E3 Ubiquitin Ligase Activity Assay


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As a professional technical service company in the field of Proteolysis Targeting Chimeric (PROTAC) technology, BOC Sciences provides a number of research and development outsourcing services. E3 ubiquitin ligase is an important enzyme related to PROTAC technology. We provide technical services for E3 ubiquitin ligase activity assay, and pursue higher service efficiency and more competitive service costs on the premise of ensuring the quality of service, thereby helping customers shorten the research cycle and reduce research costs.

Introduction

E3 ubiquitin ligase is an enzyme that specifically binds to PROTAC, and is also one of the special enzymes that play a key role in ubiquitination. E3 ubiquitin ligase plays an important role in the specific recognition of target protein and the efficiency regulation of ubiquitination reaction. The human genome encodes more than 600 E3 ubiquitin ligases, but only a portion can be recruited to degrade the protein of interest (POI), such as von Hippel-Lindau (VHL), cereblon (CRBN), inhibitors of apoptosis (IAPs), and mouse double minute 2 homologue (MDM2). E3 ubiquitin ligase activity affects the ubiquitination process and thus the degradation of the target protein. Therefore, E3 ubiquitin ligase activity assay is of great significance in the research related to PROTAC technology. The detection of E3 ubiquitin ligase activity often utilizes its auto-ubiquitination ability, because auto-ubiquitination is a characteristic that exists in almost all E3 ubiquitin ligase.

E3 Ubiquitin Ligase Activity Assay

Service for E3 Ubiquitin Ligase Activity Assay (include but not limited to the following):

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Workflow of E3 Ubiquitin Ligase Activity Assay

E3 Ubiquitin Ligase Activity Assay

References:

  1. Zheng, N.; Shabek, N. Ubiquitin ligases: structure, function, and regulation. Annual Review of Biochemistry. 2017, 86(1): 129-157.
  2. Sun, X.Y.; et al. PROTACs: great opportunities for academia and industry. Signal Transduction and Targeted Therapy. 2019, 4: 64.
  3. Marblestone, J.G.; et al. Analysis of ubiquitin E3 ligase activity using selective polyubiquitin binding proteins. Biochimica Et Biophysica Acta, 2012, 1823(11): 2094-2097.

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