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FIGURE: 1 / 1
Please note: We are reviewing Western blot images included in the antibody testing data in our catalog, including those provided by third parties. Unless expressly labeled or annotated as “raw-unedited”, Western blot images included in the antibody testing data in our catalog may have been edited, optimized or otherwise adjusted for presentation.
Apoptotic signals are often triggered by cell surface death receptors through protein-protein interactions mediated by conserved domains such as the death effector domain. A novel death effector domain (DED)-containing protein, DEDD2, has been recently identified. Over-expression of DEDD2 in transfected cells induces moderate apoptosis and results in substantial sensitization to apoptosis induced by Fas, TRAIL, and FADD. More recently, it has been shown that DEDD2 can bind caspase-8 and -10 in addition to FLIP but not FADD. Like the related protein DEDD, DEDD2 translocates from the cytosol to the nucleus upon induction of apoptosis, and it has been suggested that DEDD2 may target caspase-8 to the nucleus and that DEDD2 thus plays a critical role in death receptor-induced apoptosis. At least two alternatively spliced transcript variants encoding distinct isoforms have been found for DEDD2.
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Protein Aliases: DED-containing protein FLAME-3; DEDD2; FADD-like anti-apoptotic molecule 3; unnamed protein product
Gene Aliases: FLAME-3; FLAME3
UniProt ID: (Human) Q8WXF8
Entrez Gene ID: (Human) 162989
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