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- W2016069484 endingPage "20202" @default.
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- W2016069484 abstract "Modification of proteins by the addition of lysine (K)-63-linked polyubiquitin (polyUb) chains is suggested to play important roles in a variety of cellular events, including DNA repair, signal transduction, and receptor endocytosis. However, identifying such modifications in living cells is complex and cumbersome. We have generated a monoclonal antibody (mAb) that specifically recognizes K63-linked polyUb, but not any other isopeptide-linked (K6, K11, K27, K29, K33, or K48) polyUb or monoubiquitin. We demonstrate the sensitivity and specificity of this K63Ub-specific mAb to detect K63Ub-modified proteins in cell lysates by Western blotting and in cells by immunofluorescence, and K63Ub-modified TRAF6 and MEKK1 in vitro and ex vivo. This unique mAb will facilitate the analysis of K63-linked polyubiquitylation ex vivo and presents a strategy for the generation of similar reagents against other forms of polyUb." @default.
- W2016069484 created "2016-06-24" @default.
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- W2016069484 date "2008-12-23" @default.
- W2016069484 modified "2023-09-25" @default.
- W2016069484 title "Analysis of nondegradative protein ubiquitylation with a monoclonal antibody specific for lysine-63-linked polyubiquitin" @default.
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- W2016069484 doi "https://doi.org/10.1073/pnas.0810461105" @default.
- W2016069484 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2629300" @default.
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