* Please be kindly noted that our services and products can only be used for research to organizations or companies and not intended for any clinical or individuals.
The goal of Proteolysis Targeting Chimeric (PROTAC) technology is to degrade the target protein, so in some related studies, the degradation ability of the target proteins needs to be measured. With many years of technical experience and professional technical team, BOC Sciences has established an advanced one-stop PROTAC service platform to provide multiple technical services related to PROTAC technology, including degradation ability assay. Our rich experience and professional technical capabilities can help customers achieve degradation analysis of target proteins in a shorter period.
PROTAC technology is a potential technology in the field of drug design. PROTAC compounds have two specific ligands that can interact with E3 ubiquitin ligase and recruit the target proteins. It can trigger ubiquitination of the target protein through the ubiquitin proteasomal system (UPS), and finally induce the protein of interest to be targeted for degradation by proteasome. Therefore, degradation ability analysis of PROTAC technology can be carried out by measuring the degradation rate of the target protein directly, or by analyzing the ubiquitination of the target protein. Various parameters in the development process of PROTAC technology will ultimately affect the degradation efficiency of the target protein, such as the stability of the PROTAC compound. Therefore, the study of protein degradation ability is also an important field in the research of PROTAC technology. Analysis of degradation ability can help researchers to analyze the potency of PROTAC in promoting the degradation of targeted proteins in detail, and is conducive to the development and optimization of PROTAC technology.
Our Services for Degradation Ability Assay (include but not limited to the following):
- TR-FRET In-Vitro Ubiquitylation Assay
Time-Resolved Fluorescence Resonance Energy Transfer (TR-FRET) is a technology that can realize single ubiquitination or multiple ubiquitination assays through the detection of fluorophores, which is beneficial to the analysis and evaluation of the degradation ability of PROTAC technology. BOC Sciences has a first-class TR-FRET technology platform and a professional technical team to provide customers with high-quality technical support services for PROTAC technology-related researches.
- ELISA-Based In-Vitro Ubiquitylation Assay
In PROTAC technology, ubiquitin-tagged target proteins can be specifically recognized and degraded by the proteasome. Enzyme-Linked Immunosorbent Assay (ELISA) technology can utilize anti-ubiquitin antibodies to specifically identify this type of ubiquitin-tagged protein, and detect the level of ubiquitinated protein to help analyze and evaluate the degradation ability of PROTAC technology. Our ELISA-based in-vitro ubiquitylation assay service platform includes sandwich ELISA and competitive ELISA.
- Degradation rate measurement and half-life analysis
The degradation rate and half-life are not only related to the protein sequence, conformational location and cell state, but also affected by the degradation pathway. The degradation rate is related to the level of ubiquitination and the stability of the PROTAC ternary compound, thus the degradation rate can reflect the potency of PROTAC to a certain extent. Moreover, the UPS-mediated degradation pathway also has an impact on half-life. Therefore, the measurement and analysis of the degradation rate and half-life between different PROTAC systems can help to evaluate and further optimize PROTAC functions.
- Multiple technology platforms (TR-FRET, ELISA, mass spectrometry, etc)
- Experienced experts team
- Provide professional analysis report
- Strictly standardized experimental operating procedures
- Highly reliable and reproducible results
Workflow of Degradation Ability Assay
- Eldeeb, M. A.; et al. A molecular toolbox for studying protein degradation in mammalian cells. Journal of neurochemistry. 2019, 151(4): 520-533.