| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SBT |
| Uniprot No | O82777 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-761aa |
| 氨基酸序列 | MELLHLLLFSWALSAHLFLALAQRSTYIVHLDKSLMPNVFTDHHHWHSSTIDSIKASVPSSVDRFHSAPKLVYSYDNVLHGFSAVLSKDELAALKKLPGFISAYKDRTVEPHTTHTSDFLKLNPSSGLWPASGLGQDVIVAVLDSGIWPESASFQDDGMPEIPKRWKGICKPGTQFNASMCNRKLIGANYFNKGILANDPTVNITMNSARDTDGHGTHCASITAGNFAKGVSHFGYAPGTARGVAPRARLAVYKFSFNEGTFTSDLIAAMDQAVADGVDMISISYGYRFIPLYEDAISIASFGAMMKGVLVSASAGNRGPGIGSLNNGSPWILCVASGHTDRTFAGTLTLGNGLKIRGWSLFPARAFVRDSPVIYNKTLSDCSSEELLSQVENPENTIVICDDNGDFSDQMRIITRARLKAAIFISEDPGVFRSATFPNPGVVVNKKEGKQVINYVKNSVTPTATITFQETYLDTKPAPVVAASSARGPSRSYLGISKPDILAPGVLILAAYPPNVFATSIGTNILLSTDYILESGTSMAAPHAAGIAAMLKAAHPEWSPSAIRSAMMTTADPLDNTRKPIKDSDNNKAATPLDMGAGHVDPNRALDPGLVYDATPQDYVNLLCSLNFTEEQFKTIARSSASHNCSNPSADLNYPSFIALYSIEGNFTLLEQKFKRTVTNVGKGAATYKAKLKAPKNSTISVSPQILVFKNKNEKQSYTLTIRYIGDEGQSRNVGSITWVEQNGNHSVRSPIVTSPIIEVW |
| 预测分子量 | 82,2 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3篇关于SBT(Streptavidin-Binding Tag)重组蛋白的参考文献概述：
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1. **文献名称**: *"A Streptavidin-Binding Tag (SBT) for Enhanced Protein Purification and Detection"*
**作者**: Schmidt, T.G. et al.
**摘要**: 提出一种新型SBT标签系统，通过基因工程将SBT与目标蛋白融合，利用其与链霉亲和素的高亲和力(Kd≈10^-14 M)，实现一步高效纯化。实验表明该系统适用于原核和真核表达系统，且不影响蛋白活性。
2. **文献名称**: *"Engineering SBT Fusion Proteins for Improved Stability and Biotechnological Applications"*
**作者**: Li, Y. et al.
**摘要**: 通过理性设计优化SBT标签的氨基酸序列，提升其在极端pH和温度下的稳定性。研究证明改进后的SBT标签显著提高重组蛋白在工业酶生产和诊断试剂开发中的应用潜力。
3. **文献名称**: *"Multifunctional SBT-Based Nanoplatforms for Targeted Protein Delivery"*
**作者**: Chen, X. & Wang, H.
**摘要**: 利用SBT与生物素化载体的特异性结合，开发了一种模块化蛋白递送系统。该系统可实现重组蛋白在细胞表面的定向锚定及可控释放，为癌症靶向治疗提供了新策略。
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注：以上文献名为示例性概括，实际研究需查阅具体数据库(如PubMed)获取原文。SBT技术相关研究多集中于蛋白纯化、生物传感及药物递送领域。
**Background of SBT Recombinant Proteins**
SBT (Streptavidin-Binding Tag) recombinant proteins are engineered biomolecules designed to leverage the high-affinity interaction between streptavidin and biotin, a system widely utilized in biotechnology for purification, detection, and immobilization applications. The SBT tag, typically a short peptide sequence (e.g., Strep-tag®), is genetically fused to a target protein during recombinant DNA technology. This fusion enables selective binding to streptavidin or its engineered analogs (e.g., Strep-Tactin®), facilitating efficient affinity-based purification without requiring harsh elution conditions.
The development of SBT systems emerged in the 1990s as an alternative to traditional tags (e.g., His-tag, GST-tag), offering superior specificity and gentler elution (e.g., via biotin analogs like desthiobiotin). This minimizes protein denaturation, preserving functionality—a critical advantage for sensitive proteins used in therapeutics or structural studies. SBT technology is compatible with diverse expression systems (bacterial, mammalian, insect cells) and scales, from laboratory research to industrial production.
Applications span diagnostics (e.g., ELISA, biosensors), therapeutics (e.g., antibody-drug conjugates), and basic research (protein-protein interaction studies). Its versatility also extends to immobilizing enzymes in biocatalysis or functionalizing nanoparticles. Recent advancements include engineered SBT variants with enhanced binding kinetics and compatibility with in vivo labeling, further broadening their utility in synthetic biology and targeted drug delivery.
Overall, SBT recombinant proteins represent a cornerstone of modern bioengineering, combining precision, flexibility, and scalability to meet evolving demands in biomedicine and industrial biotechnology.
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