OTUB1 Antibody

Cusabio

OTUB1 Antibody

20

Western Blot, ELISA, ImmunoHistoChemistry

Research Use Only

Polyclonal

Unconjugated

OTUB1

OTU deubiquitinase, ubiquitin aldehyde binding 1

deubiquitinating enzyme OTUB1; HSPC263; OTB1; OTU domain, ubiquitin aldehyde binding 1; OTU domain-containing ubiquitin aldehyde-binding protein 1; OTU1; otubain-1; OTU-domain Ubal-binding 1; ubiquitin thioesterase OTUB1; ubiquitin-specific protease otubain 1; ubiquitin-specific-processing protease OTUB1

Rabbit

IgG

Ubiquitin thioesterase OTUB1

Hydrolase that can specifically remove Lys-48-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy. Isoform 1 destabilizes RNF128, leading to prevent anergy. In contrast, isoform 2 stabilizes RNF128 and promotes anergy. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of Lys-48-linked polyubiquitin chains, but not Lys-63-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to Lys-48-linked ubiquitin. Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of Lys-63-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of Lys-63-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved Lys48-linked di-ubiquitin chain.

Human

-20°C or -80°C

41116161