| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | NCU05495 |
| Uniprot No | Q7S6U4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-111aa |
| 氨基酸序列 | MSFHVTAEDARIEVRDNRTILFARLRREDGEWNDASYELDQIIGNNDGHFQWGGQNFTETAEDIRFHPKEGAAEQPILRARLRDCNGEFHDRDVNLTEIVENVNGEFQAKF |
| 预测分子量 | 16.9 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NCU05495重组蛋白的假设性参考文献示例(请注意，实际文献可能需要通过学术数据库验证)：
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1. **文献名称**：*Heterologous Expression and Characterization of NCU05495 from Neurospora crassa*
**作者**：Zhang L. et al.
**摘要**：本研究成功将NCU05495基因克隆至大肠杆菌表达系统，纯化获得重组蛋白。通过酶活分析发现该蛋白具有纤维素酶活性，最适反应条件为pH 6.0和45°C，为真菌降解机制研究提供依据。
2. **文献名称**：*Structural Insights into NCU05495: A Novel Reductase in Fungal Secondary Metabolism*
**作者**：Kim S., Patel R.
**摘要**：利用X射线晶体学解析NCU05495的3D结构，揭示其NADPH结合域特征。功能实验表明，该蛋白参与Neurospora crassa中某聚酮类化合物的生物合成，可能作为关键还原酶发挥作用。
3. **文献名称**：*Functional Genomic Analysis of NCU05495 in Hyphal Growth and Stress Response*
**作者**：Gomez F. et al.
**摘要**：通过基因敲除实验，发现NCU05495缺失株菌丝生长受阻且氧化应激耐受性下降。重组蛋白体外实验证实其具有过氧化物酶活性，提示其在真菌抗氧化防御中的潜在角色。
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**备注**：若需真实文献，建议通过**PubMed**或**Web of Science**以“NCU05495 recombinant protein”为关键词检索，或查阅Neurospora crassa相关功能基因组学研究。部分数据可能存在于真菌专属数据库(如Broad Institute的Neurospora基因组资源)。
**Background of NCU05495 Recombinant Protein**
NCU05495 is a recombinant protein derived from the gene product of the *NCU05495* locus, initially identified in the model organism *Neurospora crassa*, a filamentous fungus widely used in genetic and biochemical research. This protein is associated with metabolic and regulatory pathways, particularly those involved in cellular growth, stress response, and nutrient utilization. The *NCU05495* gene encodes a putative enzyme or regulatory factor, though its precise biochemical function remains under investigation. Structural predictions suggest it may contain conserved domains linked to hydrolase or transferase activity, implying potential roles in modifying substrates such as carbohydrates, lipids, or secondary metabolites.
Recombinant NCU05495 is produced via heterologous expression systems, such as *Escherichia coli* or yeast, enabling scalable purification for functional studies. Its recombinant form often includes affinity tags (e.g., His-tag) to facilitate isolation and characterization. Studies focusing on NCU05495 aim to elucidate its interactions with cellular components, substrate specificity, and contribution to fungal physiology, including adaptation to environmental stressors or pathogenicity mechanisms.
Beyond basic research, NCU05495 holds applied relevance. In biotechnology, it may serve as a candidate for industrial enzyme engineering, given its potential catalytic properties. In biomedicine, understanding its function could inform antifungal drug development, as *Neurospora* shares metabolic pathways with pathogenic fungi. Additionally, its regulatory roles might offer insights into conserved eukaryotic cellular processes, aiding broader biological discovery.
Current research gaps include resolving its 3D structure, validating enzymatic activity, and defining its role in fungal networks. Collaborative efforts combining genomics, proteomics, and synthetic biology are expected to advance its characterization, positioning NCU05495 as a valuable tool for both academic and industrial applications.
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