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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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CYLD Antibody / Deubiquitinase Antibody recognizes CYLD, a lysine 63-specific deubiquitinating enzyme that negatively regulates multiple intracellular signaling pathways by removing ubiquitin chains from key signaling proteins. Originally identified as the gene mutated in familial cylindromatosis, CYLD has since emerged as an important tumor suppressor and regulator of inflammation, innate immunity, and cell survival. Through its deubiquitinase activity, CYLD controls activation of signaling molecules including TRAF2, TRAF6, NEMO, RIPK1, and additional adaptor proteins that participate in nuclear factor kappa B (NF-kappa B), c-Jun N-terminal kinase (JNK), Wnt, and transforming growth factor beta signaling. By limiting ubiquitin-dependent signal propagation, CYLD helps maintain normal cellular homeostasis and prevents excessive inflammatory responses.
CYLD is widely expressed in epithelial tissues, immune cells, and the nervous system, where it regulates cell proliferation, apoptosis, differentiation, and immune signaling. Its deubiquitinating activity is highly selective for lysine 63-linked and linear ubiquitin chains, allowing precise modulation of signaling complexes without promoting protein degradation. In addition to suppressing NF-kappa B activation, CYLD influences microtubule dynamics, cell migration, ciliogenesis, and mitotic progression through interactions with cytoskeletal and centrosomal proteins. These diverse functions place CYLD at the intersection of signal transduction, inflammation, and cytoskeletal regulation.
Loss-of-function mutations or reduced CYLD expression have been associated with familial cylindromatosis, Brooke-Spiegler syndrome, multiple familial trichoepithelioma, and numerous sporadic cancers including melanoma, hepatocellular carcinoma, colorectal cancer, breast cancer, and hematologic malignancies. CYLD also plays important roles in antiviral immunity, inflammatory disorders, and neurodegenerative disease through its regulation of innate immune signaling and programmed cell death pathways. Because altered ubiquitination contributes to many pathological conditions, CYLD has become an important research target in oncology, immunology, dermatology, and signal transduction studies.
CYLD expression and activity are tightly regulated by phosphorylation, proteolytic processing, and protein-protein interactions that fine-tune cellular responses to cytokines, microbial products, and environmental stress. As interest in ubiquitin biology continues to expand, CYLD remains a key model for understanding how reversible ubiquitination controls intracellular signaling networks. A CYLD Antibody is a valuable research tool for investigating deubiquitination, NF-kappa B signaling, inflammatory responses, tumor suppression, and ubiquitin-dependent signal transduction.
xplore additional research tools for oncogenic signaling, cell regulation, and tumor biology on our Cancer Marker Antibodies page.
Optimal dilution of the CYLD Antibody / Deubiquitinase Antibody should be determined by the researcher.
Amino acids 618-956 of human CYLD were used as the immunogen for the CYLD antibody.
After reconstitution, the CYLD antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
CYLD antibody, Deubiquitinase antibody, Cylindromatosis antibody, CYLD Lysine 63 Deubiquitinase antibody, Ubiquitin Carboxyl-Terminal Hydrolase CYLD antibody
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