Phospho-CYLD (Ser418) Antibody #4500
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 108 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-CYLD (Ser418) Antibody detects endogenous levels of CYLD protein only when phosphorylated on Ser418.
Species Reactivity:
Human
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Mouse, Rat
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser418 of human CYLD protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
CYLD is a cytoplasmic deubiquitinating enzyme encoded by a tumor suppressor gene altered in individuals diagnosed with cylindromatosis, a genetic condition characterized by benign tumors of skin appendages (1,2). Functional CYLD deubiquitinase regulates inflammation and cell proliferation by down regulating NF-κB signaling through removal of ubiquitin chains from several NF-κB pathway proteins (3,4). CYLD is a negative regulator of proximal events in Wnt/β-catenin signaling and is a critical regulator of natural killer T cell development (5,6). The transcription factor Snail can inhibit CYLD expression, resulting in melanoma cell proliferation (7).
CYLD can be phosphorylated at Ser418 by the noncanonical IKK family member IKKε. Phosphorylation at Ser418 decreases CYLD deubiquitinase activity and is important for IKKε-driven transformation (8).
- Biggs, P.J. et al. (1995) Nat Genet 11, 441-3.
- Sun, S.C. (2010) Cell Death Differ 17, 25-34.
- Regamey, A. et al. (2003) J Exp Med 198, 1959-64.
- Glittenberg, M. and Ligoxygakis, P. (2007) Fly (Austin) 1, 330-2.
- Tauriello, D.V. et al. (2010) Mol Cell 37, 607-19.
- Lee, A.J. et al. (2010) EMBO J 29, 1600-12.
- Massoumi, R. et al. (2009) J Exp Med 206, 221-32.
- Hutti, J.E. et al. (2009) Mol Cell 34, 461-72.
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