Human OTUB1 (His Tag) recombinant protein

Human OTUB1 (His Tag) recombinant protein

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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.

Ubiquitin thioesterase OTUB1

OTUB1; FLJ20113; OTB1; FLJ40710; AI850305; HSPC263; MGC111158; OTU1; MGC4584

Q96FW1

OTUB1; OTB1; OTU1; HSPC263

E. coli

A DNA sequence encoding the human OTUB1 (Q96FW1-1) (Met 1-Lys 271) was expressed, with a polyhistide tag at the N-terminus.

Human

The recombinant human OTUB1 consisting of 282 amino acids and has a calculated molecular mass of 32.8 kDa. The apparent molecular mass of the protein is approximately 37 kDa in SDS-PAGE under reducing conditions.

> 97 % as determined by SDS-PAGE