| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NT5C |
| Uniprot No | Q8TCD5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-201aa |
| 氨基酸序列 | MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRLLSWSDNWREILDSKRGAAQRE |
| 预测分子量 | 28.4 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NT5C重组蛋白的3篇参考文献及其摘要：
1. **《Activating mutations in NT5C2 in acute lymphoblastic leukemia》**
- 作者：Tzoneva, G. 等
- 摘要：该研究报道了NT5C2基因在复发型急性淋巴细胞白血病(ALL)中的激活突变，并通过重组蛋白表达证实突变体导致核苷酸酶活性异常，促进化疗药物代谢和耐药性。
2. **《Structural basis of substrate specificity in human cytosolic 5'-nucleotidase II (NT5C2)》**
- 作者：Wallden, K. 等
- 摘要：研究利用重组NT5C2蛋白进行X射线晶体学分析，解析其三维结构，揭示了底物结合位点的关键氨基酸残基，解释了该酶对核苷酸底物的选择性。
3. **《Biochemical characterization of human NT5C3A protein expressed in E. coli》**
- 作者：Hsu, C.L. 等
- 摘要：通过大肠杆菌系统表达并纯化重组NT5C3A蛋白，分析其酶动力学参数及镁离子依赖性，探讨其在嘧啶代谢中的潜在功能。
(注：以上文献标题及内容为示例性质，具体文献需通过学术数据库检索确认。)
**Background of NT5C Recombinant Protein**
The NT5C (5'-nucleotidase, cytosolic) family of enzymes plays a critical role in nucleotide metabolism by catalyzing the dephosphorylation of nucleoside monophosphates, regulating intracellular nucleotide pools and maintaining energy homeostasis. Among these, NT5C2 (also known as cN-II) has garnered significant attention due to its involvement in purine and pyrimidine salvage pathways, impacting cellular proliferation and survival. Dysregulation of NT5C activity has been linked to various pathologies, including cancer, autoimmune disorders, and drug resistance.
The development of recombinant NT5C proteins, particularly NT5C2. stems from the need to study its biochemical properties, structural dynamics, and pathological mechanisms. Recombinant NT5C is typically produced using expression systems such as *E. coli* or mammalian cells (e.g., HEK293), enabling large-scale purification for functional studies. These proteins retain enzymatic activity, allowing researchers to investigate substrate specificity, inhibitor interactions, and mutational effects.
A pivotal discovery in NT5C research was the identification of activating mutations in *NT5C2* in relapsed acute lymphoblastic leukemia (ALL), where hyperactive variants drive resistance to thiopurine chemotherapy by enhancing nucleotide degradation. This highlighted NT5C2 as a therapeutic target and spurred efforts to design inhibitors. Recombinant mutant NT5C2 proteins have been instrumental in elucidating these mechanisms and screening potential drugs.
Beyond oncology, NT5C recombinant proteins are used to explore roles in viral replication (e.g., HIV) and inflammatory responses. Structural studies using recombinant NT5C have revealed insights into catalytic domains and allosteric regulation, guiding targeted drug development.
Overall, NT5C recombinant proteins serve as vital tools for advancing understanding of nucleotide metabolism in health and disease, bridging basic research with translational applications in precision medicine.
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