentions) Iodoacetamide, by Merck Group (2 mentions) Trypsin, by Promega (2 mentions)

2 protocols using dithriothreitol

1

Protein Reduction, Alkylation, and Trypsin Digestion

Check if the same lab product or an alternative is used in the 5 most similar protocols
The protein lysate was reduced with 45 mM dithriothreitol (Sigma
Aldrich, MO), alkylated with 100 mM iodoacetamide (Sigma Aldrich, MO), and
subsequently digested with modified sequencing grade Trypsin (Promega,
Madison, WI) at 30°C overnight. The digest was then acidified using
0.1% TFA and the peptides were desalted using solid phase extraction C18
column (Supelco, Bellefonte, PA), and vacuum dried in a centrifugal
evaporator.
Roper N., Gao S., Maity T.K., Banday A.R., Zhang X., Venugopalan A., Cultraro C.M., Patidar R., Sindiri S., Brown A.L., Goncearenco A., Panchenko A.R., Biswas R., Thomas A., Rajan A., Carter C.A., Kleiner D.E., Hewitt S.M., Khan J., Prokunina-Olsson L, & Guha U. (2019). APOBEC Mutagenesis and Copy-Number Alterations Are Drivers of Proteogenomic Tumor Evolution and Heterogeneity in Metastatic Thoracic Tumors. Cell reports, 26(10), 2651-2666.e6.
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2

Protein Reduction, Alkylation, and Trypsin Digestion

Check if the same lab product or an alternative is used in the 5 most similar protocols
The protein lysate was reduced with 45 mM dithriothreitol (Sigma
Aldrich, MO), alkylated with 100 mM iodoacetamide (Sigma Aldrich, MO), and
subsequently digested with modified sequencing grade Trypsin (Promega,
Madison, WI) at 30°C overnight. The digest was then acidified using
0.1% TFA and the peptides were desalted using solid phase extraction C18
column (Supelco, Bellefonte, PA), and vacuum dried in a centrifugal
evaporator.
Roper N., Gao S., Maity T.K., Banday A.R., Zhang X., Venugopalan A., Cultraro C.M., Patidar R., Sindiri S., Brown A.L., Goncearenco A., Panchenko A.R., Biswas R., Thomas A., Rajan A., Carter C.A., Kleiner D.E., Hewitt S.M., Khan J., Prokunina-Olsson L, & Guha U. (2019). APOBEC Mutagenesis and Copy-Number Alterations Are Drivers of Proteogenomic Tumor Evolution and Heterogeneity in Metastatic Thoracic Tumors. Cell reports, 26(10), 2651-2666.e6.
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