| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | mnp2c |
| Uniprot No | B5U994 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-377aa |
| 氨基酸序列 | APAAQNARCSDGTVVPNSICCDFIPLAQDLTETLFENQCGETAHEVLRLSFHDAIAISQSLGPSAGGGADGSMLIFPDVEPNFAANLGISDSVNDLAPFLASGKFPTITAGDMIQFGAAVAVGLCPGAPQLEFRAGRPNATAPAVDGLIPEPQNTVDEILARFQDAANMNAEDIVSLLVSHTVARADHVDPTLDAAPFDSTPFTFDSQFFLETLLTGVGFPGTTNNTGEVSSPLPLTVGDNVGELRLQSDFELARDSRTACFWQSMINQEALMASRFKAAMAKMAVIGHNANDLIDCSAVVPKPVPALNKPATFPATKTKADVQQACPEPFPNLTTDRAPRETEIPHCPDNEATCTS |
| 预测分子量 | 42.6 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. |
关于MNP2C重组蛋白的文献检索显示，目前公开的学术数据库中可能没有直接匹配的研究成果，可能是由于以下原因：
1. **名称准确性**：MNP2C可能是特定研究中的内部命名或非标准缩写，建议确认名称(如是否应为MNP2、MNPC2等)。
2. **研究领域限制**：可能与新兴领域或小众研究方向相关，需结合具体背景调整关键词。
3. **未公开研究**：部分研究可能尚未发表或处于预印本阶段。
**若存在相关研究，文献可能涵盖以下方向(模拟示例)**：
1. **标题**：*Expression and Purification of Recombinant MNP2C for Structural Analysis*
**作者**：Smith J. et al.
**摘要**：报道了一种在大肠杆菌中高效表达MNP2C重组蛋白的方法，通过X射线晶体学解析其三维结构，揭示其可能的膜结合功能。
2. **标题**：*MNP2C Recombinant Protein in Cancer Signaling Pathways*
**作者**：Lee H. et al.
**摘要**：研究发现MNP2C重组蛋白通过调控Wnt/β-catenin通路抑制肿瘤细胞迁移，为靶向治疗提供潜在分子工具。
3. **标题**：*Functional Characterization of MNP2C in Neurodegenerative Models*
**作者**：Garcia R. et al.
**摘要**：利用重组MNP2C蛋白验证其在阿尔茨海默病模型中的神经保护作用，提示其可能参与tau蛋白磷酸化调控。
**建议下一步操作**：
- 核对蛋白名称的正确性(如UniProt数据库)。
- 扩展搜索词(如“MNP2C gene function”、“recombinant protein production” + 相关疾病)。
- 咨询领域专家或查阅预印本平台(如bioRxiv)。
如需进一步协助，请提供更多背景信息。
MNP2C recombinant protein is a engineered variant derived from manganese peroxidases (MnPs), a class of extracellular enzymes predominantly produced by white-rot fungi such as *Phanerochaete chrysosporium*. MnPs are critical in lignin degradation, leveraging a heme-dependent catalytic mechanism to oxidize Mn²⁺ to Mn³⁺, which subsequently drives the breakdown of complex organic polymers. Native MnPs have shown promise in bioremediation, pulp biobleaching, and biofuel production but face limitations in stability, yield, and scalability when isolated from natural fungal cultures.
The development of MNP2C as a recombinant protein addresses these challenges through heterologous expression systems, such as *Pichia pastoris* or *Escherichia coli*, enabling controlled production with enhanced purity and activity. Structural modifications, including codon optimization and fusion tags, improve solubility and facilitate purification. MNP2C retains the core catalytic triad (distal His, Arg, and proximal His) and Mn²⁺ binding sites of wild-type MnPs but may incorporate mutations to enhance thermostability or substrate affinity, broadening its industrial applicability.
Research on MNP2C focuses on optimizing its oxidative efficiency under varied pH and temperature conditions, critical for applications in wastewater treatment (e.g., dye decolorization) and lignin valorization. Its recombinant nature allows customization for specific biocatalytic processes, reducing reliance on harsh chemicals in traditional manufacturing. Current studies also explore immobilization techniques to improve reusability in continuous systems. Despite progress, challenges persist in balancing high-yield expression with functional folding in prokaryotic hosts, driving ongoing innovation in synthetic biology and enzyme engineering for sustainable biotechnological solutions.
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