Abnormal functions of the ubiquitin-proteasome system (UPS) affect a number of cellular processes, including cell cycle regulation, cell growth, proliferation, apoptosis, DNA repair, and other cellular signalling pathways. This dysregulation is considered a key factor in the development of malignant tumours, cardiovascular diseases, neurodegenerative disorders, and other diseases. As a result, the UPS has emerged as an important therapeutic target for the treatment of related conditions. Inhibiting the ubiquitin-proteasome system to regulate the degradation of specific substrate proteins represents a key strategy in modern drug development. Current research on small molecule inhibitors targeting the UPS focuses on four main areas: ubiquitin-activating enzyme E1 inhibitors, ubiquitin-conjugating enzyme E2 inhibitors, ubiquitin ligase E3 inhibitors, and proteasome inhibitors. To support these investigations, researchers frequently utilize the in vitro ubiquitination assay, a powerful tool that enables precise monitoring and analysis of ubiquitination events under controlled laboratory conditions.
1.Support for In Vitro Ubiquitination Assays
Our recombinant ubiquitin, E1, E2, and E3 ligase proteins provide essential components for reconstituting in vitro ubiquitination assay systems. Researchers can precisely monitor ubiquitin chain formation, enzyme activity, and substrate modification under controlled conditions, enabling mechanistic studies and drug screening.
2.Tools for In Vivo Ubiquitination Analysis
Understanding ubiquitination in cellular contexts requires reliable reagents. Our purified proteins can be used as positive controls, immunoprecipitation probes, or standard references in in vivo ubiquitination assay workflows, helping validate findings from cell-based models.
3.Compatible with Ubiquitin Detection Methods
Whether performing ubiquitin assay by western blot, or developing ubiquitin ELISA for quantification, our high-purity ubiquitin and conjugation machinery proteins serve as ideal standards and controls, ensuring accurate and reproducible results.
4.Critical Components for E3 Ligase and Protease Studies
With growing interest in E3 ubiquitin ligase targeting for drug discovery, including PROTAC development, our recombinant E3 ligases support binding assays and activity screening. Additionally, our deubiquitinating enzymes (DUBs) enable protease inhibition assay development for studying ubiquitin-specific proteases.
A strict QC (quality control) test report is provided for each batch.
Each batch has been verified for enzyme activity.
Verified by common homogeneous methods such as TR-FRET, Luminescence and fluorescence.
High-performance at competitive prices.
For KeyTec® protein products, each batch of protein is subjected to a series of rigorous validation procedures to obtain data such as purity, monomer/polymer morphology, enzyme activity information, positive compound validation information, and so forth.
We provide a comprehensive panel of highly active recombinant deubiquitinating enzymes, including USP2, USP4, USP7, USP8, USP11, USP14, USP36, and the USP1/UAF1 complex. These Ubiquitin-specific proteases are rigorously validated for activity (e.g., by fluorescence intensity assays) and serve as ideal tools for studying deubiquitinating enzymes function, screening specific inhibitors, and elucidating substrate recognition mechanisms. Each batch is supplied with detailed QC data to ensure reliable and reproducible results.
Our E3 ubiquitin ligase complexes, such as DDB1/CRBN and VHL/Elongin-C/Elongin-B, exhibit high purity (SDS-PAGE ≥95%) and activity validated by TR-FRET or SPR. They are valuable for investigating substrate recognition, key steps of ubiquitination, and serve as core components in PROTAC development to assess the efficiency and specificity of targeted protein degradation.
We offer a full set of ubiquitinase-related proteins, from E1 activating enzyme (UBE1) to E3 ligases. These highly active components enable researchers to reconstitute complete ubiquitination reactions in vitro, facilitating in-depth studies of enzyme kinetics, ubiquitin chain assembly mechanisms, and the modulatory effects of compounds on the ubiquitination process—powering both drug discovery and basic research.
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