CYLD Antibodies

Structure of CYLD

CYLD is a large protein with a molecular weight of approximately 130 kDa. This protein contains 956 amino acids, and the minor differences in its molecular weight mainly result from the presence of different splicing variants.

The CYLD protein contains 956 amino acids, and its structure is mainly composed of the cytoskeleton binding domain at the N-terminal and the deubiquitinating enzyme domain at the C-terminal. The core functional region of the protein is a special deubiquitinating enzyme domain, which precisely regulates signaling pathways such as NF-κB by catalyzing the removal of deubiquitination chains. The N-terminal of the protein contains three characteristic CAP-Gly domains, which mediate the interaction with tubulin. The catalytic residues at the proximal end are responsible for activating water molecules to carry out deubiquitination reactions, while the substrate recognition loop at the distal end ensures selectivity for specific ubiquitin chain types and prevents non-specific proteolysis.

Fig. 1 CYLD structure, conservation and genetic models.¹

Key structural properties of CYLD:

• Contains three characteristic CAP-Gly domains at the N-terminal
• With special C end to ubiquitin enzyme catalytic domain structure
• Identify and bind specific ubiquitin chains through "catalytic cracks"
• B-box and Coiled-coil domains mediate protein interactions

Functions of CYLD

The core function of the CYLD protein is to regulate cellular signaling pathways as a deubiquitinating enzyme. However, it is also involved in a variety of physiological and pathological processes, including inflammatory responses, apoptosis and tumor suppression.

With many different characteristics of signal protein regulation pathways, CYLD through highly specific to the substrate protein hydrolysate on lysine 63 connection ubiquitin chains to precisely restrain the nf-kappa B pathway, such as the reflected as a key molecular brake function, specially the steady-state equilibrium responsible for the maintenance of cellular signal transduction.

Applications of CYLD and CYLD Antibody in Literature

1. Marín-Rubio, José L., et al. "CYLD in health and disease." Disease Models & Mechanisms 16.6 (2023): dmm050093. https://doi.org/10.1242/dmm.050093

The article indicates that CYLD is a deubiquitinating enzyme that plays a key role in immune, tumor and neurodegenerative diseases by regulating signaling pathways such as NF-κB and Wnt. Loss of function or acquired mutations can lead to different disease phenotypes. This article reviews the mechanism of action of CYLD by combining animal models with human disease research.

2. Gu, Yanan, et al. "CYLD regulates cell ferroptosis through Hippo/YAP signaling in prostate cancer progression." Cell Death & Disease 15.1 (2024): 79. https://doi.org/10.1038/s41419-024-06464-5

The article indicates that CYLD plays a tumor suppressor role in prostate cancer. Research has found that CYLD promotes ferroptosis in tumors, inhibits cancer cell proliferation and enhances their sensitivity to ferroptosis by deubiquitinating the YAP protein and upregulating the expression of ACSL4 and TFRC. Clinical data indicate that the expression of CYLD is negatively correlated with the malignancy of cancer.

3. Verhoeft, Krista Roberta, Hoi Lam Ngan, and Vivian Wai Yan Lui. "The cylindromatosis (CYLD) gene and head and neck tumorigenesis." Cancers of the head & neck 1.1 (2016): 10. https://doi.org/10.1186/s41199-016-0012-y

The article indicates that CYLD germline mutations can trigger a rare skin syndrome, with patients suffering from multiple head and neck tumors, and some of them have a risk of malignancy. This gene is the only known tumor suppressor gene associated with this syndrome to date. Whole exome sequencing has also identified CYLD mutations in various malignant tumors, and the specific carcinogenic mechanism remains to be further clarified.

4. Li, Yueshuo, et al. "CYLD induces high oxidative stress and DNA damage through class I HDACs to promote radiosensitivity in nasopharyngeal carcinoma." Cell Death & Disease 15.1 (2024): 95. https://doi.org/10.1038/s41419-024-06419-w

The article indicates that CYLD regulates cellular antioxidant responses and DNA damage repair by binding to and inhibiting class I histone deacetylase (HDAC1/2), thereby influencing tumor radiosensitivity. The use of HDAC inhibitors can enhance the effect of radiotherapy and provide a new target for tumor treatment.

5. Lim, Michelle CC, Gunter Maubach, and Michael Naumann. "CYLD-TRAF6 interaction promotes ADP-heptose-induced NF-κB signaling in H. pylori infection." EMBO reports (2025): 1-23. https://doi.org/10.1038/s44319-025-00480-y

The article indicates that in Helicobacter pylori infection, CYLD antagonizes the deubiquitination of TRAF6 by A20 in a non-catalytic manner, enhances the activation of the classical NF-κB pathway in the early stage, and thereby triggers the A20 negative feedback mechanism. This study reveals a novel relationship between CYLD and A20 in regulating NF-κB signaling.

Creative Biolabs: CYLD Antibodies for Research

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

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