DAXX

The following DAXX reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

DAXX Antibodies

DAXX Antibodies for Homo sapiens (Human)

DAXX Proteins

DAXX Proteins for Mus musculus (Mouse)

DAXX Proteins for Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)

DAXX Proteins for Canis lupus familiaris (Dog) (Canis familiaris)

DAXX Proteins for Rattus norvegicus (Rat)

DAXX Proteins for Homo sapiens (Human)

DAXX Background

Death domain-associated protein 6 (DAXX) is a highly conserved nuclear protein involved in apoptosis, transcriptional repression, and embryonic development. It possesses a Ser/Pro/Thr-rich domain, an acidic domain, a coiled-coil region, and two paired amphipathic helices [1]. Fas-receptor stimulation causes DAXX to translocate out of the nucleus and into the cytoplasm. DAXX combines with Fas to transmit a Fas-associated death domain (FADD)-independent apoptotic signal by activating Jun N-terminal kinase (JNK) [2]. DAXX also mediates UV-induced JNK activation and apoptosis [3]. Apoptosis signal-regulating kinase 1 (Ask1) can translocate DAXX to the cytoplasm. The binding of DAXX and Ask1 may relieve an intramolecular interaction between the amino- and carboxyl-termini of Ask1, activating its kinase activity [4][5]. This a mitogen-activated protein kinase kinase kinase subsequently activates JNK. The promotion of Ask1-mediated apoptosis through DAXX is in a kinase- and caspase-independent manner [6]. Targeted ablation in the mouse unveiled that DAXX is essential for embryonic development [7]. As a component of promyelocytic leukemia protein-nuclear bodies (PML-NBs), DAXX interacts with PML in the mediation of the antiviral defense [8][9]. And DAXX also functions as a transcriptional regulator possessing transcriptional repression activity and interacts directly with several transcription factors such as Pax3/5 and Smad4 (5, 6) [10][11]. Besides, Pascal Drane´ and Khalid Ouararhni et al. identified that DAXX serves as a chaperone taking part in the replication-independent deposition of H3.3, one of the best-studied histone variants which can replace the major species, H3.1 [12].

[1] Kiriakidou, M., D. A. Driscoll, et al. Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region [J]. DNA Cell Biol. 1997, 16:1289-1298.
[2] Yang, X., R. Khosravi-Far, et al. Daxx, a novel Fas-binding protein that activates JNK and apoptosis [J]. Cell 1997, 89:1067-1076.
[3] Wu, S., H. N. Loke, and A. Rehemtulla. Ultraviolet radiation-induced apoptosis is mediated by Daxx [J]. Neoplasia 2002, 4:486-492.
[4] Chang, H. Y., H. Nishitoh, et al. Activation of apoptosis signal- regulating kinase 1 (ASK1) by the adapter protein daxx [J]. Science, 1998, 281:1860-1863.
[5] Ko, Y. G., Y. S. Kang, et al. Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm [J]. J. Biol. Chem. 2001, 276:39103-39106.
[6] Charette, S. J., H. Lambert, and J. Landry. 2001. A kinase-independent function of Ask1 in caspase-independent cell death [J]. J. Biol. Chem. 276:36071-4.
[7] Jennifer S Michaelson, Philip Leder. RNAi reveals anti-apoptotic and transcriptionally repressive activities of DAXX [J]. J Cell Sci. 2003 Jan 15;116(Pt 2):345-52.
[8] Ullman A. J., Hearing P. Cellular proteins PML and Daxx mediate an innate antiviral defense antagonized by the adenovirus E4 ORF3 protein [J]. J. Virol. 2008, 82, 7325–7335.
[9] Saffert R. T., Kalejta R. F. Inactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expression [J]. J. Virol. 2006, 80, 3863–3871.
[10] Lehembre F., Müller S., et al. Regulation of Pax3 transcriptional activity by SUMO-1-modified PML [J]. Oncogene 2001, 20, 1–9.
[11] Chang C. C., Lin D. Y., et al. Daxx mediates the small ubiquitin-like modifier-dependent transcriptional repression of Smad4 [J]. J. Biol. Chem. 2005, 280, 10164–10173.
[12] Pascal Drane´, Khalid Ouararhni, et al. The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3 [J]. Genes Dev. 2010 Jun 15; 24(12): 1253–1265.

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