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Recombinant Human DAXX protein

  • 中文名: 死亡结构域相关蛋白6(DAXX)重组蛋白
  • 别    名: DAXX;BING2;DAP6;Death domain-associated protein 6
货号: PA2000-3565
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点DAXX
Uniprot NoQ9UER7
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-740aa
氨基酸序列MATANSIIVLDDDDEDEAAAQPGPSHPLPNAASPGAEAPSSSEPHGARGS SSSGGKKCYKLENEKLFEEFLELCKMQTADHPEVVPFLYNRQQRAHSLFL ASAEFCNILSRVLSRARSRPAKLYVYINELCTVLKAHSAKKKLNLAPAAT TSNEPSGNNPPTHLSLDPTNAENTASQSPRTRGSRRQIQRLEQLLALYVA EIRRLQEKELDLSELDDPDSAYLQEARLKRKLIRLFGRLCELKDCSSLTG RVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAAARH SLGLPRQQLQLMAQDAFRDVGIRLQERRHLDLIYNFGCHLTDDYRPGVDP ALSDPVLARRLRENRSLAMSRLDEVISKYAMLQDKSEEGERKKRRARLQG TSSHSADTPEASLDSGEGPSGMASQGCPSASRAETDDEDDEESDEEEEEE EEEEEEEATDSEEEEDLEQMQEGQEDDEEEDEEEEAAAGKDGDKSPMSSL QISNEKNLEPGKQISRSSGEQQNKGRIVSPSLLSEEPLAPSSIDAESNGE QPEELTLEEESPVSQLFELEIEALPLDTPSSVETDISSSRKQSEEPFTTV LENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVE RQRSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCI PSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD
预测分子量108 kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是3篇与DAXX重组蛋白相关的参考文献(示例为模拟内容,实际文献需通过学术数据库检索):

1. **标题**: "Structural insights into DAXX interaction with histone H3.3"

**作者**: Smith J, et al.

**摘要**: 通过X射线晶体学解析了重组人DAXX蛋白与组蛋白变体H3.3的复合物结构,揭示了DAXX通过保守的α-螺旋结构域结合H3.3的分子机制,为染色质组装调控提供了结构基础。

2. **标题**: "Recombinant DAXX expression and its role in apoptosis regulation"

**作者**: Lee S, et al.

**摘要**: 报道了在大肠杆菌中高效表达并纯化具有活性的重组DAXX蛋白的方法,并证明其通过调控p53通路增强肿瘤细胞凋亡,提示其潜在抗癌应用价值。

3. **标题**: "DAXX phase separation mediated by its intrinsically disordered regions"

**作者**: Wang Y, et al.

**摘要**: 研究发现重组DAXX蛋白在体外可通过其内在无序区(IDR)发生液-液相分离(LLPS),这种相分离行为可能参与其在核小体组装和基因沉默中的功能。

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**提示**:实际文献可通过PubMed或Google Scholar以关键词 "DAXX recombinant protein"、"DAXX purification" 或 "DAXX structure/function" 检索,优先选择近5年且发表于高影响力期刊(如Nature, Cell, PNAS)的论文。

背景信息

**Background of DAXX Recombinant Protein**

DAXX (Death domain-associated protein 6), a multifunctional nuclear protein, plays critical roles in transcriptional regulation, chromatin remodeling, and apoptosis. Initially identified as a Fas death domain-binding protein, DAXX is involved in diverse cellular processes, including modulation of p53-dependent apoptosis, TGF-β signaling, and histone H3.3 incorporation into chromatin via its interaction with ATRX (α-thalassemia/mental retardation syndrome X-linked). Structurally, DAXX contains an N-terminal protein interaction domain and a C-terminal acidic region, facilitating interactions with partners like PML (promyelocytic leukemia protein) within nuclear subdomains called PML-NBs.

Recombinant DAXX protein is engineered to study its molecular mechanisms *in vitro* or in cell-based systems. Produced using bacterial or mammalian expression systems, it retains functional domains for binding partners, enzymatic assays, or structural studies. Its recombinant form is vital for investigating DAXX’s role in cancer (e.g., tumor suppression vs. oncogenic duality), neurodegeneration, and viral pathogenesis, where DAXX may act as a host defense factor. Researchers also utilize it to explore its chaperone function in depositing histone variants, epigenetic regulation, and responses to DNA damage.

The development of DAXX recombinant protein has advanced drug discovery, particularly in targeting DAXX-associated pathways in diseases like glioblastoma or leukemia. However, challenges remain in elucidating context-dependent roles of DAXX, necessitating high-purity, bioactive recombinant variants for precise biochemical and therapeutic studies.

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