| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | IDI2 |
| Uniprot No | Q9BXS1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-227aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL HRAFSVVLFN TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD AIGVRRAAQR RLQAELGIPG EQISPEDIVF MTIYHHKAKS DRIWGEHEIC YLLLVRKNVT LNPDPSETKS ILYLSQEELW ELLEREARGE VKVTPWLRTI AERFLYRWWP HLDDVTPFVE LHKIHRV |
| 预测分子量 | 29 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IDI2重组蛋白的3篇参考文献摘要概括(注：文献为示例性内容，实际引用需检索具体数据库)：
1. **文献名称**：*"Functional characterization of recombinant human IDI2 in isoprenoid biosynthesis"*
**作者**：Smith J, et al.
**摘要**：本研究通过在大肠杆菌中重组表达人源IDI2蛋白，验证其异戊二烯基二磷酸异构酶活性。结果显示，IDI2对类固醇合成的中间产物(如法尼基焦磷酸)具有催化能力，且其酶活性依赖锌离子，与IDI1存在组织特异性差异(如睾丸中高表达)。
2. **文献名称**：*"Cloning and expression analysis of IDI2 gene in mouse tissues"*
**作者**：Zhang L, et al.
**摘要**：该研究克隆了小鼠IDI2基因，并在原核系统中成功表达重组蛋白。通过酶动力学分析，发现IDI2对底物异戊烯基焦磷酸(IPP)的亲和力低于IDI1.但在睾丸和肾上腺中的表达显著高于其他组织，提示其在生殖和类固醇激素合成中的特殊作用。
3. **文献名称**：*"Structural insights into IDI2: Crystallographic study of the recombinant enzyme"*
**作者**：Brown K, et al.
**摘要**：通过X射线晶体学解析了重组人源IDI2的三维结构，发现其活性中心含保守的金属结合位点。与IDI1相比，IDI2的底物通道更狭窄，可能影响其催化效率，这为开发针对IDI2的特异性抑制剂提供了结构基础。
4. **文献名称**：*"Role of IDI2 in steroidogenesis: Knockdown and recombinant protein rescue studies"*
**作者**：Yamamoto S, et al.
**摘要**：利用siRNA敲低IDI2后，睾丸间质细胞的睾酮合成显著减少;补充重组IDI2蛋白可部分恢复代谢通路活性，证实IDI2在类固醇生成中的必要性，尤其在生殖系统中可能作为IDI1的功能补偿因子。
(注：以上文献信息为模拟内容，实际研究需参考真实发表的论文。)
**Background of IDI2 Recombinant Protein**
Isopentenyl diphosphate isomerase 2 (IDI2) is a key enzyme in the isoprenoid biosynthesis pathway, a metabolic route critical for producing diverse biomolecules, including sterols, terpenes, and vitamins. IDI2 catalyzes the reversible isomerization of isopentenyl diphosphate (IPP) to dimethylallyl diphosphate (DMAPP), two foundational precursors for synthesizing isoprenoids. While most eukaryotes and bacteria rely on a single isoform (IDI1), vertebrates uniquely express two isoforms: IDI1 and IDI2. IDI2 shares structural and functional similarities with IDI1 but exhibits distinct tissue-specific expression patterns, suggesting specialized roles in certain physiological contexts.
The IDI2 gene is evolutionarily conserved and thought to arise from gene duplication. Unlike IDI1. which is ubiquitously expressed, IDI2 shows restricted expression in tissues such as the liver, brain, and reproductive organs. This divergence hints at its potential involvement in tissue-specific isoprenoid regulation or stress responses. Studies also suggest IDI2 may function under varying cellular conditions, such as oxidative stress, where its activity could influence redox-sensitive pathways.
Recombinant IDI2 protein is engineered using heterologous expression systems (e.g., *E. coli* or yeast) to enable biochemical and structural studies. Its production allows researchers to explore enzyme kinetics, substrate specificity, and inhibition mechanisms, providing insights into isoprenoid metabolism regulation. Additionally, recombinant IDI2 serves as a tool for drug discovery, particularly in targeting diseases linked to dysregulated isoprenoid synthesis, such as cancer or metabolic disorders.
Despite progress, IDI2’s precise physiological roles and regulatory mechanisms remain incompletely understood. Ongoing research aims to clarify its contribution to cellular homeostasis and its potential as a therapeutic target, highlighting its importance in both basic and applied biosciences.
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