Recombinant human DEDD protein

MGSSHHHHHH SSGLVPRGSH MAGLKRRASQ VWPEEHGEQE HGLYSLHRMF DIVGTHLTHR DVRVLSFLFV DVIDDHERGL IRNGRDFLLA LERQGRCDES NFRQVLQLLR IITRHDLLPY VTLKRRRAVC PDLVDKYLEE TSIRYVTPRA LSDPEPRPPQ PSKTVPPHYP VVCCPTSGPQ MCSKRPARGR ATLGSQRKRR KSVTPDPKEK QTCDIRLRVR AEYCQHETAL QGNVFSNKQD PLERQFERFN QANTILKSRD LGSIICDIKF SELTYLDAFW RDYINGSLLE ALKGVFITDS LKQAVGHEAI KLLVNVDEED YELGRQKLLR NLMLQALP

Death effector domain-containing protein, also known as DEDD, is a cytoplasmic protein. It translocates to the nucleus during CD95-mediated apoptosis, where it localizes to nucleoli-like structures, activates caspase-6 and specifically inhibits RNA polymerase I-dependent transcription. The cell death activity of DEDD relates to its nuclear localization. DEDD is widely expressed in a variety of tissues, with highest levels in the testis. Overexpression of this gene was shown to induce weak apoptosis. Recombinant human DEDD protein, fused to His-tag at N-terminus, was expressed in E. coli.

E.coli

Apoptosis

38.9 kDa (338aa)