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Recombinant Human PLD4 protein

  • 中文名: 5'-3'核酸外切酶PLD4(PLD4)重组蛋白
  • 别    名: PLD4;C14orf175;5'-3' exonuclease PLD4
货号: PA2000-3282
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点PLD4
Uniprot No Q96BZ4
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 52-506aa
氨基酸序列WQVPRPPTWGQVQPKDVPRSWEHGSSPAWEPLEAEARQQRDSCQLVLVESIPQDLPSAAGSPSAQPLGQAWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVATSSPTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQVKELGAVIYNCSHLAQDLEKTFQTYWVLGVPKAVLPKTWPQNFSSHFNRFQPFHGLFDGVPTTAYFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDNALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSNIPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQSPGAQPAGATVQEQLRQLFERDWSSRYAVGLDGQAPGQDCVWQG
预测分子量 66.0 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PLD4重组蛋白的模拟参考文献示例,格式包含文献名称、作者及摘要概括:

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1. **"Recombinant Expression and Enzymatic Characterization of Human Phospholipase D4 (PLD4)"**

*Authors: Yamaguchi T, Sato H, et al.*

**摘要**:本研究成功克隆了人源PLD4基因,并在大肠杆菌系统中实现可溶性重组表达。通过亲和层析纯化后,体外酶活实验表明重组PLD4具有水解磷脂酰胆碱的活性,且其活性依赖二价金属离子(如Mg²⁺)。该研究为PLD4的生化特性分析提供了基础工具。

2. **"PLD4 Regulates Toll-like Receptor Signaling in Dendritic Cells via Recombinant Protein Functional Analysis"**

*Authors: Lee SJ, Kim M, et al.*

**摘要**:通过哺乳动物细胞表达系统制备重组PLD4蛋白,研究发现其通过调控TLR9信号通路抑制树突状细胞的过度活化。实验表明,PLD4可能通过降解特定核酸分子负向调节免疫反应,为自身免疫疾病治疗提供了潜在靶点。

3. **"Crystal Structure of the Catalytic Domain of PLD4 Reveals Unique Substrate Binding Sites"**

*Authors: Smith RA, Johnson EP, et al.*

**摘要**:本研究解析了重组PLD4蛋白催化结构域的X射线晶体结构(分辨率2.8Å),发现其拥有区别于PLD家族其他成员(如PLD1/2)的底物结合口袋。结构分析结合突变实验揭示了PLD4对特定磷脂底物的选择性机制。

4. **"PLD4 Recombinant Protein Attenuates Amyloid-β Aggregation in Alzheimer's Disease Models"**

*Authors: Chen L, Wang X, et al.*

**摘要**:利用昆虫细胞表达系统制备高纯度PLD4重组蛋白,体外实验表明其可通过水解磷脂调控淀粉样蛋白β(Aβ)的聚集。动物模型实验进一步显示,PLD4过表达能减少脑内Aβ斑块沉积,提示其在神经退行性疾病中的潜在治疗价值。

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*注:以上文献为模拟示例,实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。*

背景信息

**Background of PLD4 Recombinant Protein**

Phospholipase D4 (PLD4), a member of the phospholipase D (PLD) superfamily, is a transmembrane glycoprotein implicated in diverse cellular processes. Unlike canonical PLD enzymes (e.g., PLD1/2) that hydrolyze phosphatidylcholine to generate phosphatidic acid (PA), PLD4 lacks intrinsic phospholipase activity but shares structural homology with the PLD family. Recent studies suggest it may function as a 5'-exonuclease or interact with nucleic acids, linking it to immune regulation and nucleic acid metabolism. PLD4 is predominantly expressed in immune cells, including macrophages, dendritic cells, and microglia, where it may modulate inflammatory responses and antigen presentation.

Recombinant PLD4 protein is engineered through heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to enable functional and structural studies. Its production typically involves cloning the PLD4 gene into expression vectors, followed by purification via affinity chromatography. The recombinant protein retains key domains, such as the conserved HKD motifs critical for putative enzymatic activity, and is utilized to investigate PLD4's role in autoimmune diseases (e.g., systemic sclerosis, lupus) and neurodegenerative disorders.

Emerging evidence highlights PLD4's potential as a biomarker or therapeutic target. For instance, PLD4 polymorphisms are associated with autoimmune conditions, while its dysregulation correlates with microglial dysfunction in Alzheimer's disease. Recombinant PLD4 facilitates mechanistic studies, antibody development, and high-throughput screening for drug discovery. Despite progress, its precise molecular mechanisms and substrates remain under investigation, underscoring the need for further research to elucidate its pathophysiological relevance and therapeutic potential.

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