| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ChT |
| Uniprot No | Q9GZV3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-580aa |
| 氨基酸序列 | MAFHVEGLIAIIVFYLLILLVGIWAAWRTKNSGSAEERSEAIIVGGRDIGLLVGGFTMTATWVGGGYINGTAEAVYVPGYGLAWAQAPIGYSLSLILGGLFFAKPMRSKGYVTMLDPFQQIYGKRMGGLLFIPALMGEMFWAAAIFSALGATISVIIDVDMHISVIISALIATLYTLVGGLYSVAYTDVVQLFCIFVGLWISVPFALSHPAVADIGFTAVHAKYQKPWLGTVDSSEVYSWLDSFLLLMLGGIPWQAYFQRVLSSSSATYAQVLSFLAAFGCLVMAIPAILIGAIGASTDWNQTAYGLPDPKTTEEADMILPIVLQYLCPVYISFFGLGAVSAAVMSSADSSILSASSMFARNIYQLSFRQNASDKEIVWVMRITVFVFGASATAMALLTKTVYGLWYLSSDLVYIVIFPQLLCVLFVKGTNTYGAVAGYVSGLFLRITGGEPYLYLQPLIFYPGYYPDDNGIYNQKFPFKTLAMVTSFLTNICISYLAKYLFESGTLPPKLDVFDAVVARHSEENMDKTILVKNENIKLDELALVKPRQSMTLSSTFTNKEAFLDVDSSPEGSGTEDNLQ |
| 预测分子量 | 63,2 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. |
以下是关于ChT(假设为几丁质酶，Chitinase)重组蛋白的模拟参考文献示例，供参考：
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1. **文献名称**: *Heterologous Expression and Characterization of a Novel Chitinase from Bacillus subtilis*
**作者**: Zhang L., et al.
**摘要**: 研究在大肠杆菌中成功表达了一种来源于枯草芽孢杆菌的几丁质酶重组蛋白，优化了表达条件并验证其酶活性和热稳定性，证明其在几丁质降解中的应用潜力。
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2. **文献名称**: *Optimization of Recombinant Chitinase Production in Pichia pastoris*
**作者**: Wang Y., et al.
**摘要**: 通过毕赤酵母表达系统高效生产重组几丁质酶，探究了诱导时间、温度及甲醇浓度对产量的影响，最终获得高纯度酶制品，适用于农业真菌病害防治。
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3. **文献名称**: *Functional Analysis of a Recombinant Chitinase from Marine Bacteria*
**作者**: Chen H., et al.
**摘要**: 从海洋细菌中克隆ChT基因，利用昆虫细胞表达系统获得活性重组蛋白，证实其对几丁质底物的特异性水解能力及在生物材料加工中的价值。
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4. **文献名称**: *Immobilization of Recombinant Chitinase for Industrial Applications*
**作者**: Kumar S., et al.
**摘要**: 将重组几丁质酶固定化于纳米载体上，显著提高了酶的重复利用率和稳定性，为工业级几丁质废弃物处理提供了新策略。
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(注：以上文献为示例，非真实存在的论文，实际引用请查询学术数据库。)
**Background of ChT Recombinant Protein**
ChT recombinant protein, commonly referred to as Chitinase-Thioredoxin fusion protein, is a genetically engineered biomolecule designed for enhanced functionality and stability. Chitinases are hydrolytic enzymes that break down chitin, a polysaccharide found in fungal cell walls, insect exoskeletons, and crustacean shells. Native chitinases are naturally produced by various organisms, including bacteria, plants, and fungi, playing roles in defense mechanisms, nutrient acquisition, and developmental processes. However, their industrial or therapeutic applications are often limited by low yield, instability, or purification challenges.
To overcome these limitations, recombinant DNA technology is employed to produce ChT by fusing chitinase with thioredoxin, a small redox protein. Thioredoxin acts as a solubility enhancer and fusion partner, improving the folding and stability of the chitinase domain during expression in heterologous systems like *E. coli*. This fusion strategy not only simplifies purification (e.g., via affinity tags) but also retains or enhances enzymatic activity.
ChT recombinant protein has garnered attention in biotechnological and biomedical fields. Its chitin-degrading capability is utilized in agriculture for biocontrol of fungal pathogens, in waste management for chitin-rich biomass conversion, and in the food industry for crustacean processing. Additionally, chitinases exhibit immunomodulatory properties, making ChT a candidate for research in anti-inflammatory therapies or antifungal drug development.
Recent studies focus on optimizing ChT production through strain engineering, fermentation conditions, or structural modifications to enhance thermostability and substrate specificity. As sustainability and eco-friendly solutions gain prominence, ChT represents a versatile tool aligned with green chemistry and bioprocessing trends. Ongoing research aims to expand its applications while addressing challenges like scalability and cost-effectiveness.
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