| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | DMT1 |
| Uniprot No | Q9UQN3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-213aa |
| 氨基酸序列 | ASLFKKKTVDDVIKEQNRELRGTQRAIIRDRAALEKQEKQLELEIKKMAKIGNKEACKVLAKQLVHLRKQKTRTFAVSSKVTSMSTQTKVMNSQMKMAGAMSTTAKTMQAVNKKMDPQKTLQTMQNFQKENMKMEMTEEMINDTLDDIFDGSDDEEESQDIVNQVLDEIGIEISGKMAKAPSAARSLPSASTSKATISDEEIERQLKALGVD |
| 预测分子量 | 50.8kDa |
| 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DMT1重组蛋白的3篇参考文献及其摘要概括：
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1. **文献名称**：*Cloning and characterization of a mammalian proton-coupled metal-ion transporter*
**作者**：Gunshin, H., et al.
**摘要**：该研究首次克隆了DMT1基因(当时称为Nramp2)，并在非洲爪蟾卵母细胞中重组表达，证实其作为pH依赖的二价金属离子(如Fe²⁺)转运蛋白的功能，揭示了DMT1在肠道铁吸收中的关键作用。
2. **文献名称**：*Cellular localization and iron-responsive expression of the divalent metal transporter 1 (DMT1) in HEK293 cells*
**作者**：Canonne-Hergaux, F., et al.
**摘要**：通过在HEK293细胞中重组表达DMT1蛋白，作者发现其定位于细胞膜和内体结构，并证明其铁转运活性受细胞铁状态调控，为DMT1的细胞功能及调控机制提供了实验依据。
3. **文献名称**：*Structure of the human divalent metal transporter 1 (DMT1) in complex with transition metals*
**作者**：Yan, R., et al.
**摘要**：利用冷冻电镜技术解析了重组表达的人源DMT1蛋白的三维结构，揭示了其与铁、锰等金属离子结合的关键位点，阐明了DMT1的底物识别和质子耦合转运的分子机制。
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以上文献涵盖DMT1的基因克隆、细胞定位、结构解析等研究，均涉及重组蛋白技术的应用。如需更多文献或特定方向的研究，可进一步补充。
**Background of DMT1 Recombinant Protein**
Divalent Metal Transporter 1 (DMT1), also known as SLC11A2. is a transmembrane protein critical for cellular uptake of divalent metal ions, including iron (Fe²⁺), manganese (Mn²⁺), copper (Cu²⁺), and zinc (Zn²⁺). It belongs to the solute carrier family 11 (SLC11) and operates as a proton-coupled symporter, leveraging the H⁺ gradient to transport metals across cell membranes. DMT1 is expressed in various tissues, with prominent roles in intestinal iron absorption, erythroid iron utilization, and renal metal reabsorption. Its activity is tightly linked to systemic iron homeostasis, making it essential for processes like hemoglobin synthesis and cellular metabolism.
Structurally, DMT1 contains 12 predicted transmembrane domains and undergoes tissue-specific splicing, generating isoforms that differ in their N- or C-terminal regions. These variants may regulate subcellular localization or metal selectivity. Dysregulation of DMT1 is associated with iron-related disorders, such as iron-deficiency anemia, iron overload (e.g., hemochromatosis), and neurodegenerative conditions linked to manganese or copper toxicity.
Recombinant DMT1 protein is produced using heterologous expression systems (e.g., HEK293. Escherichia coli) to study its biophysical properties, transport mechanisms, and interactions with inhibitors or therapeutic agents. Purified DMT1 enables in vitro assays to characterize ion-binding affinities, pH dependency, and kinetic parameters. It also aids in structural studies (e.g., cryo-EM) to resolve conformational changes during transport.
Research on DMT1 recombinant protein has therapeutic implications, particularly for targeting iron metabolism disorders or metal toxicity. Additionally, it serves as a tool to explore environmental toxicology, such as heavy metal uptake in cells. Overall, DMT1 remains a focal point in understanding metal biology and developing interventions for related diseases.
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