OTUB1 Antibody

Ubiquitin Aldehyde Binding 1 (OTUB1) is a protein encoded by the OTUB1 gene. It belongs to the OTU (ovarian tumor) superfamily of predicted cysteine proteases. OTUB1 is a highly specific ubiquitin iso-peptidase, which means it can cleave ubiquitin from branched poly-ubiquitin chains but not from ubiquitinated substrates .

OTUB1 is known for its role in deubiquitination, a process that removes ubiquitin from proteins. This action is crucial for regulating protein turnover by preventing degradation. OTUB1 specifically removes ‘Lys-48’-linked conjugated ubiquitin from proteins . This regulatory role is essential in various cellular processes, including protein degradation, signal transduction, and DNA repair.

OTUB1 functions by binding to free ubiquitin, which acts as an allosteric regulator. This binding increases OTUB1’s affinity for the ubiquitin-conjugating enzyme UBE2N/UBC13 and disrupts its interaction with UBE2V1 . The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved ‘Lys48’-linked di-ubiquitin chain .

OTUB1 plays a significant role in the immune system by regulating T-cell anergy. T-cell anergy is a state where T-cells become unresponsive to antigen rechallenge and no longer respond to their cognate antigen. OTUB1 achieves this through its interaction with RNF128/GRAIL, a crucial inducer of CD4 T-cell anergy .

OTUB1 has been associated with various diseases, including diabetic retinopathy and microvascular complications of diabetes . Its role in deubiquitination pathways makes it a potential target for therapeutic interventions in diseases where protein degradation and turnover are disrupted.

The mouse anti-human OTUB1 antibody is a monoclonal antibody that targets the OTUB1 protein. It is used in various research applications, including Western blotting, immunohistochemistry, and immunofluorescence . This antibody helps in studying the expression and localization of OTUB1 in different tissues and cell lines.