USP7 Antibodies

Structure of USP7

USP7 is a large-molecular-weight deubiquitinating enzyme. Its molecular weight varies due to post-translational modifications and splicing variants. The molecular weight of the full-length human USP7 protein is approximately 130-135 kDa. This enzyme belongs to the cysteine protease family and contains multiple functional domains. The most characteristic ones are the N-terminal TRAF-like domain and the C-terminal catalytic domain. The TRAF-like domain is responsible for recognizing and binding to various substrate proteins, such as p53, MDM2, etc.; while the catalytic domain contains a conserved "cysteine-histidine-aspartic acid" catalytic triad, which is responsible for hydrolyzing the ubiquitin molecular chains attached to the substrate protein, thereby regulating the stability and function of the target protein.

Fig. 1 Schematic illustration of the protein structure of USP7.¹

Key structural properties of USP7:

• Typical ubiquitin-specific protease folding structure
• The central catalytic domain contains a Cys-His-Asp/Asn triad active site.
• The N-terminal TRAF-like domain mediates substrate recognition and protein interaction
• The C-terminal extension region is involved in regulating enzyme activity and cell localization
• Catalytic activity is highly dependent on activity at a cystine a nucleophilic attack

Functions of USP7

The core function of the USP7 gene is to regulate the stability and activity of key proteins within cells. It achieves this by specifically cutting the ubiquitin chains on the substrate proteins. This gene is involved in maintaining cellular homeostasis, responding to DNA damage, and regulating various important physiological and pathological processes such as epigenetic state regulation.

Unlike the single-function oxygen-storing protein myoglobin, USP7 plays a complex and crucial regulatory role in the cellular signaling network through dynamic and selective deubiquitination. Its dysfunction is closely related to various diseases such as cancer and neurodegenerative disorders.

Applications of USP7 and USP7 Antibody in Literature

1. Ni, Wenkai, et al. "USP7 mediates pathological hepatic de novo lipogenesis through promoting stabilization and transcription of ZNF638." Cell Death & Disease 11.10 (2020): 843. https://doi.org/10.1038/s41419-020-03075-8

Studies have shown that the deubiquitinating enzyme USP7 stabilizes ZNF638, activates the AKT/mTORC1/S6K pathway and forms a nuclear complex, thereby promoting the regulation of SREBP1C on fatty acid synthase genes, and driving the generation of liver lipids. Inhibiting the USP7/ZNF638 axis can significantly alleviate the progression of the mouse fatty liver model, providing a new target for the treatment of related liver diseases.

2. Liu, Huai, et al. "USP7 inhibits the progression of nasopharyngeal carcinoma via promoting SPLUNC1-mediated M1 macrophage polarization through TRIM24." Cell death & disease 14.12 (2023): 852. https://doi.org/10.1038/s41419-023-06368-w

Studies have shown that the deubiquitinating enzyme USP7 stabilizes the TRIM24 protein, promotes the expression of SPLUNC1 mediated by STAT3, thereby driving macrophages to polarize towards the M1 phenotype and activating the JAK/STAT pathway. M1 macrophages can inhibit the proliferation and migration of nasopharyngeal cancer cells, and the USP7/TRIM24/SPLUNC1 axis provides a new target for anti-tumor immunotherapy.

3. Dai, Xiaomeng, et al. "USP7 targeting modulates anti-tumor immune response by reprogramming Tumor-associated Macrophages in Lung Cancer." Theranostics 10.20 (2020): 9332. https://doi.org/10.7150/thno.47137

Studies have shown that inhibiting USP7, which is highly expressed in M2-type macrophages, can promote the reversion of these cells to the M1 phenotype by activating the p38 MAPK pathway, thereby enhancing the function of CD8+ T cells. The combination of USP7 inhibitors and PD-1 blockade can synergistically inhibit the growth of lung cancer, providing a new strategy for tumor immunotherapy.

4. Keshri, Swati, et al. "USP7 protects TFEB from proteasome-mediated degradation." Cell Reports 43.11 (2024). https://doi.org/10.1016/j.celrep.2024.114872

Studies have confirmed that the deubiquitinating enzyme USP7 removes the K48-linked polyubiquitin chains of the TFEB protein, preventing it from being degraded by the proteasome, thereby stabilizing the levels of TFEB in the nucleus and cytoplasm, and maintaining the functions of autophagy and lysosome biogenesis in the cells. This provides a new basis for targeting the USP7-TFEB axis to treat cancer and other metabolic-related diseases.

5. Manea, Teodora, et al. "USP7 controls NGN3 stability and pancreatic endocrine lineage development." Nature Communications 14.1 (2023): 2457. https://doi.org/10.1038/s41467-023-38146-9

Studies have shown that the deubiquitinating enzyme USP7 can bind to the transcription factor NGN3 and remove its ubiquitination modification, thereby stabilizing the protein level of NGN3. This mechanism is crucial for driving the differentiation of pancreatic endocrine precursor cells and the formation of pancreatic islet β cells, providing a new target for diabetes cell therapy.

Creative Biolabs: USP7 Antibodies for Research

Creative Biolabs specializes in the production of high-quality USP7 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 USP7 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 USP7 antibodies, custom preparations, or technical support, contact us at email.