纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | TREH |
Uniprot No | O43280 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 24-556aa |
氨基酸序列 | LPPPCES EIYCHGELLN QVQMAKLYQD DKQFVDMPLS IAPEQVLQTF TELSRDHNHS IPREQLQAFV HEHFQAKGQE LQPWTPADWK DSPQFLQKIS DAKLRAWAGQ LHQLWKKLGK KMKPEVLSHP ERFSLIYSEH PFIVPGGRFV EFYYWDSYWV MEGLLLSEMA ETVKGMLQNF LDLVKTYGHV PNGGRVYYLQ RSQPPLLTLM MDCYLTHTND TAFLQENIET LALELDFWTK NRTVSVSLEG KNYLLNRYYV PYGGPRPESY SKDVELADTL PEGDREALWA ELKAGAESGW DFSSRWLIGG PNPNSLSGIR TSKLVPVDLN AFLCQAEELM SNFYSRLGND SQATKYRILR SQRLAALNTV LWDEQTGAWF DYDLEKKKKN REFYPSNLTP LWAGCFSDPG VADKALKYLE DNRILTYQYG IPTSLQKTGQ QWDFPNAWAP LQDLVIRGLA KAPLRRAQEV AFQLAQNWIR TNFDVYSQKS AMYEKYDVSN GGQPGGGGEY EVQEGFGWTN GVVLMLLDRY GDRLTS |
预测分子量 | 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TREH(海藻糖酶)重组蛋白的3-4篇代表性文献示例,包含文献名称、作者及摘要内容概括:
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1. **文献名称**: *Molecular Cloning and Characterization of a Trehalase from the Rice Weevil, Sitophilus oryzae*
**作者**: Arakane Y. et al.
**摘要**: 本研究克隆并表达了米象(Sitophilus oryzae)的TREH基因,利用杆状病毒系统在昆虫细胞中进行重组表达。通过酶学分析发现,该重组蛋白在pH 5.0时活性最高,且在昆虫发育过程中可能参与海藻糖代谢调控,为害虫防治提供了潜在靶点。
2. **文献名称**: *Expression and Characterization of a Recombinant Trehalase from Thermophilic Bacterium in E. coli*
**作者**: Liu H. et al.
**摘要**: 研究团队在大肠杆菌中高效表达了源自嗜热菌(Thermus thermophilus)的重组TREH,优化了诱导条件与纯化工艺。结果表明,该酶在高温(70°C)下仍保持高活性,为工业级海藻糖生产提供了耐热性酶候选。
3. **文献名称**: *Trehalase Inhibition for Antifungal Therapy: Synergy with Azoles*
**作者**: Thammahong A. et al.
**摘要**: 通过重组表达真菌来源的TREH,研究发现抑制该酶活性可增强唑类抗真菌药物的效果。实验证明,重组TREH的缺失导致真菌细胞壁完整性受损,揭示了其在抗真菌联合治疗中的应用潜力。
4. **文献名称**: *Functional Analysis of Recombinant Trehalase in Salt Tolerance Mechanisms of Plants*
**作者**: Mitsui T. et al.
**摘要**: 研究利用毕赤酵母系统表达了水稻(Oryza sativa)的重组TREH,发现其活性与植物耐盐性相关。通过转基因植株实验,证实TREH通过调节海藻糖代谢途径缓解盐胁迫对细胞的损伤。
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以上文献涵盖了重组TREH在昆虫、微生物、医学及植物领域的应用研究,涉及表达系统优化、酶学特性及功能机制分析。具体文献需根据实际需求通过学术数据库(如PubMed、ScienceDirect)进一步检索验证。
**Background of TREH Recombinant Protein**
Trehalase (TREH), an enzyme responsible for catalyzing the hydrolysis of trehalose into two glucose molecules, plays a critical role in energy metabolism across diverse organisms, including bacteria, fungi, plants, and animals. Trehalose, a non-reducing disaccharide, serves as a stress protectant and energy source in many species, particularly under extreme conditions like desiccation or temperature fluctuations. TREH’s activity is vital for regulating trehalose levels, ensuring cellular homeostasis, and supporting survival mechanisms in stress-prone environments.
The recombinant form of TREH is produced via genetic engineering, typically using expression systems such as *E. coli*, yeast (*Pichia pastoris*), or mammalian cell lines. Recombinant technology enables large-scale production of the enzyme with high purity and consistency, overcoming limitations of extracting TREH from native sources, which often yield low quantities or impurities. Advances in protein engineering and purification techniques (e.g., affinity chromatography) have further optimized its stability and catalytic efficiency.
TREH recombinant protein has garnered attention in both research and industrial applications. In biomedicine, it is studied for its potential role in metabolic disorders, including TREH deficiency-linked conditions in humans, such as intestinal dysfunction. In agriculture, TREH is explored for enhancing stress tolerance in crops or as a target for antifungal agents. Industrially, it is utilized in biofuel production and food processing, where trehalose breakdown is crucial for fermentation or texture modification.
Despite its promise, challenges remain in tailoring TREH’s activity for specific applications, such as pH or temperature adaptability. Ongoing research focuses on structural analysis and mutagenesis to engineer variants with enhanced functional properties, expanding its utility in biotechnology and therapeutics.
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