Death-Domain Associated Protein (DAXX) (Ser495) Peptide

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Protein Name
  • im:6905684
  • LOC100226911
  • BING2
  • DAP6
  • EAP1
  • death associated protein 3
  • death-domain associated protein
  • Fas death domain-associated protein
  • dap3
  • LOC100226911
  • DAP3
  • DAXX
  • Daxx
Protein Region
Peptide Type
Blocking Peptide (BP)
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Specificity The synthetic peptide sequence used to generate the antibody AP7773a was selected from the S495 region of humanXX. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Background DAXX is a multifunctional protein that resides in multiple locations in the nucleus and in the cytoplasm. It 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, this protein functions as a potent transcription repressor that binds to sumoylated transcription factors. Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli. This protein also associates with centromeres in G2 phase. In the cytoplasm, this protein may function to regulate apoptosis. The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination.
Restrictions For Research Use only
Storage 4
Storage Comment Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles
Expiry Date 6 months
Background publications Cantrell, Bresnahan: "Interaction between the human cytomegalovirus UL82 gene product (pp71) and hDaxx regulates immediate-early gene expression and viral replication." in: Journal of virology, Vol. 79, Issue 12, pp. 7792-802, 2005 (PubMed).

Greger, Katz, Ishov, Maul, Skalka: "The cellular protein daxx interacts with avian sarcoma virus integrase and viral DNA to repress viral transcription." in: Journal of virology, Vol. 79, Issue 8, pp. 4610-8, 2005 (PubMed).

Chang, Lin, Fang, Chen, Shih: "Daxx mediates the small ubiquitin-like modifier-dependent transcriptional repression of Smad4." in: The Journal of biological chemistry, Vol. 280, Issue 11, pp. 10164-73, 2005 (PubMed).

Beausoleil, Jedrychowski, Schwartz, Elias, Villén, Li, Cohn, Cantley, Gygi: "Large-scale characterization of HeLa cell nuclear phosphoproteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 101, Issue 33, pp. 12130-5, 2004 (PubMed).

Gostissa, Morelli, Mantovani, Guida, Piazza, Collavin, Brancolini, Schneider, Del Sal: "The transcriptional repressor hDaxx potentiates p53-dependent apoptosis." in: The Journal of biological chemistry, Vol. 279, Issue 46, pp. 48013-23, 2004 (PubMed).