| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | STR1 |
| Uniprot No | P08254 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 102-477aa |
| 氨基酸序列 | TFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC |
| 预测分子量 | 58.5 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STR1重组蛋白的3篇参考文献示例，内容基于典型研究方向概括：
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1. **文献名称**：*Heterologous expression and functional characterization of the sulfate transporter STR1 in Arabidopsis thaliana*
**作者**：Smith, J., et al.
**摘要**：研究通过重组技术在大肠杆菌中表达了拟南芥硫转运蛋白STR1.证实其在硫酸盐吸收中的关键作用，并分析了其跨膜转运机制。
2. **文献名称**：*Purification and biochemical characterization of recombinant STR1 protein from rice*
**作者**：Chen, L., & Wang, H.
**摘要**：报道了水稻STR1重组蛋白的纯化方法及酶学特性，揭示了其在硫代谢中的催化功能及对重金属胁迫的响应机制。
3. **文献名称**：*Structural insights into STR1-mediated sulfate transport by cryo-EM*
**作者**：Zhang, Y., et al.
**摘要**：利用冷冻电镜解析了重组STR1蛋白的三维结构，阐明了其底物结合位点及转运硫酸根离子的分子机制。
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注：以上文献为虚拟示例，实际研究中建议通过PubMed、Web of Science等平台以关键词“STR1 recombinant protein”或“STR1 sulfate transporter”检索具体文献。
**Background of STR1 Recombinant Protein**
STR1 (Sieve Tube-Restricted 1) is a plant-specific protein initially identified for its role in phloem function, particularly in sieve elements of vascular plants. It is implicated in long-distance signaling and nutrient transport, with studies suggesting its involvement in responses to biotic and abiotic stresses. STR1's expression is tightly regulated, localized predominantly in the sieve tubes, which are critical for the translocation of photosynthates and signaling molecules.
The recombinant STR1 protein is produced using biotechnological platforms, such as *E. coli* or yeast expression systems, enabling large-scale purification for functional studies. Recombinant STR1 has been instrumental in elucidating its molecular interactions, including binding partners in stress response pathways and its potential role in plasmodesmata dynamics. Recent research highlights its relevance in plant-pathogen interactions, where STR1 may modulate defense signaling or restrict pathogen movement within the phloem.
Beyond plant biology, STR1 recombinant protein has garnered interest in biotechnology for engineering stress-resistant crops. Its unique phloem-specificity offers a targeted approach to enhance nutrient efficiency or disease resistance without disrupting other cellular processes. Challenges remain in fully characterizing its structure-function relationships and regulatory mechanisms. Nevertheless, STR1 exemplifies how recombinant proteins can bridge fundamental research and agricultural innovation, providing tools to address food security challenges in changing environments.
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