Ubiquitin, ubiquitin chains, and their derivatives are indispensable molecular tools for studying the structure and function of proteins ubiquitylation. In order to overcome the barriers that such molecules are difficult to synthesize, our company has developed a series of Ubiquitin-related products with high purity, homogeneity, and definite structure on the basis of proteins chemical synthesis technology, ranging from μg to g grade with 70% to 99% purity. They can be used in basic research and peptide drug discovery, which help you with drugs screening and related scientific research experiments.
The ubiquitination modification involves a series of reactions of ubiquitin-activating enzyme E1, ubiquitin-conjugating enzyme E2, and ubiquitin ligase E3:
First, the enzyme E1 (protein number 1r4n) adheres to the Cys residue in the tail of the ubiquitin molecule to activate ubiquitin under the condition of ATP energy supply, and then, E1 transfers the activated ubiquitin molecule to the E2 enzyme (protein number 1fxt) , and then, E2 enzymes and some different kinds of E3 enzymes jointly recognize the target protein and carry out ubiquitination modification on it. According to the relative ratio of E3 to the target protein, the target protein can be monoubiquitinated and modified by polyubiquitination. The E3 enzymes (protein numbers 1ldk and 1fqv) are shaped like a clip, and the target protein is attached in the gap in the middle. The left domain of the enzyme determines the specific recognition of the target protein, and the right domain positions the E2 enzyme to transfer ubiquitin molecules. The result of protein ubiquitination is that the labeled protein is broken down by proteases into smaller polypeptides, amino acids, and ubiquitins that can be reused.
Ubiquitination plays an important role in protein localization, metabolism, function, regulation and degradation. At the same time, it is also involved in the regulation of almost all life activities such as cell cycle, proliferation, apoptosis, differentiation, metastasis, gene expression, transcriptional regulation, signal transmission, damage repair, inflammation and immunity. Ubiquitination is closely related to the pathogenesis of tumors, cardiovascular and other diseases. Therefore, as a major achievement of biochemical research in recent years, it has become a new target for research and development of new drugs.
Ubiquitin is a highly conserved protein widely found in nuclear cells. It cooperates with ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2), and ubiquitin ligase (E3) to achieve ubiquitination and modification of specific proteins, and finally achieves the removal of aging, damaged and misfolded proteins, and is conducive to maintaining The normal physiological function of cells plays a very important role. In addition, some ubiquitination reactions can also achieve functional regulation independent of protein degradation.
Ubiquitin chains of different lengths and types can be applied to biochemical functions such as interaction and enzyme activity as well as structural biology study of crystals, electron microscopes, and Nuclear Magnetic Resonance.
Ubiquitin-derived cross-linking probes can be used to detect unknown interacting proteins from normal or diseased cells and new targets for disease treatment.
Ubiquitin-derived fluorescent probes can be used to analyze the activity and specificity of deubiquitinase and high throughput screening of deubiquitinase inhibitors.
Types of Ubiquitination
DNA repair, endocytosis, histone regulation, virus budding, proteasomal and lysosome degradation
Cell signaling/kinase activation and cytokine signaling, DNA damage response, endocytosis
Lysosomal degradation, Wnt signaling
The physiological function is not yet clear
Cell Cycle/Proteasomal degradation, ERAD, cell signaling such as TNF and Wnt signaling
The physiological function is not yet clear; however, it has been suggested to inhibit proteasomal degradation and involvement in DNA damage repair
Regulation of NF-κB signaling in inflammation, protein degradation
Endocytosis, proteasomal and lysosomal degradation
MHC endocytosis (K11/K63), kinase activation (K33/K29)
The advantages of pseudo-isopeptide bond products are as follows:
Low cost and high purity
Does not affect the recognition of substrate by ubiquitin recognition enzymes
Can be cleaved by the deubiquitinase
We offer the following products:
Multi-ubiquitin Chain Products Linked by Pseudoisopeptide Bonds
Ubiquitins Modified Histones Linked by Pseudoisopeptide Bonds