Recombinant Human Death domain-associated protein 6 (DAXX), partial

Code CSB-RP012444h
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
BING 2; BING2; CENP-C binding protein; DAP 6; DAP6; Daxx; DAXX_HUMAN; Death associated protein 6; Death domain associated protein 6; Death domain associated protein; Death domain-associated protein 6; EAP 1; EAP1; ETS1 associated protein 1; ETS1-associated protein 1; Fas binding protein; Fas death domain associated protein; Fas death domain-associated protein; hDaxx; MGC126245; MGC126246
Homo sapiens (Human)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
Protein Length
Tag Info
N-terminal GST-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

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 histone chaperone that facilitates deposition of histone H3.3. Acts as 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.
Gene References into Functions
  1. Data show that phosphatase and tensin homolog (PTEN) interacts with death domain associated protein (DAXX) and, in turn PTEN directly regulates oncogene expression by modulating DAXX-histone H3.3 (H3.3) association on the chromatin. PMID: 28497778
  2. Daxx directly binds to the DNA-binding domain of Slug, impeding histone deacetylase 1 (HDAC1) recruitment and antagonizing Slug E-box binding. This, in turn, stimulates E-cadherin and occludin expression and suppresses Slug-mediated epithelial-mesenchymal transition (EMT) and cell invasiveness. PMID: 28004751
  3. Results show that the X-linked nuclear protein (ATRX)-Fas death domain-associated protein (DAXX) complex is involved in gene repression and telomere chromatin structure. PMID: 29084956
  4. disruption of CENP-B/Daxx-dependent H3.3 pathway deregulates heterochromatin marks H3K9me3, ATRX and HP1alpha at centromeres and elevates chromosome instability PMID: 29273057
  5. Disrupting the ATRX/DAXX complex and inhibiting telomerase activity in telomerase-positive cancer cells lead to the alternative lengthening of telomeres switch. PMID: 27578458
  6. Study found that enhanced nuclear accumulation of Daxx correlated with the malignant phenotype in gastric mucosa. PMID: 28812328
  7. ATRX or DAXX loss was proved to be an independent predictor for OS of PanNETs in a multivariate Cox regression analysis including well-established risk factors; tumor stage and tumor grade. PMID: 28591701
  8. Both primary Alternative lengthening of telomeres(ALT) -positive and ATRX/DAXX-negative PanNETs are independently associated with aggressive clinicopathologic behavior and displayed reduced recurrence-free survival. In contrast, ALT activation and loss of ATRX/DAXX are both associated with better overall survival in patients with metastases PMID: 27663587
  9. Whole-exome sequencing has identified recurrent mutations in the genes DAXX and ATRX, which correlate with loss of protein expression and alternative lengthening of telomeres (ALT).ALT and DAXX/ATRX loss in PanNETs was associated with shorter disease-free survival (DFS) and disease-specific survival (DSS) and likely plays a significant role in driving metastatic disease PMID: 27407094
  10. We propose that mutations in alpha thalassemia-mental retardation syndrome X-linked (ATRX)/death-domain associated protein (DAXX) prime alternative lengthening of telomeres activation by disrupting telomeric heterochromatin. PMID: 28741530
  11. Structural and biochemical characterization of DAXX-ATRX interaction. PMID: 28875283
  12. Structural basis for DAXX interaction with ATRX. PMID: 28875424
  13. Given the high frequency of ATRX and DAXX mutations in cancer, these chromatin regulators likely play a key role in pathogenesis [review] PMID: 28062559
  14. H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements. PMID: 28334823
  15. DAXX gene plays a role in the pathogenesis of neuroendocrine pancreatic neoplasms. PMID: 28371511
  16. The widespread dynamic nature of DAXX methylation in association with trophoblast differentiation and placenta-associated pathologies is consistent with an important role for this gene in proper placental development and function. PMID: 28223336
  17. findings reveal a previously unappreciated cross-talk between two crucial tumor suppressor genes, MEN1 and DAXX, thought to work by independent pathways PMID: 27872097
  18. The interaction of Daxx C-terminal domain and androgen receptor suppresses cholesterol synthesis.Daxx C-terminal domain binds directly to androgen receptor. PMID: 27671201
  19. HDAC1 and DAXX are co-repressors associated with epigenetic regulation that help to control promoter histone acetylation reactions involved in regulating GAD67. PMID: 26812044
  20. We provide an overview of the individual components (ATRX, DAXX and/or H3.3) tested in each study and propose a model where the ATRX/DAXX chaperone complex deposits H3.3 to maintain the H3K9me3 modification at heterochromatin throughout the genome. PMID: 26773061
  21. Daxx and Atrx safeguard the genome by silencing repetitive elements when DNA methylation levels are low. PMID: 26340527
  22. Studies of the dynamics of the response of PML nuclear body components and IFI16 to invading herpes simplex virus 1 genomes demonstrated that human Daxx (hDaxx) and IFI16 respond more rapidly than PML. PMID: 26468536
  23. identifying Daxx as a broad cellular inhibitor of reverse-transcription. Altogether, these findings unravel a novel antiviral function for PML and PML nuclear body-associated protein Daxx PMID: 26566030
  24. PML, hDaxx and Sp100 primarily act as cellular restriction factors during lytic human cytomegalovirus replication and during the dynamic process of reactivation but do not serve as key determinants for the establishment of latency. PMID: 26057166
  25. ATRX- and DAXX-deficient PNETs have distinct genome-wide DNA methylation profiles. Loss of DAXX and not ATRX appears to be the driver event in altering genome-wide methylation changes in PNETs. PMID: 25900181
  26. These findings collectively support a DAXX-centric pathway for telomere maintenance, where DAXX interaction with the telomerase regulates telomerase assembly in Cajal bodies and telomerase targeting to telomeres. PMID: 25416818
  27. Knock-down of the cellular DAXX protein modulates the human papillomavirus genome replication and transcription in U2OS cells--papillomavirus replication is reduced in the absence of this component of ND10. PMID: 26148509
  28. establish DAXX as a pro-survival protein in PCa and reveal that, in the early stages of tumorigenesis, autophagy suppresses prostate tumor formation. PMID: 25903140
  29. Daxx downregulation should be essentially needed for the increase of anti-tumor activity through enhancement of viral replication and cellular arrest with the combination of TRAIL/shBcl-xL-induced apoptosis and oncolytic adenovirus. PMID: 25748050
  30. ATM kinase and Wip1 phosphatase were identified as opposing regulators of DAXX-S564 phosphorylation and the role of DAXX phosphorylation and DAXX itself are independent of p53-mediated gene expression. PMID: 25659035
  31. In neuroblastoma, alternative lengthening of telomere was caused by ATRX or DAXX gene alterations. PMID: 25487495
  32. Methylation changes were enriched in MSX1, CCND2, and DAXX at specific loci within the hippocampus of patients with schizophrenia and bipolar disorder. PMID: 25738424
  33. DAXX expression not lost in ileal neuroendocrine tumors PMID: 25439321
  34. Cytoplasmic localization of DAXX can increase injury sensitivity of ox-LDL on cells, and nuclear localization can antagonise the effect of ox-LDL. PMID: 25120166
  35. A higher number of gene mutations and the DAXX/ATRX and KRAS gene mutations are correlated with a poor prognosis of Chinese patients with pancreatic neuroendocrine tumors. PMID: 25210493
  36. Daxx protein interacts with HPV16 E2 protein, mainly in cytoplasm. PMID: 25842852
  37. Authors propose that Epstein-Barr virus tegument protein BNRF1 replaces ATRX to reprogram Daxx-mediated H3.3 loading, in turn generating chromatin suitable for latent gene expression. PMID: 25275136
  38. DENV C disrupts Daxx and NF-kappaB interaction to induce CD137-mediated apoptosis during DENV infection PMID: 25019989
  39. Urothelial carcinoma DAXX expression could be used in clinical practice as a marker of aggressiveness. PMID: 23819605
  40. In the progress of the cervical cancer, Daxx gradually translocates from nucleus into nuclear membrane, cytoplasm and cell membrane. PMID: 24398161
  41. DAXX has a role in misregulation of localization of the centromeric histone variant CenH3/CENP-A PMID: 24530302
  42. Loss of DAXX or ATRX is associated with chromosome instability in pancreatic neuroendocrine tumors and shorter survival times of patients. PMID: 24148618
  43. The status of ATRX or DAXX protein loss in neuroendocrine tumor differed among the organs in which these tumors arose, and these proteins may play site-specific roles in the development of these tumors. PMID: 23954140
  44. Overexpression of the chromatin remodeler death-domain-associated protein in prostate cancer is an independent predictor of early prostate-specific antigen recurrence. PMID: 23642739
  45. DAXX silencing suppresses mouse ovarian surface epithelial cell growth by inducing senescence and DNA damage. PMID: 23542781
  46. USP7 and Daxx are necessary to regulate proper execution of mitosis, partially via regulation of CHFR and Aurora-A kinase stability. PMID: 23348568
  47. The results suggest that hantavirus infection interferes with DAXX-mediated apoptosis, and expression of interferon-activated Sp100 and ISG-20 proteins may indicate intracellular intrinsic antiviral attempts. PMID: 23830076
  48. We demonstrate a specific role of DAXX, independently of ATRX, in the recruitment of H3.3 to PML bodies, in a process that can be facilitated by ASF1A. PMID: 23222847
  49. Data suggest that the pro-apoptotic protein Daxx specifically interacts with one or more substrates SUMOylated by PIAS1 and this interaction leads to apoptosis following UV irradiation. PMID: 22976298
  50. M1 prevents repressional function of Daxx during infection, thereby exerting a survival role PMID: 23548901

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Subcellular Location
Cytoplasm. Nucleus, nucleoplasm. Nucleus, PML body. Nucleus, nucleolus. Chromosome, centromere.; [Isoform beta]: Nucleus.; [Isoform gamma]: Nucleus.
Protein Families
DAXX family
Tissue Specificity
Database Links

HGNC: 2681

OMIM: 603186

KEGG: hsa:1616

STRING: 9606.ENSP00000266000

UniGene: Hs.336916

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