| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ITPR2 |
| Uniprot No | Q14571 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 全长 |
| 氨基酸序列 | full |
| 预测分子量 | 308 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ITPR2重组蛋白的3篇参考文献示例(内容为模拟虚构，供参考)：
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1. **文献名称**: *Structural insights into IP3R2 channel gating by cryo-EM*
**作者**: Fan G. et al. (2018)
**摘要**: 本研究利用冷冻电镜技术解析了重组人源ITPR2蛋白(在HEK293细胞中表达纯化)的近原子分辨率结构，揭示了其配体结合域的构象变化及钙离子释放的分子机制。
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2. **文献名称**: *Functional characterization of ITPR2 recombinant protein in calcium signaling*
**作者**: Higo T. et al. (2005)
**摘要**: 通过在大肠杆菌和昆虫细胞中重组表达ITPR2蛋白，研究发现其C端结构域对钙离子通道的调控至关重要，并证实其与凋亡相关蛋白Bcl-2的相互作用。
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3. **文献名称**: *Disease-associated mutations alter IP3R2 recombinant protein stability*
**作者**: Alzayady K.J. et al. (2016)
**摘要**: 该文献在哺乳动物细胞中表达了携带遗传病相关突变的ITPR2重组蛋白，发现突变导致蛋白异常聚集并减弱其钙释放能力，为疾病机制提供了分子证据。
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4. **文献名称**: *Tissue-specific splicing variants of ITPR2 exhibit distinct calcium flux properties*
**作者**: Boulware M.J. et al. (2003)
**摘要**: 研究比较了不同组织来源的ITPR2剪接变体重组蛋白的钙信号活性，发现神经元特异性变体对IP3敏感性显著高于其他亚型。
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注：以上文献信息为模拟示例，实际研究中请通过PubMed或Google Scholar检索真实文献。
**Background of ITPR2 Recombinant Protein**
The inositol 1.4.5-trisphosphate receptor type 2 (ITPR2) is a critical intracellular calcium (Ca²⁺) release channel located on the endoplasmic reticulum membrane. It belongs to the IP3 receptor family (IP3R1-3), which regulates Ca²⁺ signaling pathways involved in diverse cellular processes, including metabolism, apoptosis, and gene expression. ITPR2 is predominantly expressed in tissues such as the liver, pancreas, and brain, where it modulates Ca²⁺ flux in response to extracellular stimuli like hormones and neurotransmitters. Dysregulation of ITPR2 is linked to pathologies such as metabolic disorders, neurodegenerative diseases, and cancer.
Recombinant ITPR2 protein is engineered through molecular cloning and expression systems (e.g., mammalian or insect cell lines) to produce functional or truncated forms for research. This allows precise study of its structure, ligand-binding properties (e.g., IP3 and ATP interaction), and regulatory mechanisms (e.g., phosphorylation by kinases). Recombinant ITPR2 is particularly valuable for investigating its role in diseases; for example, mutations in ITPR2 are associated with spinocerebellar ataxia and metabolic syndrome.
Structurally, ITPR2 contains an N-terminal ligand-binding domain, a central regulatory region, and a C-terminal transmembrane channel domain. Recombinant variants may include tagged versions (e.g., GFP or His-tag) for purification, localization, or interaction studies. Its applications span drug discovery, calcium signaling assays, and mechanistic studies of cellular pathways. By enabling targeted manipulation, recombinant ITPR2 advances understanding of Ca²⁺-mediated signaling and its therapeutic potential in treating related disorders.
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