RING1 Antibodies

Structure of RING1

RING1, as the core component of Polycomb inhibitory complex 1 (PRC1), has a molecular weight of approximately 39-45 kDa, and the specific value varies depending on the subtype and post-translational modification. The sequence differences of key functional domains among different species may lead to subtle differences in molecular weight.

Human RING1 protein is composed of 336 amino acids with a compact tertiary structure stabilized by the RING domain (residues 50-100) and the RAWUL domain (residues 150-200). These domains mediate protein-protein interactions and E3 ubiquitin ligase activity.

Fig. 1 Structural Insights into the RING-between-RING Architecture of Parkin Core Domain.¹

Key structural properties of RING1:

• Conservative RING domain
• Multi-subunit binding interface
• Dynamic control element
• Epigenetic effector module

Functions of RING1

RING1, as the core catalytic subunit of the PRC1 complex, mainly functions to regulate gene silencing through epigenetic modification. Meanwhile, it is also involved in a variety of important biological processes, including cell fate determination and the occurrence and development of diseases.

The substrate recognition feature of RING1 presents a "dual-lock mechanism": Structural lock: RING-BMI1 heterodimer specifically recognizes nucleosome surfaces; Epigenetic locking: Preferentially binds to chromatin regions with pre-existing H3K27me3 markers.

Applications of RING1 and RING1 Antibody in Literature

1. Wei, Jianhua, et al. "Role of Bmi1 in H2A ubiquitylation and Hox gene silencing." Journal of Biological Chemistry 281.32 (2006): 22537-22544. https://www.jbc.org/article/S0021-9258(19)47591-1/fulltext

The article indicates that RING1 forms the H2A ubiquitin ligase complex with BMI1, RING2, etc. Among them, BMI1 significantly enhances the H2A ubiquitination activity of RING1/RING2 by stabilizing the structure of the complex. This modification directly regulates the silencing of the HoxC5 gene and cell proliferation. The deletion of BMI1 leads to the global deletion of H2A ubiquitination, the upregulation of HoxC5 expression and the slowdown of cell growth. Experiments confirmed that the ubiquitination of H2A was enriched in the 5' regulatory region of the HoxC5 gene, revealing a new mechanism by which BMI1-RING1 regulates the expression of target genes through epigenetics.

2. Gao, Song, et al. "Low expression of the polycomb protein RING1 predicts poor prognosis in human breast cancer." Frontiers in Oncology 10 (2021): 618768. https://doi.org/10.3389/fonc.2020.618768

This article's research found that RING1, a core member of the polycomb protein family, plays a key role in the occurrence and development of various cancers. As an important epigenetic regulatory factor, the expression characteristics and prognostic value of RING1 in breast cancer still need to be further explored, which provides a new research direction for targeted therapy of breast cancer.

3. Alchanati, Iris, et al. "The E3 ubiquitin-ligase Bmi1/Ring1A controls the proteasomal degradation of Top2α cleavage complex–a potentially new drug target." PloS one 4.12 (2009): e8104. https://doi.org/10.1371/journal.pone.0008104

The article indicates that Bmi1/Ring1A E3 ubiquitin ligase is involved in the drug-induced degradation process of Top2α proteasome. Inhibiting Bmi1 can block the degradation of Top2α, prolong the retention time of its DNA cleavage complex, and enhance the therapeutic effect of the drug. Experiments have confirmed that this complex can directly ubiquitinate Top2α, and the small molecule inhibitors obtained through screening can block this process and produce a synergistic effect with the topoisomerase 2 agent.

4. Rui, Xiaohui, et al. "Long non-coding RNA C5orf66-AS1 promotes cell proliferation in cervical cancer by targeting miR-637/RING1 axis." Cell death & disease 9.12 (2018): 1175. https://doi.org/10.1038/s41419-018-1228-z

This article found that lncRNA C5orf66-AS1 was abnormally highly expressed in cervical cancer and relieved its inhibitory effect on RING1 by competitively binding to miR-637. RING1, as a key regulatory factor, mediates the regulatory effect of the C5orf66-AS1/miR-637 axis on the proliferation, apoptosis and cell cycle of cervical cancer cells. In vivo and in vitro experiments have confirmed that targeting this pathway can significantly inhibit tumor growth, providing a new target for the treatment of cervical cancer

5. He, Zhen, et al. "Ring 1 and YY1 binding protein is expressed in murine spermatocytes but dispensable for spermatogenesis." Genes 11.1 (2020): 84. https://doi.org/10.3390/genes11010084

This article has found that the Ring1-binding protein Rybp plays a key regulatory role in spermatogenesis. As the core component of the multicomb protein complex, RING1 is specifically enriched in spermatocytes through Rybp and regulates the expression of meiosis related genes. Although Rybp knockout does not directly affect fertility, the Ring1-RYBP complex may precisely regulate the spermatogenesis process through epigenetic mechanisms, revealing the important role of RING1 in the development of germ cells.

Creative Biolabs: RING1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality RING1 antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western Blot, Immunohistochemistry, and other research applications.

• Custom RING1 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 RING1 antibodies, custom preparations, or technical support, contact us at info@creative-biolabs.com.