OTUB2 Protein, Human (GST)

OTUB2 is a hydrolase that efficiently removes conjugated ubiquitin from proteins in vitro, implying a crucial role in preventing protein degradation and regulating turnover. Its deubiquitinating activity targets “Lys-11”, “Lys-48” and “Lys-63” linked polyubiquitin chains, with preference for the latter. OTUB2 Protein, Human (GST) is the recombinant human-derived OTUB2 protein, expressed by E. coli , with N-GST labeled tag. The total length of OTUB2 Protein, Human (GST) is 234 a.a., with molecular weight of ~52.0 kDa.

As a hydrolase, OTUB2 exhibits the capacity to efficiently remove conjugated ubiquitin from proteins in vitro, suggesting a pivotal regulatory role in protein turnover by preventing degradation. With its deubiquitination activity, OTUB2 acts on 'Lys-11', 'Lys-48', and 'Lys-63'-linked polyubiquitin chains, displaying a preference for the latter. This specificity underscores OTUB2's selectivity in modulating diverse ubiquitin linkages, emphasizing its potential significance in orchestrating cellular processes related to protein ubiquitination and degradation.

Human

E. coli

N-GST

Q96DC9 (M1-H234)

78990  [NCBI]

MSETSFNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDGNCFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMDTALNHHVFPEAATPSVYLLYKTSHYNILYAADKH

Approximately 52.0 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.