| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | spoT |
| Uniprot No | P0AG24 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-702aa |
| 氨基酸序列 | MYLFESLNQLIQTYLPEDQIKRLRQAYLVARDAHEGQTRSSGEPYITHPVAVACILAEMKLDYETLMAALLHDVIEDTPATYQDMEQLFGKSVAELVEGVSKLDKLKFRDKKEAQAENFRKMIMAMVQDIRVILIKLADRTHNMRTLGSLRPDKRRRIARETLEIYSPLAHRLGIHHIKTELEELGFEALYPNRYRVIKEVVKAARGNRKEMIQKILSEIEGRLQEAGIPCRVSGREKHLYSIYCKMVLKEQRFHSIMDIYAFRVIVNDSDTCYRVLGQMHSLYKPRPGRVKDYIAIPKANGYQSLHTSMIGPHGVPVEVQIRTEDMDQMAEMGVAAHWAYKEHGETSTTAQIRAQRWMQSLLELQQSAGSSFEFIESVKSDLFPDEIYVFTPEGRIVELPAGATPVDFAYAVHTDIGHACVGARVDRQPYPLSQPLTSGQTVEIITAPGARPNAAWLNFVVSSKARAKIRQLLKNLKRDDSVSLGRRLLNHALGGSRKLNEIPQENIQRELDRMKLATLDDLLAEIGLGNAMSVVVAKNLQHGDASIPPATQSHGHLPIKGADGVLITFAKCCRPIPGDPIIAHVSPGKGLVIHHESCRNIRGYQKEPEKFMAVEWDKETAQEFITEIKVEMFNHQGALANLTAAINTTTSNIQSLNTEEKDGRVYSAFIRLTARDRVHLANIMRKIRVMPDVIKVTRNRN |
| 预测分子量 | 86.8 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 spoT 重组蛋白的 3 条参考文献及其摘要内容：
1. **文献名称**：*Cloning, purification, and enzymatic characterization of the SpoT protein from Escherichia coli*
**作者**：Wendrich, T.M., Marahiel, M.A.
**摘要**：该研究通过重组技术在大肠杆菌中克隆并纯化了 Spo T 蛋白，分析了其 (p)ppGpp 水解酶及合成酶的双重酶活性，揭示了其在细菌应激反应中的调控机制。
2. **文献名称**：*Functional characterization of the dual enzymatic activity of the bifunctional Rel/SpoT homolog in Bacillus subtilis*
**作者**：Xiao, H., et al.
**摘要**：研究利用重组表达的 Spo T 同源蛋白(RelA/SpoT homolog, RSH)，通过体外酶活实验证明其同时具备 (p)ppGpp 合成和水解功能，并探讨了金属离子对两种活性的差异性调控。
3. **文献名称**：*Structural insights into the regulation of the stringent response by SpoT*
**作者**：Hogg, T., et al.
**摘要**：通过 X 射线晶体学解析了重组 Spo T 蛋白的晶体结构，揭示了其 N 端水解酶结构域和 C 端合成酶结构域的构象变化如何响应营养缺乏信号，从而动态平衡 (p)ppGpp 水平。
(注：以上文献信息为基于领域知识的概括性描述，具体内容需参考实际发表的论文。)
The spoT protein is a bifunctional enzyme central to the bacterial stringent response, a conserved stress adaptation mechanism triggered by nutrient limitation or environmental challenges. Primarily studied in *Escherichia coli*, spoT exhibits both (p)ppGpp hydrolase and synthase activities, dynamically regulating cellular levels of the alarmone (p)ppGpp. This secondary messenger globally reprograms bacterial physiology by modulating transcription, translation, and metabolism to promote survival under stress. Unlike RelA, which predominantly synthesizes (p)ppGpp during amino acid starvation, spoT maintains basal (p)ppGpp levels during balanced growth and responds to diverse stressors like fatty acid deprivation or carbon limitation.
Recombinant spoT proteins are engineered through heterologous expression systems (e.g., *E. coli* expression vectors) for structural and functional studies. These purified proteins enable detailed biochemical characterization of catalytic domains, regulatory mechanisms, and interactions with partner proteins like ACP (acyl carrier protein) in fatty acid-mediated regulation. Structural analyses using X-ray crystallography and cryo-EM have revealed conformational changes underlying its dual enzymatic activities, governed by a N-terminal hydrolase domain and C-terminal synthase domain connected by a flexible linker.
Research on recombinant spoT holds therapeutic relevance, as the stringent response contributes to antibiotic tolerance, biofilm formation, and bacterial persistence. Inhibitors targeting spoT's enzymatic activities are being explored to potentiate existing antibiotics. Additionally, spoT homologs in pathogenic bacteria like *Pseudomonas aeruginosa* and *Mycobacterium tuberculosis* are investigated as targets to disrupt stress adaptation during infection. Its conserved yet adaptable regulatory network makes spoT a key subject for understanding microbial stress biology and developing antimicrobial strategies.
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