PBRM1 Antibodies

Structure of PBRM1

The molecular weight of the PBRM1 protein is approximately 200 kDa. Its molecular weight is relatively conserved among different species, with the main differences arising from the complex composition of its multiple domains.

PBRM1 is a large multi-domain protein, with its primary structure consisting of approximately 1650 amino acids and folding into multiple independent functional modules. The core function of this protein relies on its tandem 6 bromine domains, which can specifically recognize and bind to the acetylated tails of histones, thereby anchoring the entire chromatin remodeling complex to specific genomic regions. Additionally, the C-terminal BROMO domain is crucial for maintaining the overall stability of the complex and subunit assembly. This protein does not contain a catalytic active center, and its function is mainly achieved through protein-protein interactions and protein-nucleic acid interactions.

Fig. 1 3D structure of PBRM1 and the mutation cite is shown.¹

Key structural properties of PBRM1:

• Composed of multiple linked bromodomains
• Through the BROMO domain-mediated protein interaction
• The function is entirely dependent on protein-protein interactions.

Functions of PBRM1

The protein encoded by the PBRM1 gene (BAF180) mainly functions as the core subunit of the chromatin remodeling complex SWI/SNF, regulating gene transcription. Additionally, it plays a crucial role in various cellular processes, including DNA damage repair and cell cycle regulation.

Unlike single-function oxygen storage proteins, PBRM1 integrates multiple epigenetic signals through its multiple brom domains, acting like a complex "signal hub" that links chromatin state with a wide range of cellular functions. The consequences of its functional loss are pleiotropic, highlighting its central role in maintaining cellular homeostasis.

Applications of PBRM1 and PBRM1 Antibody in Literature

1. Aili, Abudureyimujiang, et al. "Mutational analysis of PBRM1 and significance of PBRM1 mutation in anti-PD-1 immunotherapy of clear cell renal cell carcinoma." Frontiers in Oncology 11 (2021): 712765. https://doi.org/10.3389/fonc.2021.712765

This study analyzed the impact of PBRM1 gene mutations and expression on immunotherapy for renal cell carcinoma and found that PBRM1 deletion was associated with a reduction in CD4+T cells within the tumor, affecting the efficacy of anti-PD-1 therapy and suggesting its potential as a therapeutic target.

2. Gu, Di, et al. "PBRM1 deficiency sensitizes renal cancer cells to DNMT inhibitor 5-fluoro-2'-deoxycytidine." Frontiers in Oncology 12 (2022): 870229. https://doi.org/10.3389/fonc.2022.870229

Research has found that renal cancer cells lacking PBRM1 have an enhanced response to DNA damage and are sensitive to DNA-toxic drugs. The DNMT inhibitor Fdcyd selectively inhibits the growth of the apoptotic factor XAF1 by inducing DNA damage and activating it, providing a new strategy for the treatment of PBRM1-mutated renal cell carcinoma.

3. Lane, Karen A., et al. "PBRM1 directs PBAF to pericentromeres and protects centromere integrity." Nature Communications 16.1 (2025): 1980. https://doi.org/10.1038/s41467-025-57277-9 

Research reveals the crucial role of the chromatin remodeling complex PBAF in maintaining the stability of centromere structure. The absence of its subunit PBRM1 can lead to centromere fragility, increase genomic instability, and make cells dependent on spindle examination points, suggesting potential therapeutic targets.

4. Zimmer, Kai, et al. "PBRM1 mutations might render a subtype of biliary tract cancers sensitive to drugs targeting the DNA damage repair system." NPJ precision oncology 7.1 (2023): 64. https://doi.org/10.1038/s41698-023-00409-5

Research has found that PBRM1 mutations account for approximately 8.1% of biliary tract cancers, often accompanied by co-mutations in chromatin remodeling and DNA repair genes. In vitro experiments suggest that the absence of PBRM1 can enhance the sensitivity to PARP/ATR inhibitors, providing a new basis for targeted therapy.

5. Li, Rui, et al. "PBRM1 deficiency enhances PD1 immunotherapeutic sensitivity via chromosomal accessibility in colorectal cancer." Theranostics 15.8 (2025): 3316. https://doi.org/10.7150/thno.100793  

This study found that the deletion of PBRM1 significantly enhanced the sensitivity of PD-1 immunotherapy by increasing chromosome openness, activating the NF-κB pathway and releasing chemokines CCL5/CXCL10, thereby increasing the infiltration of CD8+T/NK cells in colorectal cancer.

Creative Biolabs: PBRM1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality PBRM1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom PBRM1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our PBRM1 antibodies, custom preparations, or technical support, contact us at email.