Anti-BAP1

In 1X PBS, pH 7.4, with 0.09% sodium azide. 'BRCA1-associated protein-1,' or BAP1 interacts with the RING finger domain of BRCA1. The N-terminal 240 amino acids of the predicted 729-amino acid human protein show homology to ubiquitin C-terminal hydrolases (UCHs), thiol proteases that catalyze proteolytic processing of ubiquitin. In addition, BAP1 contains an acidic region, a highly charged C-terminal region, and 2 putative nuclear localization signals.. BAP1 and BRCA1 associate in vivo and have overlapping subnuclear localization patterns.1 BAP1 enhances BRCA1-mediated inhibition of breast cancer cell growth. Northern blot analysis indicates that BAP1 is expressed as a 4-kb mRNA in all human tissues tested, with A 4.8-kb transcript expressed exclusively in testis. Northern blot analysis and in situ hybridization reveal that BAP1 and BRCA1 are coexpressed during murine breast development and remodeling. The BAP1 gene has been mapped to 3p21.3, a region of loss of heterozygosity for breast cancer as well as frequently deleted in lung carcinomas.1 Intragenic homozygous rearrangements and deletions of BAP1 appear in lung carcinoma cell lines. It has been postulated that BAP1 is a tumor suppressor gene that functions in the BRCA1 growth control pathway.1 Protein function: Deubiquitinating enzyme that plays a key role in chromatin by mediating deubiquitination of histone H2A and HCFC1. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not deubiquitinate monoubiquitinated histone H2B. Acts as a regulator of cell growth by mediating deubiquitination of HCFC1 N-terminal and C-terminal chains, with some specificity toward 'Lys-48'- linked polyubiquitin chains compared to 'Lys-63'-linked polyubiquitin chains. Deubiquitination of HCFC1 does not lead to increase stability of HCFC1. Interferes with the BRCA1 and BARD1 heterodimer activity by inhibiting their ability to mediate ubiquitination and autoubiquitination. It however does not mediate deubiquitination of BRCA1 and BARD1. Able to mediate autodeubiquitination via intramolecular interactions to couteract monoubiquitination at the nuclear localization signal (NLS), thereby protecting it from cytoplasmic sequestration (PubMed:24703950). Acts as a tumor suppressor. [The UniProt Consortium]