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D7810

Sigma-Aldrich

Anti-Daxx antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-BING2, Anti-DAP6, Anti-EAP1, Anti-SMIM40

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 120 kDa

species reactivity

mouse, human, monkey

technique(s)

microarray: suitable
western blot: 1:4,000 using human acute lymphoma Jurkat whole cell extract

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DAXX(1616)
mouse ... Daxx(13163)

General description

Death domain associated protein (Daxx), also known as ETS associated protein 1 (EAP1), is an adaptor protein that binds to the death domain of Fas. Daxx is a 120 kDa protein with a nuclear localization signal sequence. It is highly acidic due to extended glutamic acid-rich domains. Daxx mRNA is extensively expressed in fetal and adult human and mouse tissues. Daxx has also been found in the nucleus where it localizes with the promyelocytic leukemia protein (PML), a gene of acute promyelocytic leukemia (APL).

Specificity

Anti-Daxx specifically recognizes human Daxx (120 kDa).

Immunogen

Synthetic peptide corresponding to the C-terminus of human Daxx. This sequence is identical in mouse and monkey.

Application

Anti-Daxx antibody is suitable for:
  • western blot (1:4,000 using human acute lymphoma Jurkat whole cell extract)
  • microarray
  • the detection and localization of Daxx by immunoblotting

Anti-Daxx antibody produced in rabbit has been used to visualize hDaxx.

Biochem/physiol Actions

The death domain-associated protein (Daxx) is a protein that interacts with FAS and subsequently regulates cellular apoptosis. Daxx also interacts with H3.3 histone and α-thalassemia X-linked mental retardation protein (ATRX) to regulate chromatin deposition at telomeres. In addition, it also acts as a pro-apoptotic molecule that can specifically enhance Fas-induced apoptosis by activating the Jun N-terminal kinase (JNK) signaling pathway, through its interaction with the apoptosis signal-regulating kinase 1 (ASK1).

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

IXO11097:
D7810-.2ML:
D7810-VAR:
D7810-BULK:


Certificates of Analysis (COA)

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Jonghwa Lee et al.
Life science alliance, 3(8) (2020-05-29)
Nuclear lipid droplets (nLDs) form on the inner nuclear membrane by a mechanism involving promyelocytic leukemia (PML), the protein scaffold of PML nuclear bodies. We report that PML structures on nLDs in oleate-treated U2OS cells, referred to as lipid-associated PML
Human cytomegalovirus immediate-early gene expression is restricted by the nuclear domain 10 component Sp100
Adler M, et al.
The Journal of General Virology, 92(7), 1532-1538 (2011)
The ?readers? of unacetylated p53 represent a new class of acidic domain proteins
Wang D, et al.
Nucleus (Austin, Tex.), 8(4), 360-369 (2017)
The replication defect of ICP0-null mutant herpes simplex virus 1 can be largely complemented by the combined activities of human cytomegalovirus proteins IE1 and pp71
Everett RD, et al.
Journal of virology, 87(2), 978-990 (2013)
Piia Kivipõld et al.
Virology journal, 12, 104-104 (2015-07-08)
The human papillomavirus (HPV) genomes can replicate, and are maintained as autonomously replicating extrachromosomal plasmids in human U2OS cells. Previous studies have shown that HPV genomes are transcriptionally active in U2OS cells and can express the viral early proteins required

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