OTUD6A Protein, Human

The OTUD5 protein is a deubiquitinating enzyme with complex regulatory functions that acts as a negative regulator in the innate immune system. It exhibits peptidase activity against "Lys-48" and "Lys-63" linked polyubiquitin chains, and in vitro, it can cleave "Lys-11" linked ubiquitin chains. OTUD6A Protein, Human is the recombinant human-derived OTUD6A protein, expressed by E. coli , with tag free.

OTUD6A is a deubiquitinating enzyme known for its ability to hydrolyze various types of polyubiquitin chains. Specifically, OTUD6A exhibits deubiquitinating activity towards 'Lys-27', 'Lys-29', 'Lys-33', and 'Lys-11'-linked polyubiquitin chains. This enzymatic function involves the cleavage of ubiquitin molecules from substrate proteins, contributing to the regulation of protein degradation and cellular signaling pathways. As a member of the ovarian tumor domain-containing family of deubiquitinases, OTUD6A plays a role in modulating ubiquitin-dependent processes, providing a fine-tuning mechanism for cellular protein homeostasis and signaling.

Human

E. coli

Tag Free

Q7L8S5 (M1-L288)

139562

Full Length

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

<1 EU/μg, determined by LAL method.