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AB153698

Anti-CYLD antibody - N-terminal

4

(1 Review)

|

(4 Publications)

Rabbit Polyclonal CYLD antibody. Suitable for WB, ICC/IF and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Fragment Protein within Human CYLD aa 1-250.

View Alternative Names

CYLD1, KIAA0849, HSPC057, CYLD, Ubiquitin carboxyl-terminal hydrolase CYLD, Deubiquitinating enzyme CYLD, Ubiquitin thioesterase CYLD, Ubiquitin-specific-processing protease CYLD

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-CYLD antibody - N-terminal (AB153698)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-CYLD antibody - N-terminal (AB153698)

Immunofluorescent analysis of methanol-fixed HeLa cells labeling CYLD with ab153698 at 1/200 dilution. (Lower image shows cells co-stained with Hoechst 33342.

Western blot - Anti-CYLD antibody - N-terminal (AB153698)
  • WB

Unknown

Western blot - Anti-CYLD antibody - N-terminal (AB153698)

7.5% SDS PAGE

All lanes:

Western blot - Anti-CYLD antibody - N-terminal (ab153698) at 1/1000 dilution

All lanes:

HeLa whole cell lysate at 30 µg

Predicted band size: 107 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF, WB

applications

Immunogen

Recombinant Fragment Protein within Human CYLD aa 1-250. The exact immunogen used to generate this antibody is proprietary information.

Q9NQC7

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.025% Proclin 300 Constituents: PBS, 20% Glycerol (glycerin, glycerine)
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

CYLD also known as cylindromatosis or turban tumor syndrome is a protein that serves mainly as a deubiquitinating enzyme. This protein has a mass of approximately 108 kDa and is expressed in a variety of tissues most notably the skin and lungs. It is a negative regulator of cell signaling cascades particularly in pathways where ubiquitination needs to be controlled. CYLD interacts directly with other proteins to remove ubiquitin chains a process that is essential for regulating the degradation of proteins and maintaining cellular functions.
Biological function summary

The deubiquitination activity of CYLD plays a critical role in controlling inflammation and cell proliferation. This protein often associates with complexes that regulate the activity of NF-kB signaling pathways. By removing ubiquitin from specific substrates CYLD limits the activation of NF-kB therefore modulating inflammatory responses in the body. Additionally CYLD's role extends to controlling cell cycle progression and preventing uncontrolled cell growth making it essential in tissue homeostasis.

Pathways

CYLD is a significant regulator of the NF-kB and Wnt signaling pathways. It interacts with proteins such as TRAF2 TRAF6 and NEMO which are important in these pathways. CYLD prevents constitutive activation of NF-kB therefore serving as a checkpoint in inflammation and immune response. In the Wnt signaling pathway CYLD's regulation affects the turnover of beta-catenin highlighting its role in developmental processes and cellular differentiation.

CYLD is closely associated with cylindromatosis and familial adenomatous polyposis. Mutations or disruptions in CYLD function can lead to these conditions where abnormal cell proliferation occurs due to unregulated NF-kB activation. In cylindromatosis CYLD mutations result in the benign skin tumors known as cylindromas. Furthermore its connection to proteins like TRAF2 links it to other tumorigenic processes emphasizing CYLD's influence in both inflammatory and proliferative disorders.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis (PubMed : 18313383, PubMed : 18636086, PubMed : 26670046, PubMed : 26997266, PubMed : 27458237, PubMed : 27591049, PubMed : 29291351, PubMed : 32185393). Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors (PubMed : 12917689, PubMed : 12917691, PubMed : 32185393). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed : 12917690). Negative regulator of Wnt signaling (PubMed : 20227366). Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed : 19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed : 18222923, PubMed : 20194890). Required for normal cell cycle progress and normal cytokinesis (PubMed : 17495026, PubMed : 19893491). Inhibits nuclear translocation of NF-kappa-B (PubMed : 18636086). Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (PubMed : 18636086). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (By similarity). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (By similarity). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis : recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed : 26670046, PubMed : 26997266, PubMed : 27458237, PubMed : 27591049). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (PubMed : 26997266). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed : 29291351). Removes also 'Lys-63'-linked polyubiquitin chains of MAP3K1 and MA3P3K3, which inhibit their interaction with MAP2K1 and MAP2K2 (PubMed : 34497368).
See full target information CYLD

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Molecular medicine (Cambridge, Mass.) 27:137 PubMed34711178

2021

IκB kinase promotes Nrf2 ubiquitination and degradation by phosphorylating cylindromatosis, aggravating oxidative stress injury in obesity-related nephropathy.

Applications

Unspecified application

Species

Unspecified reactive species

Yin-Yin Chen,Han Hong,Yu-Ting Lei,Jia Zou,Yi-Ya Yang,Li-Yu He

Haematologica 107:1131-1143 PubMed34162177

2021

Characterization of GECPAR, a noncoding RNA that regulates the transcriptional program of diffuse large B-cell lymphoma.

Applications

Unspecified application

Species

Unspecified reactive species

Sara Napoli,Luciano Cascione,Andrea Rinaldi,Filippo Spriano,Francesca Guidetti,Fangwen Zhang,Maria Teresa Cacciapuoti,Afua Adjeiwaa Mensah,Giulio Sartori,Nicolas Munz,Mattia Forcato,Silvio Bicciato,Annalisa Chiappella,Paola Ghione,Olivier Elemento,Leandro Cerchietti,Giorgio Inghirami,Francesco Bertoni

Journal of cellular biochemistry 121:1250-1259 PubMed31489998

2019

Guanylate-binding protein-2 inhibits colorectal cancer cell growth and increases the sensitivity to paclitaxel of paclitaxel-resistant colorectal cancer cells by interfering Wnt signaling.

Applications

Unspecified application

Species

Unspecified reactive species

Jing Wang,Hui Min,Bin Hu,Xiaorong Xue,Yufan Liu

Oncotarget 8:111386-111395 PubMed29340061

2017

Analysis of the mutational landscape of classic Hodgkin lymphoma identifies disease heterogeneity and potential therapeutic targets.

Applications

Unspecified application

Species

Unspecified reactive species

Elena Mata,Antonio Díaz-López,Ana M Martín-Moreno,Margarita Sánchez-Beato,Ignacio Varela,María J Mestre,Carlos Santonja,Fernando Burgos,Javier Menárguez,Mónica Estévez,Mariano Provencio,Beatriz Sánchez-Espiridión,Eva Díaz,Carlos Montalbán,Miguel A Piris,Juan F García
View all publications

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