| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CTBS |
| Uniprot No | Q01459 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 39-385aa |
| 氨基酸序列 | TD CPCPEPELCR PIRHHPDFEV FVFDVGQKTW KSYDWSQITT VATFGKYDSE LMCYAHSKGA RVVLKGDVSL KDIIDPAFRA SWIAQKLNLA KTQYMDGINI DIEQEVNCLS PEYDALTALV KETTDSFHRE IEGSQVTFDV AWSPKNIDRR CYNYTGIADA CDFLFVMSYD EQSQIWSECI AAANAPYNQT LTGYNDYIKM SINPKKLVMG VPWYGYDYTC LNLSEDHVCT IAKVPFRGAP CSDAAGRQVP YKTIMKQINS SISGNLWDKD QRAPYYNYKD PAGHFHQVWY DNPQSISLKA TYIQNYRLRG IGMWNANCLD YSGDAVAKQQ TEEMWEVLKP KLLQR |
| 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CTBS(几丁质酶B亚基)重组蛋白的3篇参考文献示例(文献信息为虚拟概括，供参考)：
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1. **标题**: *Efficient Expression and Purification of Recombinant CTBS in Escherichia coli for Industrial Applications*
**作者**: Zhang, L.; Wang, Q.; et al.
**摘要**: 本研究通过优化大肠杆菌表达系统(BL21/pET28a)，实现CTBS重组蛋白的高效可溶性表达。采用镍柱亲和层析结合分子筛纯化，获得纯度>95%的蛋白，酶活测定显示其降解几丁质底物的比活性达320 U/mg，为工业化生产提供了可靠方案。
2. **标题**: *Structural and Functional Characterization of CTBS Chimeras in Fungal Resistance*
**作者**: Kumar, S.; Li, J.; et al.
**摘要**: 通过分子动力学模拟及定点突变，解析了CTBS的底物结合域关键位点(Glu156/Trp189)。重组蛋白在转基因拟南芥中表达后，显著增强对灰霉病(Botrytis cinerea)的抗性，证明其作为植物抗病工程蛋白的应用潜力。
3. **标题**: *CTBS-Fc Fusion Protein as a Novel Vaccine Adjuvant: Mechanistic Insights*
**作者**: Rodriguez, A.; Chen, H.; et al.
**摘要**: 构建CTBS与IgG Fc段的融合蛋白，实验表明其可通过激活树突状细胞TLR4/MyD88通路增强抗原呈递。小鼠模型中，CTBS-Fc联合流感疫苗使中和抗体滴度提升8倍，为新型疫苗佐剂开发提供了理论依据。
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注：以上文献为示例性概括，实际研究中建议通过PubMed/Google Scholar检索关键词“recombinant CTBS”、“chitinase B subunit”等获取真实文献。
**Background of CTBS Recombinant Protein**
CTBS (Chitotriosidase) recombinant protein is a engineered version of the human enzyme chitotriosidase, primarily produced through recombinant DNA technology. Chitotriosidase, a chitinase, is naturally secreted by activated macrophages and plays a role in hydrolyzing chitin, a polysaccharide found in fungal cell walls, insect exoskeletons, and parasitic organisms. Although humans lack endogenous chitin, the enzyme is thought to contribute to innate immune responses against chitin-containing pathogens.
The recombinant form of CTBS is generated by inserting the *CHIT1* gene (encoding chitotriosidase) into expression systems like bacterial, yeast, or mammalian cells. This allows large-scale production of the protein for research and therapeutic applications. CTBS recombinant protein retains the enzymatic activity of its natural counterpart, enabling studies on chitin degradation mechanisms, immune modulation, and disease biomarkers.
Clinically, elevated chitotriosidase levels are associated with lysosomal storage disorders (e.g., Gaucher disease), atherosclerosis, and chronic inflammatory conditions. Recombinant CTBS serves as a critical tool in developing diagnostic assays and understanding disease progression. However, genetic deficiencies in chitotriosidase (observed in certain populations) limit its universal utility, spurring interest in engineered variants with enhanced stability or activity.
In biotechnology, CTBS recombinant protein is explored for eco-friendly chitin waste processing and antifungal agent development. Challenges include optimizing expression yields, ensuring proper post-translational modifications, and minimizing immunogenicity in therapeutic contexts. Ongoing research focuses on structure-function relationships and fusion proteins to expand its applications.
Overall, CTBS recombinant protein bridges biomedical research and industrial innovation, offering insights into chitin-related biology and practical solutions for health and environmental challenges.
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