| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NIT1 |
| Uniprot No | Q86X76 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-327 aa |
| 活性数据 | MLGFITRPPH RFLSLLCPGL RIPQLSVLCA QPRPRAMAIS SSSCELPLVA VCQVTSTPDK QQNFKTCAEL VREAARLGAC LAFLPEAFDF IARDPAETLH LSEPLGGKLL EEYTQLAREC GLWLSLGGFH ERGQDWEQTQ KIYNCHVLLN SKGAVVATYR KTHLCDVEIP GQGPMCESNS TMPGPSLESP VSTPAGKIGL AVCYDMRFPE LSLALAQAGA EILTYPSAFG SITGPAHWEV LLRARAIETQ CYVVAAAQCG RHHEKRASYG HSMVVDPWGT VVARCSEGPG LCLARIDLNY LRQLRRHLPV FQHRRPDLYG NLGHPLS |
| 分子量 | 35.8 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人NIT1蛋白的参考文献示例(内容为虚构示例，仅作参考格式说明)：
1. **文献名称**: *Recombinant Human NIT1 Protein: Expression and Enzymatic Characterization*
**作者**: Zhang Y. et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化重组人NIT1蛋白，验证其水解多种腈类底物的酶活性，揭示其在代谢通路中的潜在作用。
2. **文献名称**: *Structural Insights into the Function of Human NIT1 as a Tumor Suppressor*
**作者**: Li X. et al.
**摘要**: 通过X射线晶体学解析重组人NIT1的三维结构，证明其与肿瘤抑制相关的活性位点突变可能影响细胞凋亡调控。
3. **文献名称**: *Development of a High-Yield NIT1 Recombinant Production System in Insect Cells*
**作者**: Smith J. et al.
**摘要**: 利用杆状病毒-昆虫细胞系统优化NIT1重组蛋白表达，产量较传统方法提高5倍，为大规模药物筛选奠定基础。
4. **文献名称**: *NIT1 Deficiency and Its Role in Neurodegenerative Disorders*
**作者**: Wang H. et al.
**摘要**: 通过重组NIT1蛋白功能实验，发现其缺失可能导致神经毒素代谢异常，与帕金森病病理模型相关。
(注：以上文献为示例，实际需通过学术数据库检索真实文献。)
**Background of Recombinant Human NIT1 Protein**
Nitrilase 1 (NIT1), encoded by the *NIT1* gene, is a member of the nitrilase superfamily, a group of enzymes conserved across species that hydrolyze nitriles, amides, or related compounds. Human NIT1. localized predominantly in the cytoplasm, is implicated in cellular detoxification pathways by processing endogenous or xenobiotic nitriles into carboxylic acids and ammonia. Structurally, it contains a characteristic nitrilase domain and forms homooligomers for catalytic activity. While its precise physiological substrates remain under investigation, NIT1 is hypothesized to participate in metabolite regulation, DNA damage response, and possibly tumor suppression due to its association with apoptosis-related pathways.
Recombinant human NIT1 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to enable functional studies. Its production allows for detailed biochemical characterization, including substrate specificity, kinetic analysis, and interaction mapping. Researchers utilize recombinant NIT1 to explore its enzymatic mechanism, potential roles in cancer biology (e.g., as a tumor suppressor in certain cancers), and connections to metabolic disorders. Additionally, it serves as a tool for drug discovery, targeting enzyme activity modulation or elucidating its involvement in cellular stress responses. Ongoing studies aim to clarify its broader biological significance and therapeutic potential in human diseases.
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