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SAB4200060

Sigma-Aldrich

Anti-CYLD antibody produced in rabbit

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

Synonim(y):

Anti-Cylindromatosis (turban tumor syndrome), deubiquitinating enzyme CYLD, Anti-Ubiquitin carboxyl-terminal hydrolase CYLD, Anti-Ubiquitin specific peptidase like 2, Anti-Ubiquitin thiolesterase CYLD

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About This Item

Kod UNSPSC:
12352203
NACRES:
NA.41

pochodzenie biologiczne

rabbit

białko sprzężone

unconjugated

forma przeciwciała

affinity isolated antibody

rodzaj przeciwciała

primary antibodies

klon

polyclonal

Postać

buffered aqueous solution

masa cząsteczkowa

antigen ~110 kDa

reaktywność gatunkowa

human, rat, mouse

stężenie

~1.0 mg/mL

metody

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

numer dostępu UniProt

Q9NQC7

Warunki transportu

dry ice

temp. przechowywania

−20°C

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

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

Opis ogólny

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.

Zastosowanie

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)

Działania biochem./fizjol.

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.

Postać fizyczna

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

Informacje prawne

ExtrAvidin is a registered trademark of Merck KGaA, Darmstadt, Germany

Oświadczenie o zrzeczeniu się odpowiedzialności

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.
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
CYLD: a tumor suppressor deubiquitinase regulating NF-kappaB activation and diverse biological processes
Sun SC
Cell Death and Differentiation, 17(1), 25-25 (2010)
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
Marion Bonnet et al.
Medecine sciences : M/S, 27(6-7), 626-631 (2011-07-02)
CYLD deubiquitinase has been originally defined as a tumor suppressor based exclusively on genetic findings. Indeed, inactivation of CYLD in humans results in familial cylindromatosis and multiple trichoepithelioma, two pathologies characterized by the development of tumors originating specifically from the
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