| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CUT1 |
| Uniprot No | P30272 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 17-228aa |
| 氨基酸序列 | SPIATNVEKPSELEARQLNSVRNDLISGNAAACPSVILIFARASGEVGNMGLSAGTNVASALEREFRNDIWVQGVGDPYDAALSPNFLPAGTTQGAIDEAKRMFTLANTKCPNAAVVAGGYSQGTAVMFNAVSEMPAAVQDQIKGVVLFGYTKNLQNRGRIPDFPTEKTEVYCNASDAVCFGTLFLLPAHFLYTTESSIAAPNWLIRQIRAA |
| 预测分子量 | 35.5 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CUT1重组蛋白的3-4篇参考文献的简要列举：
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1. **文献名称**：*The Arabidopsis CER1 gene encodes a novel enzyme involved in cuticular wax biosynthesis*
**作者**：Lacey Samuels, et al.
**摘要**：研究报道拟南芥CUT1(CER1)重组蛋白在角质层蜡质合成中的关键作用，通过异源表达证实其参与长链醛脱氢酶活性，影响植物表皮屏障功能。
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2. **文献名称**：*Heterologous expression and characterization of recombinant CUT1 lipase in Pichia pastoris*
**作者**：J. Smith, et al.
**摘要**：利用毕赤酵母系统高效表达重组CUT1脂肪酶，纯化后分析其酶学特性，证明其在低温催化中的高效性及工业应用潜力。
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3. **文献名称**：*Functional analysis of CUT1 in Fusarium graminearum via CRISPR/Cas9-mediated gene knockout*
**作者**：A. Zhang, et al.
**摘要**：通过CRISPR/Cas9技术敲除禾谷镰刀菌CUT1基因，发现其缺失导致菌丝生长缺陷和毒力下降，表明CUT1在病原真菌侵染中的必要性。
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4. **文献名称**：*Optimization of CUT1 recombinant protein production in E. coli for biocatalytic applications*
**作者**：H. Wang, et al.
**摘要**：系统优化大肠杆菌表达CUT1重组蛋白的发酵条件(如诱导温度、IPTG浓度)，显著提高蛋白可溶性和活性，为规模化制备提供方案。
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注：上述文献为虚拟示例，实际研究中建议通过学术数据库(如PubMed、Web of Science)检索具体论文。
CUT1 recombinant protein, derived from the Cutinase 1 enzyme, is a hydrolytic enzyme initially identified in phytopathogenic fungi such as *Fusarium solani*. Cutinases belong to the α/β-hydrolase superfamily and are renowned for their ability to degrade cutin, a hydrophobic polyester component of plant cuticles. This enzyme catalyzes the hydrolysis of ester bonds in cutin, facilitating fungal invasion through plant surfaces. Beyond its natural role, CUT1 has garnered significant biotechnological interest due to its broad substrate specificity, which includes synthetic polyesters like polyethylene terephthalate (PET), making it a promising candidate for industrial and environmental applications.
Structurally, CUT1 is a compact, single-domain protein (∼22 kDa) featuring a catalytic triad (Ser-His-Asp) common to serine esterases. Its stability under varying pH and temperature conditions enhances its utility in diverse processes. Recombinant CUT1 is typically produced via heterologous expression in microbial systems (e.g., *E. coli* or yeast), enabling scalable and cost-effective production. Advances in protein engineering, such as directed evolution, have further optimized its activity and thermostability for industrial use.
Applications span multiple fields: in bioremediation, CUT1 degrades plastic waste; in detergents, it acts as a lipid-stain remover; in biofuels, it assists in lipid transesterification. Additionally, it serves as a model enzyme for studying structure-function relationships in esterases. Ongoing research focuses on enhancing its catalytic efficiency and substrate range, positioning recombinant CUT1 as a versatile tool in sustainable biotechnology and circular economy initiatives.
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