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Death-Domain Associated Protein (DAXX) antibody
|Synonyms||DAP6, EAP1, BING2, MGC126245, MGC126246, MGC150289, DAP-3, 4921514D13Rik, im:6905684, LOC100226911|
Alternatives ELISA, Immunofluorescence (IF), Flow Cytometry (FACS), Western Blotting (WB)
|1 reference available|
|Price||363.00 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 3 to 4 Business Days|
|Immunogen||Purified recombinant fragment of human DAXX expressed in E. Coli.|
DAXX (death-domain associated protein), it 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, the encoded 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, the encoded 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. Alternative splicing results in multiple transcript variants.
Synonyms: DAP6, EAP1, BING2
Western Blotting: 1/500 - 1/2000.
Immunofluorescence: 1/200 - 1/1000.
Flow cytometry: 1/200 - 1/400.
ELISA: Propose dilution 1/10000.
Not yet tested in other applications.
Determining optimal working dilutions by titration test.
|Purification||Protein G Affinity Chromatography|
|Buffer||PBS containing 50% glycerol and 0.03% sodium azide.|
|Preservative||0.03% sodium azide|
|Storage||Store at 4℃, for long term storage, store at -20℃.|
|Restrictions||For Research Use only|
Beausoleil, Jedrychowski, Schwartz et al.: "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).