Anti-CYLD antibody produced in rabbit

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.

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)

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.

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

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