D7810
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
Recommended Products
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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Product No.
Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
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)
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
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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