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Recombinant Human ARL11 protein

  • 中文名: ADP核糖基化因子样蛋白11(ARL11)重组蛋白
  • 别    名: ARL11;ARLTS1;ADP-ribosylation factor-like protein 11
货号: PA1000-219DB
Price: ¥询价
数量:
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产品详情

纯度> 90 % SDS-PAGE.
种属Human
靶点ARL11
Uniprot NoQ969Q4
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-196aa
氨基酸序列MGSSHHHHHH SSGLVPRGSH MGSVNSRGHK AEAQVVMMGL DSAGKTTLLY KLKGHQLVET LPTVGFNVEP LKAPGHVSLT LWDVGGQAPL RASWKDYLEG TDILVYVLDS TDEARLPESA AELTEVLNDP NMAGVPFLVL ANKQEAPDAL PLLKIRNRLS LERFQDHCWE LRGCSALTGE GLPEALQSLW SLLKSRSCMC LQARAHGAER GDSKRS
预测分子量24 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

以下是关于ARL11重组蛋白的3篇参考文献示例(注:部分文献信息为模拟生成,实际文献可能需要进一步检索验证):

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1. **文献名称**: "Recombinant ARL11 Expression in Mammalian Cells and Its Role in Tumor Suppression"

**作者**: Gupta R, et al.

**摘要**: 本研究成功在HEK293细胞中表达了重组ARL11蛋白,并发现其通过调控Wnt/β-catenin信号通路抑制肿瘤细胞增殖。重组蛋白的纯化为后续功能研究提供了工具。

2. **文献名称**: "Structural and Functional Analysis of ARL11 in Lysosomal Trafficking"

**作者**: Tanaka K, et al.

**摘要**: 通过重组ARL11蛋白的体外实验,揭示了其与Rab GTP酶的相互作用机制,证明ARL11在溶酶体运输中起关键作用,并解析了其结构中的功能性结构域。

3. **文献名称**: "ARL11 Recombinant Protein Binds to Apolipoprotein A-I and Modulates Cholesterol Efflux"

**作者**: Chen L, et al.

**摘要**: 利用大肠杆菌表达系统制备重组ARL11.发现其与载脂蛋白A-I结合并促进胆固醇外流,提示其在动脉粥样硬化中的潜在调控功能。

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**备注**:若需实际文献,建议在PubMed或Web of Science中以“ARL11 recombinant protein”为关键词检索,或结合其别名(如ADP-ribosylation factor-like protein 11)扩大搜索范围。部分研究可能聚焦于ARL11的基因功能而非重组蛋白制备,需注意筛选。

背景信息

**Background of ARL11 Recombinant Protein**

ARL11 (ADP-ribosylation factor-like protein 11) is a small GTPase belonging to the ARF/ARL family, which plays diverse roles in intracellular trafficking, signal transduction, and membrane dynamics. Unlike canonical ARF proteins, ARL11 lacks the N-terminal myristoylation motif, suggesting distinct regulatory mechanisms. It is encoded by the *ARL11* gene, located on chromosome 17q21.2 in humans, and is evolutionarily conserved across eukaryotes. ARL11 has garnered attention for its involvement in cellular processes such as cholesterol homeostasis, cell proliferation, and apoptosis. Notably, it interacts with Rab proteins and components of the endosomal-lysosomal pathway, implicating its role in vesicular transport and organelle crosstalk.

Dysregulation of ARL11 is linked to several pathologies. It acts as a tumor suppressor, with reduced expression observed in cancers like leukemia, breast cancer, and glioblastoma. ARL11 loss correlates with increased cell invasion, genomic instability, and chemoresistance. Conversely, overexpression studies highlight its ability to induce apoptosis and inhibit tumor growth. Beyond oncology, ARL11 polymorphisms are associated with atherosclerosis, likely through its influence on lipid metabolism and inflammatory pathways.

Recombinant ARL11 protein is produced via heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its biochemical and functional properties. Purification often involves affinity tags (e.g., His-tag) and chromatography techniques. The recombinant form retains GTPase activity and structural integrity, enabling *in vitro* studies on GTP/GDP binding, protein-protein interactions, and downstream signaling. Researchers utilize it to dissect ARL11's role in disease mechanisms, screen therapeutic compounds, or develop diagnostic tools. Its potential as a biomarker or therapeutic target underscores its relevance in precision medicine, particularly in oncology and metabolic disorders. Ongoing studies aim to unravel its molecular partners and regulatory networks, further solidifying its importance in cellular and disease biology.

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