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rabbit anti-Daxx (CT) polyclonal antibody 8072


Antibody summary

  • Rabbit polyclonal to Daxx (CT)
  • Suitable for: ELISA,WB,IHC-P,IF,IP
  • Isotype: IgG
  • 100 µg
SKU: 8072parent Category: Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in







1 mg/mL




Daxx (CT)

available sizes

100 µg

Available product – rabbit anti-Daxx (CT) polyclonal antibody 8072

Tested applications
Recommended dilutions
Immunoblotting: use at 1:500-1:1,000 dilution.

Immunocytochemistry: use at 10ug/mL.

These are recommended concentrations.

Enduser should determine optimal concentrations for their applications.

Positive control: Whole cell lysate from HeLa cells.
Peptide corresponding to aa 722- 740 at the C-terminus of human Daxx (accession no. CAG33366).
Size and concentration
100µg and lot specific
Storage Instructions
This antibody is stable for at least one (1) year at -20°C. Avoid multiple freeze-thaw cycles.
Storage buffer
PBS, pH 7.4.
peptide affinty purifcation
Compatible secondaries
goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863
goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control
Rabbit polyclonal - Isotype Control
target relevance
Protein names
Death domain-associated protein 6 (Daxx) (hDaxx) (ETS1-associated protein 1) (EAP1) (Fas death domain-associated protein)
Gene names
Protein family
DAXX family
FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. 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. Proposed to mediate 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. Shows restriction activity towards human cytomegalovirus (HCMV). Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (PubMed:15016915). {ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:15364927, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17081986, ECO:0000269|PubMed:17942542, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:24530302}.
Subellular location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11495919, ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:9407001}. Nucleus, nucleoplasm {ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:9407001}. Nucleus, PML body {ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:17081986, ECO:0000269|PubMed:21482821, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:25275136}. Nucleus, nucleolus {ECO:0000269|PubMed:23222847}. Chromosome, centromere {ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:9645950}. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli (Probable). Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies (PubMed:12953102, PubMed:14990586, PubMed:23222847, PubMed:24200965). Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres (PubMed:9645950). Detected in cytoplasmic punctate structures (PubMed:11842083). Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress (PubMed:12968034). Colocalizes with RASSF1 in the nucleus (PubMed:18566590). Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures (PubMed:16845383). {ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:23222847, ECO:0000269|PubMed:24200965, ECO:0000269|PubMed:9645950, ECO:0000305|PubMed:10669754}.; SUBCELLULAR LOCATION: [Isoform beta]: Nucleus {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1. {ECO:0000269|PubMed:21482821}.; SUBCELLULAR LOCATION: [Isoform gamma]: Nucleus {ECO:0000269|PubMed:21482821}. Note=Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1. {ECO:0000269|PubMed:21482821}.
SUBUNIT: Homomultimer. Interacts (via C-terminus) with TNFRSF6 (via death domain). Interacts with PAX5, SLC2A4/GLUT4, MAP3K5, TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC, ETS1, sumoylated PML, UBE2I, MCRS1 and TP53. Interacts (via N-terminus) with HIPK2 and HIPK3. Interacts with HIPK1, which induces translocation from PML/POD/ND10 nuclear bodies to chromatin and enhances association with HDAC1. Interacts (non-phosphorylated) with PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4 and histones H2A, H2B, H3, H3.3 and H4. Interacts with SPOP; mediating CUL3-dependent proteasomal degradation. Interacts with CBP; the interaction is dependent the sumoylation of CBP and suppresses CBP transcriptional activity via recruitment of HDAC2 directly in the complex with TP53 and HIPK2. Interacts with AXIN1; the interaction stimulates the interaction of DAXX with TP53, stimulates 'Ser-46' phosphorylation of TP53 on and induces cell death on UV irradiation. Interacts with MDM2; the interaction is direct. Interacts with USP7; the interaction is direct and independent of MDM2 and TP53. Part of a complex with DAXX, MDM2 and USP7 under non-stress conditions. Interacts (via N-terminus) with RASSF1 (via C-terminus); the interaction is independent of MDM2 and TP53; RASSF1 isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage. Interacts with ATRX to form the chromatin remodeling complex ATRX:DAXX. Interacts with HSF1 (via homotrimeric form preferentially); this interaction relieves homotrimeric HSF1 from repression of its transcriptional activity by HSP90-dependent multichaperone complex upon heat shock (PubMed:15016915). Interacts with SUMO1P1/SUMO5 (PubMed:27211601). {ECO:0000269|PubMed:10393185, ECO:0000269|PubMed:10669754, ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:11003656, ECO:0000269|PubMed:11483955, ECO:0000269|PubMed:11495919, ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:11948183, ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:12953102, ECO:0000269|PubMed:12968034, ECO:0000269|PubMed:14678985, ECO:0000269|PubMed:14990586, ECO:0000269|PubMed:15016915, ECO:0000269|PubMed:15240113, ECO:0000269|PubMed:15364927, ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:16845383, ECO:0000269|PubMed:17210684, ECO:0000269|PubMed:18566590, ECO:0000269|PubMed:20444888, ECO:0000269|PubMed:20504901, ECO:0000269|PubMed:20651253, ECO:0000269|PubMed:21134643, ECO:0000269|PubMed:23075851, ECO:0000269|PubMed:23142979, ECO:0000269|PubMed:27211601, ECO:0000269|PubMed:9645950}.; SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus/HHV-5 tegument phosphoprotein pp71 and protein UL123. {ECO:0000269|PubMed:18922870}.; SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus protein BNRF1. {ECO:0000269|PubMed:25275136}.; SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 E1B-55K protein; this interaction might alterate the normal interactions of DAXX, PML, and TP53, which may contribute to cell transformation. {ECO:0000269|PubMed:14557665}.; SUBUNIT: (Microbial infection) Interacts with Puumala hantavirus nucleoprotein. {ECO:0000269|PubMed:11907324}.
Post-translational modification
PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000269|PubMed:11842083, ECO:0000269|PubMed:12150977, ECO:0000269|PubMed:17081986}.; PTM: Phosphorylated by HIPK1 upon glucose deprivation. {ECO:0000269|PubMed:10393185, ECO:0000269|PubMed:12140263, ECO:0000269|PubMed:12968034}.; PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it. {ECO:0000269|PubMed:16524876, ECO:0000269|PubMed:20153724}.
Target Relevance information above includes information from UniProt accession : Q9UER7
The UniProt Consortium


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Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.



relevant to this product
Western blot


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