YOD1 belongs to the ovarian tumor domain (OUT) containing subfamily of deubiquitinating enzymes (DUBs), which are cysteine proteases specifically removing ubiquitin from ubiquitin-conjugated protein substrates (1). YOD1 participates in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins via deubiquitination of 'Lys-11', 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains (2). YOD1 positively regulates the stability of ITCH resulting in the activation of YAP in liver cancer study (3).
DUBA8; OTUD2; PRO0907
1. Sowa ME, et al. Defining the human deubiquitinating enzyme interaction landscape. Cell. 2009 Jul 23;138(2):389-403.
2. Flierman D, et al. Non-hydrolyzable Diubiquitin Probes Reveal Linkage-Specific Reactivity of Deubiquitylating Enzymes Mediated by S2 Pockets. Cell Chem Biol. 2016 Apr 21;23(4):472-82.
3. Kim Y, et al. Deubiquitinase YOD1: the potent activator of YAP in hepatomegaly and liver cancer. BMB Rep. 2017 Jun;50(6):281-282.
Sample Purity Data. For specific information on a given lot, see related technical data sheet.
Storage, Stability, and Shipping:
Store product at –70oC. For optimal storage, aliquot target into smaller quantities after centrifugation and store at recommended temperature. For most favorable performance, avoid repeated handling and multiple freeze/thaw cycles.
There are no related publications available for this product.
Cancer, Cardiovascular Disease, Cell Cycle, Cellular Stress, Invasion/Metastasis, Metabolic Disorder