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    Glossary Dithiothreitol

    chemical reducing agent that breaks disulfide bonds in proteins

    Dithiothreitol (DTT) is a chemical compound used in biochemistry and molecular biology to break disulfide bonds in proteins, which helps to denature them and maintain their reduced state. This is particularly useful in experiments where maintaining the protein's structure is crucial, such as in electrophoresis or protein folding studies.

    Research 6 of 286

    1. Characterisation of low abundance wool proteins through novel differential extraction techniques Electrophoresis · 2010 · 26 citations
    2. Cross-linked features of mouse pelage hair resistant to detergent extraction ˜The œanatomical record · 1999 · 15 citations
    3. Reductive Stress Selectively Disrupts Collagen Homeostasis and Modifies Growth Factor-independent Signaling Through the MAPK/Akt Pathway in Human Dermal Fibroblasts Molecular & cellular proteomics · 2019 · 9 citations
    4. Improved two‐dimensional electrophoretic mapping of Japanese human hair proteins; application to curved and straight Japanese human hairs; and protein identification by MALDI MS and MS/MS quadrupole time‐of‐flight mass spectrometry International Journal of Cosmetic Science · 2020
    5. Cross‐linked features of mouse pelage hair resistant to detergent extraction ˜The œanatomical record · 1999
    6. Inheritance of Some Electrophoretic Phenotypes of Human Hair Advances in forensic haemogenetics · 1990
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