Daxx Antibody [H1F20] | Primary Antibodies

Application: Reactivity: Human, Mouse, Rat

Lane 1: K562, Lane 2: A20, Lane 3: PC12

Usage Information

Dilution
WB1:1000 IF1:25

Application
WB, IF

Reactivity
Human, Mouse, Rat

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
110 kDa

Positive Control	K562 cells; A20 cells; PC12 cells; HeLa cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Daxx Antibody [H1F20] detects endogenous levels of total Daxx protein.

Clone
H1F20

Synonym(s)
DAXX; Death domain-associated protein 6; Daxx (hDaxx); ETS1-associated protein 1 (EAP1); Fas death domain-associated protein; BING2; DAP6

Background
Daxx (Death domain-associated protein) is a ubiquitously expressed nuclear scaffold protein, initially identified as a Fas-interactor, that primarily localizes to promyelocytic leukemia nuclear bodies (PML-NBs) and is essential for chromatin remodeling, transcriptional regulation, and apoptosis modulation; knockout of Daxx in mice leads to embryonic lethality due to excessive developmental apoptosis. Daxx contains an N-terminal helical bundle (4HB) domain that mediates interactions with partners such as ATRX, p53, and MDM2; a central H3.3/H4-binding region that folds with histone dimers to function as an H3.3-specific chaperone, depositing H3.3 at PML-NBs and telomeres; poly-Asp/Glu (polyD/E) motifs that sense misfolded proteins and facilitate their refolding; two SUMO-interaction motifs (SIMs) that regulate sumoylation and PML-NB targeting; and a C-terminal domain that associates with Fas, CENP-C, and DNA methyltransferases. Daxx facilitates ATRX-dependent H3.3 deposition for heterochromatin silencing and telomere maintenance, assembles the telomerase holoenzyme in Cajal bodies via N-terminal interactions with TERT subunits (DKC1, GAR1, NHP2) to promote telomerase targeting and prevent telomere shortening, represses transcription of NF-κB and E2F-1 targets through HDAC recruitment and PML-NB scaffolding, modulates apoptosis via Fas/JNK activation while exhibiting anti-apoptotic effects during development, and responds to cellular stress by binding misfolded proteins to maintain proteostasis. Disease-associated mutations in Daxx disrupt binding to partners, such as impairing H3.3/ATRX-mediated deposition or blocking telomerase assembly via N-terminal lesions, while post-translational sumoylation enhances PML targeting, phosphorylation modulates subnuclear localization, and interactions with HIPK2 and TGF-β pathways integrate signals for cell cycle control and survival. Dysregulation of Daxx contributes to cancer through H3.3 perturbations that promote oncogene expression, to alpha-thalassemia syndromes via ATRX mutations, and to neurodegenerative diseases due to failures in proteostasis.

Background

Daxx (Death domain-associated protein) is a ubiquitously expressed nuclear scaffold protein, initially identified as a Fas-interactor, that primarily localizes to promyelocytic leukemia nuclear bodies (PML-NBs) and is essential for chromatin remodeling, transcriptional regulation, and apoptosis modulation; knockout of Daxx in mice leads to embryonic lethality due to excessive developmental apoptosis. Daxx contains an N-terminal helical bundle (4HB) domain that mediates interactions with partners such as ATRX, p53, and MDM2; a central H3.3/H4-binding region that folds with histone dimers to function as an H3.3-specific chaperone, depositing H3.3 at PML-NBs and telomeres; poly-Asp/Glu (polyD/E) motifs that sense misfolded proteins and facilitate their refolding; two SUMO-interaction motifs (SIMs) that regulate sumoylation and PML-NB targeting; and a C-terminal domain that associates with Fas, CENP-C, and DNA methyltransferases. Daxx facilitates ATRX-dependent H3.3 deposition for heterochromatin silencing and telomere maintenance, assembles the telomerase holoenzyme in Cajal bodies via N-terminal interactions with TERT subunits (DKC1, GAR1, NHP2) to promote telomerase targeting and prevent telomere shortening, represses transcription of NF-κB and E2F-1 targets through HDAC recruitment and PML-NB scaffolding, modulates apoptosis via Fas/JNK activation while exhibiting anti-apoptotic effects during development, and responds to cellular stress by binding misfolded proteins to maintain proteostasis. Disease-associated mutations in Daxx disrupt binding to partners, such as impairing H3.3/ATRX-mediated deposition or blocking telomerase assembly via N-terminal lesions, while post-translational sumoylation enhances PML targeting, phosphorylation modulates subnuclear localization, and interactions with HIPK2 and TGF-β pathways integrate signals for cell cycle control and survival. Dysregulation of Daxx contributes to cancer through H3.3 perturbations that promote oncogene expression, to alpha-thalassemia syndromes via ATRX mutations, and to neurodegenerative diseases due to failures in proteostasis.

References
https://pubmed.ncbi.nlm.nih.gov/37633949/ https://pubmed.ncbi.nlm.nih.gov/31350900/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%