Deubiquitylation involves the removal of ubiquitin molecules from target proteins. Ubiquitin is a small protein that can be covalently attached to other proteins, marking them for various fates, primarily degradation, but also regulation or localization within the cell. Deubiquitylation is the reverse process, catalysed by deubiquitylating enzymes (DUBs), which remove ubiquitin from target proteins. The human DUBs are classified into several families based on their structural and functional properties, including the ubiquitin-specific proteases (USPs), ubiquitin carboxyl-terminal hydrolases (UCHs), ovarian tumour proteases (OTUs), Machado-Joseph disease protein domain proteases (MJDs), and JAB1/MPN/MOV34 metalloenzymes (JAMMs), amongst others. Each family of DUBs may have multiple members, contributing to the overall diversity of DUBs in the human genome. USP14 (Ubiquitin-Specific Protease 14) for example is involved in regulating protein degradation via the proteasome. It associates with the proteasome and removes ubiquitin chains from protein substrates prior to degradation. By selectively deubiquitylating proteins, USP14 can delay or inhibit their proteasomal degradation. This process is important for maintaining protein homeostasis and controlling the turnover of specific proteins. USP1 (Ubiquitin-Specific Protease 1) is a DUB primarily involved in DNA repair and genome stability maintenance. It deubiquitylates and stabilizes proteins like FANCD2 and PCNA, involved in repairing DNA damage and preventing genomic instability. Deubiquitylation by USP1 therefore ensures the efficient completion of DNA repair processes. CYLD (Cylindromatosis) is a DUB that negatively regulates inflammatory signalling pathways. It deubiquitylates key components of the NF-κB signaling pathway, such as NEMO and TRAF2, leading to the inhibition of pro-inflammatory gene expression. Dysregulation of CYLD can result in chronic inflammation and autoimmune diseases. VMS1 (Valosin-Containing Protein/CDC48-Mediated Extractor 1) is a DUB involved in protein quality control processes. It interacts with the ATPase VCP/CDC48 and removes ubiquitin chains from misfolded or damaged proteins. This process is essential for targeting aberrant proteins for degradation and maintaining cellular proteostasis. A20 (TNFAIP3) is a multifunctional protein that acts as both an E3 ligase and a DUB. It regulates various cellular signalling pathways, including NF-κB and TNF signalling, by deubiquitylating specific substrates. A20's deubiquitylation activity is essential for dampening inflammatory responses and preventing excessive activation of these pathways. USP7 (Ubiquitin-Specific Protease 7) is a DUB that regulates the stability and activity of several cell cycle-related proteins, including p53 and Mdm2. By deubiquitylating p53, USP7 stabilizes this tumour suppressor protein, leading to cell cycle arrest and apoptosis in response to DNA damage. Conversely, it also deubiquitylates and stabilizes Mdm2, which targets p53 for degradation, allowing for controlled cell cycle regulation. AMSH (Associated Molecule with the SH3 Domain of STAM) is a DUB involved in endocytosis and protein trafficking. It participates in the removal of ubiquitin from proteins associated with the endosomal sorting complex required for transport (ESCRT), facilitating the sorting and trafficking of membrane proteins to their designated cellular compartments. Thus, deubiquitylation impacts a wide range of cellular pathways and functions, ensuring the proper functioning of proteins, maintaining cellular homeostasis, and playing regulatory roles in various physiological and pathological processes. We offer a wide product range of research reagents for studying deubiquitination, including TNFAIP3 antibodies, BAP1 antibodies, JAB1 antibodies, Ataxin 3 antibodies, and USP15 antibodies. Explore our full deubiquitination product range below and discover more, for less.