This rat IgG monoclonal antibody was raised against the kinase domain of E3 ubiquitin-protein ligase UBR5 (EDD).
EDD/UBR5/hHYD is a putative tumor suppressor and HECT (homologous to E6-AP C-terminus)-domain-containing E3 ubiquitin ligase implicated in cellular pathways including the regulation of gene expression, the DNA damage response, and in necroptosis after it was identified in a siRNA screen. EDD regulates gene expression transcriptionally, by forming complexes with transcription factors, and translationally by regulating protein levels of Paip2, a poly-A-binding protein inhibitor. EDD is also important in the cellular DNA damage response, mediating ATM phosphorylation of its substrates CHK2 and p53 after DNA damage to control cell cycle arrest. Given its multiple functions in mediating cellular processes, EDD likely acts as a chaperone protein, coordinating the various protein complexes involved in different cellular pathways.
From the laboratory of Junying Yuan, PhD, Harvard University.
|EDD (E3 ubiquitin-protein ligase UBR5)
|EDD bacterial fusion protein (40 kd of kinase domain)
|PBS, 0.05% (w/v) Sodium Azide
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