| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CHS1 |
| Uniprot No | P08004 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4-200aa |
| 氨基酸序列 | QNNRSRNEYHSNRKNEPSYELQNAHSGLFHSSNEELTNRNQRYTNQNASMGSFTPVQSLQFPEQSQQTNMLYNGDDGNNNTINDNERDIYGGFVNHHRQRPPPATAEYNDVFNTNSQQLPSEHQYNNVPSYPLPSINVIQTTPELIHNGSQTMATPIERPFFNENDYYYNNRNSRTSPSIASSSDGYADQEARPILE |
| 预测分子量 | 26.6 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CHS1重组蛋白的3篇代表性文献摘要示例(注：文献信息为模拟生成，仅供参考)：
1. **《Functional characterization of recombinant chitin synthase 1 from Saccharomyces cerevisiae》**
- 作者：Bowen et al.
- 摘要：本研究成功在大肠杆菌中表达并纯化了酿酒酵母CHS1重组蛋白，证实其具有体外催化几丁质合成的活性，并通过定点突变揭示了关键结构域对酶功能的调控机制。
2. **《Expression and RNA interference of chitin synthase 1 gene in Tribolium castaneum》**
- 作者：Arakane et al.
- 摘要：利用杆状病毒系统在昆虫细胞中表达赤拟谷盗CHS1重组蛋白，发现其参与表皮几丁质合成。通过RNA干扰抑制CHS1导致幼虫发育异常，证明其在昆虫蜕皮中的必要性。
3. **《Crystal structure of chitin synthase 1 from Aspergillus fumigatus》**
- 作者：Martínez-Rucobo et al.
- 摘要：解析了烟曲霉CHS1重组蛋白的晶体结构，阐明其底物结合口袋和催化中心的三维构象，为抗真菌药物设计提供了结构基础。
*注：实际文献需通过PubMed、Web of Science等学术平台检索关键词“Chitin synthase 1 recombinant”获取。*
**Background of CHS1 Recombinant Protein**
Chitin synthase 1 (CHS1) is an enzyme critical for chitin biosynthesis, a structural polysaccharide found in fungi, arthropods, and other organisms. In fungi, chitin is a key component of cell walls, contributing to structural integrity, morphogenesis, and stress resistance. CHS1 belongs to the glycosyltransferase family and catalyzes the polymerization of N-acetylglucosamine (GlcNAc) into chitin chains using UDP-GlcNAc as a substrate. Its activity is tightly regulated, as chitin synthesis must be spatially and temporally coordinated with cell growth and division.
The study of CHS1 has significant implications for understanding fungal biology and pathogenesis. Many pathogenic fungi, including *Candida* and *Aspergillus* species, rely on chitin for survival and virulence, making CHS1 a potential target for antifungal therapies. However, native CHS1 is challenging to isolate due to its membrane-associated nature and low abundance. Recombinant CHS1 protein, produced via heterologous expression systems (e.g., *E. coli*, yeast, or insect cells), enables detailed biochemical and structural studies.
Recombinant CHS1 is typically generated by cloning the *CHS1* gene into expression vectors, followed by purification using affinity chromatography. This approach allows researchers to analyze enzyme kinetics, inhibitor screening, and structure-function relationships. Studies using recombinant CHS1 have revealed insights into its catalytic mechanism, regulatory domains, and interaction with antifungal agents. Additionally, engineered variants of CHS1 help explore resistance mechanisms and optimize drug design.
Beyond biomedical applications, CHS1 recombinant protein is used in biotechnology for chitin production in vitro, with potential uses in agriculture (e.g., biopesticides) and materials science (e.g., biodegradable polymers). Despite progress, challenges remain, such as maintaining enzyme stability and activity post-purification. Ongoing research aims to refine expression systems and functional assays to advance CHS1-related applications.
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