OTUD5 Protein, Human (His, FLAG)

The OTUD5 protein is a deubiquitinating enzyme that crucially eliminates the innate immune response through peptidase activity on "Lys-48" and "Lys-63" linked polyubiquitin chains, thereby inhibiting TRAF3-mediated Type I interferon production. It acts as a regulator of neuroectodermal differentiation by cleaving “Lys-48” linked ubiquitin chains to prevent the degradation of chromatin regulators such as ARID1A, HDAC2 and HCF1. OTUD5 Protein, Human (His, FLAG) is the recombinant human-derived OTUD5 protein, expressed by E. coli , with N-6*His, N-Flag labeled tag. The total length of OTUD5 Protein, Human (His, FLAG) is 180 a.a., .

OTUD5 Protein, a deubiquitinating enzyme, plays a crucial role as a negative regulator of the innate immune system, exhibiting peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, and the ability to cleave 'Lys-11'-linked ubiquitin chains in vitro. It exerts its influence through TRAF3 deubiquitination, subsequently suppressing type I interferon (IFN) production. Additionally, OTUD5 serves as a key controller of neuroectodermal differentiation, counteracting the degradation of essential chromatin regulators like ARID1A, HDAC2, and HCF1 by cleaving 'Lys-48'-linked ubiquitin chains. Furthermore, following phosphorylation by MTOR, OTUD5 acts as a positive regulator of mTORC1 and mTORC2 signaling, mediating the deubiquitination of BTRC and enhancing its stability. This multifaceted role underscores the significance of OTUD5 in modulating diverse cellular processes, highlighting its pivotal contributions to immune regulation, cellular differentiation, and signaling pathways.

Human

E. coli

N-6*His;N-Flag

Q96G74 (G172-G351)

55593

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.