OTUD2 Protein, Human

OTUD2 is a key hydrolase in cellular processes that actively participates in endoplasmic reticulum-associated degradation (ERAD) by deubiquitinating misfolded luminal proteins. It trims ubiquitin chains from the substrate, helping them pass through the VCP/p97 pore. OTUD2 Protein, Human is the recombinant human-derived OTUD2 protein, expressed by E. coli , with tag free. The total length of OTUD2 Protein, Human is 347 a.a., .

OTUD2, a hydrolase with pivotal roles in cellular processes, is actively involved in endoplasmic reticulum-associated degradation (ERAD) by removing conjugated ubiquitin from misfolded lumenal proteins. It contributes to the ERAD mechanism by potentially trimming ubiquitin chains on associated substrates, facilitating their passage through the VCP/p97 pore. Specifically, OTUD2 exhibits deubiquitination activity towards 'Lys-27', 'Lys-29', and 'Lys-33'-linked polyubiquitin chains, as well as 'Lys-11'-linked ubiquitin chains. The ability to cleave both polyubiquitin and di-ubiquitin underscores its versatility. Beyond ERAD, OTUD2 may play a crucial role in macroautophagy, influencing the clearance of damaged lysosomes. Its involvement in autophagy includes recruiting PLAA, UBXN6, and VCP to damaged lysosome membranes adorned with K48-linked ubiquitin chains, facilitating their removal and promoting autophagosome formation. This multifaceted functionality highlights OTUD2's significance in cellular quality control mechanisms.

Human

E. coli

Tag Free

Q5VVQ6 (F2-V348)

55432

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

<1 EU/μg, determined by LAL method.