protein cellular localization

Protein ubiquitination is an enzymatic post-translational modification in which an ubiquitin protein is attached to a substrate protein. Ubiquitination involves three main steps: activation, conjugation, and ligation, performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s), respectively. Ubiquitination affects cellular processes such as apoptosis, cell cycle, DNA damage repair, and membrane transportation, etc. by regulating the degradation of proteins (via the proteasome and lysosome), altering the cellular localization of proteins, affecting proteins activity, and promoting or preventing protein-protein interactions. Deregulation of ubiquitin pathway leads to many diseases such as neurodegeneration, cancer, infection and immunity, etc.

MCE offers a unique collection of 360 small molecule modulators with biological activity used for ubiquitination research. Compounds in this library target the key enzymes in ubiquitin pathway. MCE Ubiquitination Compound Library is a useful tool for the research of ubiquitination regulation and the corresponding diseases.

A protease (also called a peptidase, proteinase, or proteolytic enzyme) is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. Proteases play important roles in regulating multiple biological processes in all living organisms, such as regulating the fate, localization, and activity of many proteins, modulating protein-protein interactions, creating new bioactive molecules, contributing to the processing of cellular information, and generating, transducing, and amplifying molecular signals.

Proteases are important targets in drug discovery. Some protease inhibitors are often used as anti-virus drugs and anti-cancer drugs. MCE offers a unique collection of 747 protease inhibitors. MCE Protease Inhibitor Library is critical for drug discovery and development.