| 纯度 | >95%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NIT2 |
| Uniprot No | Q9NQR4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-276aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMTSFRLALIQLQISSIKSDNVTRACSF IREAATQGAKIVSLPECFNSPYGAKYFPEYAEKIPGESTQKLSEVAKECS IYLIGGSIPEEDAGKLYNTCAVFGPDGTLLAKYRKIHLFDIDVPGKITFQ ESKTLSPGDSFSTFDTPYCRVGLGICYDMRFAELAQIYAQRGCQLLVYPG AFNLTTGPAHWELLQRSRAVDNQVYVATASPARDDKASYVAWGHSTVVNP WGEVLAKAGTEEAIVYSDIDLKKLAEIRQQIPVFRQKRSDLYAVEMKKP |
| 预测分子量 | 33 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. |
以下是基于假设性研究的参考文献示例，请注意这些信息可能需要进一步验证：
1. **文献名称**：*Cloning and Functional Characterization of Recombinant Human NIT2 Protein*
**作者**：Smith J, et al.
**摘要**：研究报道了人源NIT2基因在大肠杆菌中的重组表达及纯化，证实其具有硝基还原酶活性，为后续代谢研究奠定基础。
2. **文献名称**：*Structural Insights into NIT2 Recombinant Protein via X-ray Crystallography*
**作者**：Brown K, et al.
**摘要**：通过重组NIT2蛋白的晶体结构解析，揭示了其底物结合域的关键氨基酸残基，解释了酶催化机制。
3. **文献名称**：*Role of Recombinant NIT2 in Arginine Metabolism and Cancer Cell Proliferation*
**作者**：Wang Y, et al.
**摘要**：体外实验表明，重组NIT2通过调节精氨酸代谢抑制肝癌细胞生长，提示其潜在抑癌功能。
4. **文献名称**：*Optimization of NIT2 Recombinant Protein Production in Yeast Expression Systems*
**作者**：Zhang L, et al.
**摘要**：比较了酵母系统中NIT2重组蛋白的分泌表达策略，提高了蛋白产量并保留酶活性。
**注意**：以上文献为假设性示例，实际研究需通过PubMed或Google Scholar检索确认。建议使用关键词“NIT2 recombinant protein”或“NIT2 + expression/purification/function”查找最新文献。
**Background of NIT2 Recombinant Protein**
NIT2. a member of the nitrilase superfamily, is a key enzyme involved in nitrogen metabolism, particularly in the detoxification and recycling of nitrogenous compounds. Originally identified in fungi such as *Neurospora crassa* and *Aspergillus nidulans*, NIT2 functions as a ω-amidase, catalyzing the hydrolysis of α-ketoglutarate (α-KG) derivatives like α-ketoglutaramate (KGM) and α-ketosuccinamate (KSM) to produce glutamate and ammonia. This activity links carbon and nitrogen cycles by converting keto acids into metabolically usable forms, supporting cellular growth under nitrogen-limiting conditions.
Structurally, NIT2 contains a conserved catalytic triad (Cys-Glu-Lys) and a flexible substrate-binding pocket, enabling broad substrate specificity. Unlike other nitrilases, it does not require a pyridoxal phosphate (PLP) cofactor, distinguishing its mechanism within the superfamily. Its role extends beyond fungi; homologs exist in plants, bacteria, and mammals, suggesting evolutionary conservation in nitrogen homeostasis.
Recombinant NIT2 is produced via heterologous expression in *E. coli* or yeast systems, often fused with tags (e.g., His-tag) for purification. Studies leverage this protein to explore its enzymatic kinetics, substrate preferences, and potential biotechnological applications. For instance, it is investigated for bioremediation (degrading nitrile pollutants) or biofertilizer development (enhancing nitrogen use efficiency in crops). Additionally, its involvement in glutamine metabolism has sparked interest in cancer and metabolic disorder research, as altered α-KG levels correlate with disease progression.
Overall, NIT2 recombinant protein serves as a versatile tool for deciphering nitrogen-related pathways and developing sustainable solutions in agriculture, environmental science, and medicine. Ongoing research aims to optimize its stability and activity for industrial scalability.
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