| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SPS1 |
| Uniprot No | P19623 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-302aa |
| 氨基酸序列 | REGWFRETCSLWPGQALSLQVEQLLHHRRSRYQDILVFRSKTYGNVLVLDGVIQCTERDEFSYQEMIANLPLCSHPNPRKVLIIGGGDGGVLREVVKHPSVESVVQCEIDEDVIQVSKKFLPGMAIGYSSSKLTLHVGDGFEFMKQNQDAFDVIITDSSDPMGPAESLFKESYYQLMKTALKEDGVLCCQGECQWLHLDLIKEMRQFCQSLFPVVAYAYCTIPTYPSGQIGFMLCSKNPSTNFQEPVQPLTQQQVAQMQLKYYNSDVHRAAFVLPEFARKALNDVS |
| 预测分子量 | 59.4 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SPS1重组蛋白的参考文献示例(内容为虚构，仅作格式参考)：
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1. **文献名称**：*Cloning, Expression, and Purification of Recombinant SPS1 Protein in Escherichia coli*
**作者**：Zhang Y, et al.
**摘要**：本研究成功克隆了SPS1基因，并在大肠杆菌中实现了高效表达。通过亲和层析纯化获得高纯度重组蛋白，并验证其磷酸酶活性，为后续功能研究奠定基础。
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2. **文献名称**：*Functional Characterization of SPS1 in MAPK Signaling Pathway Regulation*
**作者**：Smith JL, et al.
**摘要**：通过体外实验证实，重组SPS1蛋白通过抑制Ras/MAPK信号通路调控细胞增殖，为癌症治疗中靶向SPS1的潜在应用提供了理论依据。
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3. **文献名称**：*Structural Insights into SPS1 Recombinant Protein by X-ray Crystallography*
**作者**：Lee H, et al.
**摘要**：首次解析了SPS1重组蛋白的晶体结构(分辨率2.1Å)，揭示了其底物结合域的关键氨基酸残基，阐明了酶催化机制的结构基础。
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4. **文献名称**：*SPS1 Recombinant Protein Enhances Drought Tolerance in Transgenic Plants*
**作者**：Wang X, et al.
**摘要**：在拟南芥中过表达重组SPS1蛋白，显著提高了植物的抗旱性，表明其在植物逆境响应中的关键作用。
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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检索具体文献。)
SPS1 (Sulfate Permease 1) recombinant protein is a genetically engineered protein derived from the SPS1 gene, which encodes a sulfate transporter involved in sulfur assimilation pathways. Initially identified in plants like *Arabidopsis thaliana*, SPS1 facilitates sulfate uptake across plasma membranes, critical for synthesizing sulfur-containing amino acids (e.g., cysteine and methionine) and coenzymes. Its homologs exist in fungi, bacteria, and mammals, reflecting conserved roles in cellular sulfur homeostasis.
Recombinant SPS1 is typically produced using heterologous expression systems, such as *E. coli* or yeast, enabling large-scale purification for structural and functional studies. The protein’s structure includes transmembrane domains and substrate-binding sites, which are essential for sulfate ion transport. Research focuses on elucidating its kinetic properties, regulation by sulfur availability, and interactions with other transporters or regulatory proteins.
Beyond basic science, SPS1 recombinant protein has applications in agriculture (e.g., engineering crops with enhanced sulfate uptake under sulfur-deficient soils) and biomedicine (e.g., studying sulfur metabolism disorders). It also serves as a tool for probing environmental stress responses, as sulfate transport is linked to plant adaptation to abiotic stresses. Recent studies explore its potential in synthetic biology for sulfate-dependent biosensors. Despite progress, challenges remain in optimizing expression yields and maintaining functional integrity during purification. Overall, SPS1 recombinant protein bridges fundamental sulfur metabolism research with biotechnological innovations.
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