Strategy for Development of Site-Specific Ubiquitin Antibodies

Frontiers in Chemistry
Ila van KruijsbergenFred van Leeuwen

Abstract

Protein ubiquitination is a key post-translational modification regulating a wide range of biological processes. Ubiquitination involves the covalent attachment of the small protein ubiquitin to a lysine of a protein substrate. In addition to its well-established role in protein degradation, protein ubiquitination plays a role in protein-protein interactions, DNA repair, transcriptional regulation, and other cellular functions. Understanding the mechanisms and functional relevance of ubiquitin as a signaling system requires the generation of antibodies or alternative reagents that specifically detect ubiquitin in a site-specific manner. However, in contrast to other post-translational modifications such as acetylation, phosphorylation, and methylation, the instability and size of ubiquitin-76 amino acids-complicate the preparation of suitable antigens and the generation antibodies detecting such site-specific modifications. As a result, the field of ubiquitin research has limited access to specific antibodies. This severely hampers progress in understanding the regulation and function of site-specific ubiquitination in many areas of biology, specifically in epigenetics and cancer. Therefore, there is a high demand for antibodie...Continue Reading

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Citations

Feb 12, 2021·The Journal of Cell Biology·Carolina Dos Santos PassosRobert E Cohen

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Methods Mentioned

BETA
ubiquitination
immunoprecipitation
ELISA
Surface Plasmon Resonance
FCS
affinity purification

Software Mentioned

Waters Mass Lynx Mass Spectrometry

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