Anti-Daxx 抗体 (ab2017)
Key features and details
- Rabbit polyclonal to Daxx
- Suitable for: ICC/IF
- Reacts with: Human
- Isotype: IgG
製品の概要
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製品名
Anti-Daxx antibody
Daxx 一次抗体 製品一覧 -
製品の詳細
Rabbit polyclonal to Daxx -
由来種
Rabbit -
アプリケーション
適用あり: ICC/IFmore details -
種交差性
交差種: Human -
免疫原
Synthetic peptide corresponding to Human Daxx aa 722-740.
Sequence:TSVATQCDPEEIIVLSDSD
(Peptide available asab7879) -
特記事項
The Life Science industry has been in the grips of a reproducibility crisis for a number of years. Abcam is leading the way in addressing this with our range of recombinant monoclonal antibodies and knockout edited cell lines for gold-standard validation. Please check that this product meets your needs before purchasing.
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製品の特性
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製品の状態
Liquid -
保存方法
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. -
バッファー
pH: 7.2
Preservative: 0.02% Sodium azide -
Concentration information loading...
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精製度
DEAE-Chromatography -
ポリ/モノ
ポリクローナル -
アイソタイプ
IgG -
研究分野
関連製品
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Compatible Secondaries
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Isotype control
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Recombinant Protein
アプリケーション
The Abpromise guarantee
Abpromise保証は、 次のテスト済みアプリケーションにおけるab2017の使用に適用されます
アプリケーションノートには、推奨の開始希釈率がありますが、適切な希釈率につきましてはご検討ください。
アプリケーション | Abreviews | 特記事項 |
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ICC/IF |
Use a concentration of 10 µg/ml.
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特記事項 |
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ICC/IF
Use a concentration of 10 µg/ml. |
ターゲット情報
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機能
Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as histone chaperone that facilitates deposition of histone H3.3. Acts as targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. In case of overexpression of centromeric histone variant CENPA (as found in various tumors) is involved in its mislocalization to chromosomes; the ectopic localization involves a heterotypic tetramer containing CENPA, and histones H3.3 and H4 and decreases binding of CTCF to chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Shows restriction activity towards human cytomegalovirus (HCMV). -
組織特異性
Ubiquitous. -
配列類似性
Belongs to the DAXX family. -
ドメイン
The Sumo interaction motif mediates Sumo binding, and is required both for sumoylation and binding to sumoylated targets. -
翻訳後修飾
Sumoylated with SUMO1 on multiple lysine residues.
Phosphorylated by HIPK1 upon glucose deprivation.
Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it. -
細胞内局在
Nucleus. Diffuse nuclear distribution pattern and no comparable dot-like accumulation of isoform 1 and Cytoplasm. Nucleus, nucleoplasm. Nucleus, PML body. Nucleus, nucleolus. Chromosome, centromere. Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli (Probable). Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies (PubMed:12953102, PubMed:14990586, PubMed:23222847, PubMed:24200965). Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres (PubMed:9645950). Detected in cytoplasmic punctate structures (PubMed:11842083). Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress (PubMed:12968034). Colocalizes with RASSF1 in the nucleus (PubMed:18566590). Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures (PubMed:16845383). - Information by UniProt
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参照データベース
- Entrez Gene: 1616 Human
- Omim: 603186 Human
- SwissProt: Q9UER7 Human
- Unigene: 336916 Human
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別名
- BING 2 antibody
- BING2 antibody
- CENP-C binding protein antibody
see all
データシートおよび資料
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SDS download
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Datasheet download
参考文献 (2)
ab2017 は 2 報の論文で使用されています。
- Lee JS & Zhang Z O-linked N-acetylglucosamine transferase (OGT) interacts with the histone chaperone HIRA complex and regulates nucleosome assembly and cellular senescence. Proc Natl Acad Sci U S A 113:E3213-20 (2016). PubMed: 27217568
- Dionne KR et al. Daxx upregulation within the cytoplasm of reovirus-infected cells is mediated by interferon and contributes to apoptosis. J Virol 87:3447-60 (2013). PubMed: 23302889