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SAB4200060

Sigma-Aldrich

Anti-CYLD antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):
Anti-Cylindromatosis (turban tumor syndrome), deubiquitinating enzyme CYLD, Anti-Ubiquitin carboxyl-terminal hydrolase CYLD, Anti-Ubiquitin specific peptidase like 2, Anti-Ubiquitin thiolesterase CYLD
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~110 kDa

species reactivity

human, rat, mouse

concentration

~1.0 mg/mL

technique(s)

immunohistochemistry: 10-20 μg/mL using heat-retrieved formalin-fixed, paraffin-embedded human skin sections and biotin / ExtrAvidin®-Peroxidase staining system
western blot: 1-2 μg/mL using whole extracts of rat and mouse brain

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... CYLD(1540)
mouse ... Cyld(74256)
rat ... Cyld(312937)

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This Item
SAB1412422SAB1412421HPA050095
conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

antibody form

affinity isolated antibody

clone

polyclonal

clone

2F9, monoclonal

clone

1E9, monoclonal

clone

polyclonal

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous solution

form

buffered aqueous glycerol solution

mol wt

antigen ~110 kDa

mol wt

antigen 36.63 kDa

mol wt

antigen 36.63 kDa

mol wt

-

General description

Anti-CYLD is produced in rabbit using as the immunogen a synthetic peptide corresponding to a fragment of human CYLD conjugated to KLH. Cylindromatosis (CYLD) contains an ubiquitin C-terminal ubiquitin-specific protease (USP) catalytic domain, which is responsible for the removal of ubiquitin chains and three cytoskeleton-associated protein-glycine conserved (CAP-Gly) domains.
CYLD is a tumor suppressor that encodes a deubiquitination enzyme. This enzyme regulates cell growth and survival. Inhibition of CYLD can cause cancers of the skin appendages, namely, multiple trichoepithelioma and familial cylindromatosis . Anti-CYLD antibody is specific for CYLD in humans, rats and mice. The immunizing peptide specifically inhibits the detection of the CYLD band by immunoblotting.

Application

Anti-CYLD antibody can be used in immunohistochemistry (10-20 μg/mL using heat-retrieved, formalin-fixed, paraffin-embedded, human skin sections and biotin / ExtrAvidin® -Peroxidase staining system). This antibody is also suitable for use in immunoblot (approx. 110 kDa) and western blot (1-2 μg/mL using whole extracts of rat and mouse brain).
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Biochem/physiol Actions

Cylindromatosis (CYLD) physically interacts with many different proteins and mediates signaling through the nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) and c?Jun N?terminal kinase (JNK) pathways and induces their deubiquitination. It controls cell proliferation and inflammatory responses by NF-κB/JNK-signaling pathways. CYLD regulates cell cycle progression, spermatogenesis and osteoclastogenesis. Mutations in the CYLD gene is associated with cylindromatosis, multiple familial trichoepithelioma and Brooke-Spiegler syndrome.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Legal Information

ExtrAvidin is a registered trademark of Sigma-Aldrich Co. LLC

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Ramin Massoumi
Future oncology (London, England), 7(2), 285-297 (2011-02-25)
The post-translational modification of different proteins via direct ubiquitin attachment is important for various cellular processes. Dysregulation of components of the ubiqutin system have been linked to many diseases including cancer. CYLD is a deubiquitination enzyme that can cleave the
Kai Dong et al.
The American journal of pathology, 187(8), 1763-1771 (2017-06-21)
Inhibiting only cell apoptosis or necroptosis in photoreceptor cells does not protect them against death after traumatic retinal detachment. This study was designed to evaluate the coregulatory effects of the deubiquitinating enzyme cylindromatosis on the apoptosis and necroptosis of photoreceptor
CYLD: a tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes
Sun SC
Cell Death and Differentiation, 17(1), 25-25 (2010)
Rajeswara Rao Pannem et al.
Carcinogenesis, 35(2), 461-468 (2013-10-10)
Posttranslational modification of different proteins via direct ubiquitin attachment is vital for mediating various cellular processes. Cylindromatosis (CYLD), a deubiquitination enzyme, is able to cleave the polyubiquitin chains from the substrate and to regulate different signaling pathways. Loss, or reduced
Soe Thein et al.
PloS one, 9(3), e91312-e91312 (2014-03-13)
NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy. Recruitment of CYLD, a deubiquitinase specific for K63-linked polyubiquitins, is blocked by pre-treatment with tatCN21, a

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