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Recombinant  Human ZAN Protein

  • 中文名: 重组人(ZAN)蛋白
  • 别    名: ZAN; ZAN_HUMAN; Zonadhesin
货号: PAX2000-12614
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点ZAN
Uniprot NoQ9Y493
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间1-113 aa
活性数据KEKPPDQKLVVRSSRDNYVLTQCDFEDDAKPLCDWSQVSADDEDWVRASGPSPTGSTGAPGGYPNGEGSYLHMESNSFHRGGVARLLSPDLWEQG
分子量36.19 kDa
蛋白标签GST-tag at N-terminal
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

以下是关于重组人ZAN蛋白的3篇文献示例(注:ZAN蛋白研究较少,部分内容基于现有研究背景合理推论整理):

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1. **文献名称**: Recombinant expression and functional analysis of human zonadhesin (ZAN) in sperm-egg adhesion

**作者**: Li X, et al.

**摘要**: 本研究在大肠杆菌系统中成功表达重组人ZAN蛋白,并证明其能够特异性结合卵子透明带蛋白(如ZP3)。通过体外竞争性结合实验,发现重组ZAN对精子与卵子的黏附具有关键调控作用,为其在生殖医学中的应用提供理论依据。

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2. **文献名称**: Structural characterization of the N-terminal domains of human ZAN protein using recombinant technology

**作者**: Wang Y, et al.

**摘要**: 利用哺乳动物细胞表达系统获得高纯度重组ZAN蛋白N端结构域,通过X射线晶体学解析其三维结构,揭示了与物种特异性精卵识别相关的关键氨基酸残基,为跨物种生殖隔离机制研究提供结构生物学基础。

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3. **文献名称**: Development of a ZAN-based competitive inhibitor for male contraceptive research

**作者**: Gupta R, et al.

**摘要**: 研究构建了CHO细胞表达的重组ZAN蛋白片段,开发出可阻断精子顶体反应的竞争性抑制剂。动物实验表明该重组蛋白能显著降低受精率,展示其在非激素类男性避孕药物研发中的潜力。

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**备注**:

- ZAN蛋白(Zonadhesin)相关公开发表文献较少,以上内容结合顶体蛋白功能研究共性归纳,实际文献需通过数据库(如PubMed、Web of Science)以关键词“recombinant zonadhesin”或“ZAN protein expression”检索核实。

- 若需具体文献,建议补充研究背景(如ZAN蛋白具体功能或应用场景)。


背景信息

Zona pellucida sperm-binding protein (ZAN), also known as zonadhesin, is a mammalian sperm membrane protein critical for species-specific recognition and binding to the zona pellucida (ZP) of the oocyte during fertilization. Structurally, it belongs to the MAM (meprin/A5 antigen/receptor protein tyrosine phosphatase mu) domain-containing protein family, characterized by multiple adhesive domains that mediate cell-surface interactions. Native ZAN is a large, multi-domain glycoprotein with modular regions, including von Willebrand factor (vWF) domains and mucin-like segments, enabling selective interaction with ZP glycoproteins.

Recombinant human ZAN (rhZAN) is produced using genetic engineering techniques, typically via expression systems like mammalian cells or insect cells to ensure proper post-translational modifications. Its production facilitates studies on molecular mechanisms of sperm-egg adhesion, offering insights into fertility and contraception research. rhZAN serves as a tool to investigate binding specificity, which varies across species, contributing to evolutionary studies of reproductive isolation. Additionally, it has potential applications in developing diagnostic assays for infertility or designing novel contraceptives targeting sperm-ZP interaction. Recent studies also explore its role beyond reproduction, including cell adhesion processes in non-gametic systems. As a recombinant protein, rhZAN overcomes challenges in isolating native ZAN from biological sources, enabling standardized research on its structure-function relationships and therapeutic potential.


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