UHRF1 Antibodies

Structure of UHRF1

UHRF1 is a multi-domain nuclear protein with a molecular weight of approximately 90 kDa. The relative molecular mass varies slightly among different species due to differences in amino acid sequences.

The UHRF1 protein contains multiple functional domains, and its overall conformation is formed through the cooperative interaction between these domains, resulting in a dynamically changeable "bifurcate"-like spatial structure. The secondary structure of this protein consists of α-helices, β-sheets, and random coils, and it is responsible for recognizing different epigenetic modification signals. The SRA domain embedded in the UHRF1 structure (a domain that can specifically recognize hemimethylated DNA) can directly bind to hemimethylated DNA, while its Tudor domain and PHD domain respectively recognize specific modifications on the tail of histone H3, jointly mediating the chromatin localization of the protein. The collaborative action of these domains enables UHRF1 to "read" various epigenetic information, recruit it to specific chromatin regions, and thereby regulate downstream functions.

Fig. 1 Representation of UHRF1 functional domains and their functions.¹

Key structural properties of UHRF1:

• Multi-domain architecture consisting of multiple conserved functional domains
• SRA domain specifically recognizes hemimethylated DNA
• Tudor domain and PHD domain work together to recognize modified histones
• RING domain has E3 ubiquitin ligase activity, mediating substrate ubiquitination

Functions of UHRF1

The main function of UHRF1 is to act as an epigenetic regulatory factor, ensuring the accurate transmission of DNA methylation patterns during DNA replication. This protein participates in a variety of crucial molecular and cellular processes through the coordinated action of its multiple domains.

The binding and dissociation kinetics of UHRF1 within the cell exhibit a highly coordinated pattern. The binding curve of UHRF1 to chromatin shows dynamic periodic changes, which are closely related to the cell cycle progression. This unique binding characteristic indicates that UHRF1 can precisely regulate its residence time on chromatin according to the cell cycle stage. During the DNA replication period, it briefly binds to complete the transmission of epigenetic modifications, and then rapidly dissociates to advance the cell cycle process.

Applications of UHRF1 and UHRF1 Antibody in Literature

1. Kim, Ahhyun, and Claudia A. Benavente. "Oncogenic roles of UHRF1 in cancer." Epigenomes 8.3 (2024): 26. https://doi.org/10.3390/epigenomes8030026

The article indicates that UHRF1 maintains epigenetic modifications through multiple functional domains, is overexpressed in various tumors and plays a role in carcinogenesis. This article reviews its structural function, interactions with key proteins, and the carcinogenic mechanism in solid tumors, and explores potential therapeutic strategies targeting UHRF1.

2. Gu, Lili, Yongming Fu, and Xiong Li. "Roles of post-translational modifications of UHRF1 in cancer." Epigenetics & Chromatin 17.1 (2024): 15. https://doi.org/10.1186/s13072-024-00540-y

The article indicates that UHRF1, as a RING family E3 ubiquitin ligase, regulates its stability, activity and localization through various post-translational modifications. It is abnormally highly expressed in various tumors and inhibits tumor suppressor genes. This article reviews the types of modifications and their functions, providing a basis for targeted therapy.

3. Liu, Yi, et al. "UHRF1-mediated ferroptosis promotes pulmonary fibrosis via epigenetic repression of GPX4 and FSP1 genes." Cell death & disease 13.12 (2022): 1070. https://doi.org/10.1038/s41419-022-05515-z

The study has for the first time discovered that UHRF1 methylates and inhibits GPX4 and FSP1, thereby mediating ferroptosis in alveolar epithelial cells and promoting pulmonary fibrosis. Targeting UHRF1 can block the fibrotic process and provide a new therapeutic target.

4. Tiedemann, Rochelle L., et al. "UHRF1 ubiquitin ligase activity supports the maintenance of low-density CpG methylation." Nucleic acids research 52.22 (2024): 13733-13756.https://doi.org/10.1093/nar/gkae1105

The study found that UHRF1 regulates DNMT1 through ubiquitination signals, maintaining DNA methylation. Abnormalities in this process can lead to low-density CpG hypomethylation and the formation of partial methylated regions, revealing a new mechanism of epigenetic dysregulation in cancer.

5. Kuang, Bo-Hua, et al. "UHRF1 induces metastasis in thyroid cancer." Journal of Oncology 2022.1 (2022): 7716427. https://doi.org/10.1155/2022/7716427

The study found that UHRF1 promotes metastasis in thyroid cancer. The mechanism involves binding and activating the transcription factor c-Jun/AP-1, thereby upregulating the expression of IL-6 and MIF. The UHRF1/AP-1 complex may become a potential therapeutic target.

Creative Biolabs: UHRF1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality UHRF1 antibodies for research and industrial applications. Our portfolio includes monoclonal and polyclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom UHRF1 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 UHRF1 antibodies, custom preparations, or technical support, contact us at email.