Recombinant OTUB1 protein (His tag)

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Recombinant Human Ubiquitin Thioesterase OTUB1 (EC 3.4.19.12) Fragment (residues 2-271) is a high-purity protein designed for studying deubiquitinating enzyme activity and regulatory functions. This fragment fully encompasses the OTU domain, making it an ideal tool for investigating Lys-48-linked ubiquitin chain removal and non-catalytic roles in DNA repair and mTOR signaling pathways.

OTUB1 is a crucial deubiquitinating enzyme in Homo sapiens that specifically hydrolyzes Lys-48-linked conjugated ubiquitin from proteins, thereby preventing protein degradation and regulating protein turnover. It plays significant roles in T-cell anergy regulation through its interaction with RNF128/GRAIL and deubiquitinates estrogen receptor alpha (ESR1). Beyond its catalytic function, OTUB1 has important non-catalytic roles in DNA repair by inhibiting RNF168 activity through binding to UBE2N/UBC13, limiting Lys-63-linked histone modifications at DNA damage sites. Additionally, it regulates mTORC1 and mTORC2 complexes through phosphorylation-dependent mechanisms, influencing RPTOR and DEPTOR ubiquitination states. The protein is primarily localized in the cytoplasm, where it executes these diverse regulatory functions in cellular homeostasis and stress response pathways.