DAXX Antibody

Background

This antibody is designed, produced, and validated as part of a collaboration between Rockland and the National Cancer Institute (NCI). DAXX, the Death domain-associated protein 6, resides in multiple locations in the nucleus and in the cytoplasm and interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1. In the nucleus, DAXX functions as a potent transcription corepressor that binds to several sumoylated transcription factors. Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli through interactions with MCSR1 and PML. These interactions may regulate TNFRSF6-dependent apoptosis through the meditations of the activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination. DAXX acts as histone chaperone that facilitates deposition of histone H3.3. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Anti-DAXX Antibody is useful for researchers interested in Apoptosis, TGF-Beta, MAPK Signaling Pathway, Cancer, Immunology and Nuclear Signaling research.