BAP1 Protein, Human (His)

BAP1 protein deubiquitinates histone H2A and HCFC1, mediating deubiquitination of H2AK119ub1. It regulates cell growth by deubiquitinating HCFC1 chains and inhibits BRCA1 and BARD1 activity. BAP1 also protects itself from cytoplasmic sequestration and acts as a tumor suppressor. BAP1 Protein, Human (His) is the recombinant human-derived BAP1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of BAP1 Protein, Human (His) is 728 a.a., .

The BAP1 protein functions as a deubiquitinating enzyme with a critical role in chromatin regulation, mediating the deubiquitination of histone H2A and HCFC1. As a catalytic component of the PR-DUB complex, it specifically targets histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1), highlighting its involvement in chromatin dynamics. BAP1 does not deubiquitinate monoubiquitinated histone H2B. It further serves as a regulator of cell growth by mediating the deubiquitination of HCFC1 N-terminal and C-terminal chains, displaying specificity towards 'Lys-48'-linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Intriguingly, the deubiquitination of HCFC1 by BAP1 does not lead to an increase in HCFC1 stability. BAP1 interferes with the BRCA1 and BARD1 heterodimer activity, inhibiting their ability to mediate ubiquitination and autoubiquitination, although it does not directly mediate deubiquitination of BRCA1 and BARD1. Moreover, BAP1 can undergo autodeubiquitination via intramolecular interactions, counteracting monoubiquitination at the nuclear localization signal (NLS) and thereby protecting it from cytoplasmic sequestration. This multifaceted functionality positions BAP1 as a tumor suppressor.

Human

E. coli

N-6*His

Q92560 (N2-Q729)

8314

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

<1 EU/μg, determined by LAL method.