| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SLC39A4 |
| Uniprot No | Q6P5W5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-647aa |
| 氨基酸序列 | MASLVSLELGLLLAVLVVTATASPPAGLLSLLTSGQGALDQEALGGLLNTLADRVHCANGPCGKCLSVEDALGLGEPEGSGLPPGPVLEARYVARLSAAAVLYLSNPEGTCEDARAGLWASHADHLLALLESPKALTPGLSWLLQRMQARAAGQTPKMACVDIPQLLEEAVGAGAPGSAGGVLAALLDHVRSGSCFHALPSPQYFVDFVFQQHSSEVPMTLAELSALMQRLGVGREAHSDHSHRHRGASSRDPVPLISSSNSSSVWDTVCLSARDVMAAYGLSEQAGVTPEAWAQLSPALLQQQLSGACTSQSRPPVQDQLSQSERYLYGSLATLLICLCAVFGLLLLTCTGCRGVTHYILQTFLSLAVGAVTGDAVLHLTPKVLGLHTHSEEGLSPQPTWRLLAMLAGLYAFFLFENLFNLLLPRDPEDLEDGPCGHSSHSHGGHSHGVSLQLAPSELRQPKPPHEGSRADLVAEESPELLNPEPRRLSPELRLLPYMITLGDAVHNFADGLAVGAAFASSWKTGLATSLAVFCHELPHELGDFAALLHAGLSVRQALLLNLASALTAFAGLYVALAVGVSEESEAWILAVATGLFLYVALCDMLPAMLKVRDPRPWLLFLLHNVGLLGGWTVLLLLSLYEDDITF |
| 预测分子量 | 68,4 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. |
以下是关于SLC39A4重组蛋白的模拟参考文献(建议通过学术数据库核实具体文献)：
1. **文献名称**：*Expression and functional characterization of recombinant human SLC39A4 (ZIP4) in HEK293 cells*
**作者**：Dufner-Beattie, J., et al.
**摘要**：研究通过哺乳动物表达系统(HEK293细胞)成功表达SLC39A4重组蛋白，证实其在细胞膜上的定位及锌离子转运功能，并发现其表达水平受细胞外锌浓度调控。
2. **文献名称**：*Purification and structural analysis of the SLC39A4 zinc transporter using a prokaryotic expression system*
**作者**：Bafaro, E., et al.
**摘要**：利用大肠杆菌表达系统纯化SLC39A4重组蛋白，通过X射线晶体学解析其跨膜结构域，揭示锌结合位点及与遗传性缺锌症(Acrodermatitis enteropathica)相关的突变影响。
3. **文献名称**：*Functional complementation of yeast zinc transport mutants by SLC39A4 recombinant protein*
**作者**：Wang, F., et al.
**摘要**：在酵母缺锌突变株中异源表达SLC39A4重组蛋白，恢复其锌吸收能力，证明该蛋白在进化保守的锌转运机制中的作用，并筛选出关键功能域。
4. **文献名称**：*In vitro analysis of zinc transport kinetics by recombinant SLC39A4 using proteoliposomes*
**作者**：Kimura, T., et al.
**摘要**：将纯化的SLC39A4重组蛋白重构至脂质体中，通过体外实验量化其锌离子转运活性及pH依赖性，揭示转运动力学特征及病理突变体的功能缺陷。
**注**：以上为基于领域研究的模拟参考文献，实际引用时请通过PubMed或Web of Science核实原文信息。
SLC39A4. also known as ZIP4. is a member of the Zrt-/Irt-like protein (ZIP) family, which plays a critical role in cellular zinc homeostasis by mediating zinc uptake across plasma membranes. This transmembrane protein is primarily expressed in enterocytes, pancreatic acinar cells, and other tissues involved in nutrient absorption. Zinc, an essential trace element, is vital for enzymatic activity, immune function, and DNA synthesis. Dysregulation of ZIP4 has been linked to severe health conditions, most notably acrodermatitis enteropathica (AE), a rare autosomal recessive disorder caused by SLC39A4 mutations. AE manifests as zinc deficiency syndromes, including dermatitis, diarrhea, and immune dysfunction, underscoring ZIP4's importance in dietary zinc absorption.
Recombinant SLC39A4 protein is engineered to study its structure-function relationships, zinc transport mechanisms, and interactions with other proteins or therapeutic agents. Produced via heterologous expression systems (e.g., mammalian cells, yeast, or Escherichia coli), the recombinant protein retains functional domains, such as the extracellular zinc-binding region and transmembrane helices critical for metal ion translocation. Its applications span biomedical research, including elucidating molecular defects in AE, exploring ZIP4's role in cancers (e.g., pancreatic and prostate cancers where overexpression correlates with tumor progression), and screening potential zinc transport modulators. Additionally, recombinant ZIP4 serves as a tool to develop targeted therapies, such as zinc supplementation strategies or inhibitors for cancer treatment. Studies using this protein have also advanced understanding of zinc's systemic regulation and its impact on metabolic and signaling pathways. Ongoing research aims to resolve its 3D structure and dynamics, which could unlock novel therapeutic avenues for zinc-related disorders.
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