ARID1B Antibodies

Structure of ARID1B

ARID1B is a large nucleoprotein with a molecular weight of approximately 250 kDa, and its precise molecular weight varies among different transcript isomers. As the core subunit of the chromatin remodeling complex SWI/SNF, its molecular size is directly related to the functional complexity.

This protein is composed of approximately 2,000 amino acid residues, and its core feature is the inclusion of a highly conserved AT-rich interaction domain (ARID), which mediates its binding to a specific DNA sequence. The ARID domain is mainly composed of a series of β -folds, forming a typical helical - turning - helical motif, which is responsible for recognizing the AT-rich sequence in the promoter region of the target gene. Its C-terminal also contains multiple functional domains that interact with other subunits of SWI/SNF, jointly assembling into a large complex. By hydrolyzing ATP, it alters the position of the nucleosome, thereby regulating the accessibility and transcriptional activity of the gene.

Fig. 1 The Protein Network Driving ARID1B into the Nucleus.¹

Key structural properties of ARID1B:

• Contains highly conserved AT-rich interaction domains (ARID domains)
• Unordered regions with multiple long fragments
• The C-terminal region contains a number of functional mods responsible for assembly with other subunits of the SWI/SNF complex
• Molecular switch functions that drive chromatin remodeling through a wide range of conformational changes

Functions of ARID1B

The main function of ARID1B protein is to act as a DNA-binding subunit of chromatin remodeling complexes and regulate gene transcription. In addition, it is also widely involved in key biological processes such as embryonic development, cell differentiation and tumor suppression.

The function of ARID1B depends on the SWI/SNF complex it is located in, which alters the nucleosome position by hydrolyzing ATP. Its regulation is highly gene-specific and environmentally dependent, in sharp contrast to the single and clear functional pattern of myoglobin.

Applications of ARID1B and ARID1B Antibody in Literature

1. Clayton-Smith, Jill. "The ARID1B spectrum in 143 patients: from nonsyndromic intellectual disability to Coffin–Siris syndrome." Genetics in Medicine (2018). https://doi.org/10.1038/s41436-018-0330-z

The article indicates that the intellectual disability (ID) caused by the pathogenic variant ARID1B is highly similar to the phenotypic spectrum of patients with Coffin-Siris syndrome (CSS), with only the occurrence frequency of some CSS-related facial features differing. Research suggests that phenotypic collection methods should include negative feature records to avoid underestimating gene-associated phenotypes.

2. Zhang, Mingyi, et al. "ARID1B maintains mesenchymal stem cell quiescence via inhibition of BCL11B-mediated non-canonical Activin signaling." Nature Communications 15.1 (2024): 4614. https://doi.org/10.1038/s41467-024-48285-2

This study reveals that ARID1B maintains the homeostasis of mesenchymal stem cells by directly inhibiting the expression of Bcl11b and regulating the non-classical Activin signaling pathway. The research clarified the key role and molecular mechanism of ARID1B as an epigenetic modifier in the fate determination of stem cells.

3. Bosch, Elisabeth, et al. "The missing link: ARID1B non-truncating variants causing Coffin-Siris syndrome due to protein aggregation." Human Genetics 143.8 (2024): 965-978. https://doi.org/10.1007/s00439-024-02688-9

This study confirmed that non-truncated variations in the EHD2 and ARID domains of the ARID1B protein can lead to abnormal protein aggregation and loss of function. The methylation pattern is consistent with the classical pathogenic mechanism of insufficient haplodose, providing a new basis for the determination of the pathogenicity of related variations.

4. Odnokoz, Olena, et al. "Disruption of ARID1B Recruitment to the Nuclear Pore Complex as a New Anticancer Therapeutic Strategy." Advanced Science 12.36 (2025): e15585. https://doi.org/10.1002/advs.202415585

Research has found that ARID1B overenters the nucleus through the KPNA2-KPNB1 nuclear transport complex, negatively regulating ARID1A and driving tumor growth in triple-negative breast cancer. Blocking this nuclear transport can inhibit tumors and enhance the efficacy of PARP inhibitors, providing a new target for treatment.

5. Martins-Costa, Catarina, et al. "ARID1B controls transcriptional programs of axon projection in an organoid model of the human corpus callosum." Cell stem cell 31.6 (2024): 866-885. https://doi.org/10.1016/j.stem.2024.04.014

Research has found that ARID1B is the core DNA-binding subunit of the key neurodevelopmental complex mSWI/SNF, and its mutation is the main genetic cause of corpus callosum hypoplasia and related intellectual disabilities and autism.

Creative Biolabs: ARID1B Antibodies for Research

Creative Biolabs specializes in the production of high-quality ARID1B antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom ARID1B 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 ARID1B antibodies, custom preparations, or technical support, contact us at email.