| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ITPR1 |
| Uniprot No | Q14643 |
| 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 | 313 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ITPR1重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Structure of the human IP3R1 channel in lipid nanodiscs"
**作者**: Fan, G., et al.
**摘要**: 本研究利用冷冻电镜技术解析了重组人源ITPR1(IP3R1)在脂质纳米盘中的高分辨率结构，揭示了其钙离子通道的构象变化及配体结合域的调控机制，为理解ITPR1介导的钙信号传导提供了结构基础。
2. **文献名称**: "Recombinant IP3 receptor exhibits multiple conductance states and regulated by calcium"
**作者**: Sato, M., et al.
**摘要**: 通过表达和纯化重组ITPR1蛋白，结合单通道电生理记录，发现ITPR1具有多种电导状态，并受钙离子浓度动态调控，阐明了其在细胞内钙震荡中的作用机制。
3. **文献名称**: "ITPR1 mutations in spinocerebellar ataxia disrupt receptor function via dominant-negative effects"
**作者**: Bezprozvanny, I., et al.
**摘要**: 研究利用重组ITPR1突变体蛋白，证明某些遗传性小脑共济失调相关突变通过显性负效应破坏钙释放功能，为疾病机制提供了分子层面的解释。
*注：上述文献为示例性质，实际引用时建议通过PubMed或Google Scholar核对最新研究。*
The inositol 1.4.5-trisphosphate receptor type 1 (ITPR1) is a critical intracellular calcium (Ca²⁺) release channel predominantly located on the endoplasmic reticulum membrane. It plays a central role in Ca²⁺ signaling, which regulates diverse cellular processes, including gene expression, apoptosis, metabolism, and synaptic plasticity. ITPR1 is activated by its ligand inositol 1.4.5-trisphosphate (IP3), produced via phospholipase C (PLC)-coupled signaling pathways in response to extracellular stimuli such as hormones, neurotransmitters, or growth factors. Structurally, ITPR1 contains an N-terminal ligand-binding domain, a central modulatory region, and a C-terminal transmembrane domain that forms the ion-conducting pore. Its activity is finely tuned by Ca²⁺ itself (bidirectional regulation), ATP, phosphorylation, and interacting proteins like IRBIT or Bcl-2.
Recombinant ITPR1 protein is engineered for in vitro studies to dissect its structural and functional properties. Produced using heterologous expression systems (e.g., bacterial, insect, or mammalian cells), it enables detailed investigations into channel gating mechanisms, ligand-binding dynamics, and Ca²⁺ flux regulation. Purification methods often involve affinity tags (e.g., His-tag) and chromatography techniques. This recombinant tool has been pivotal in studying ITPR1-related pathologies, such as spinocerebellar ataxia type 15 (SCA15) and Gillespie syndrome, which are linked to ITPR1 mutations causing aberrant Ca²⁺ signaling. Additionally, it aids in drug discovery targeting Ca²⁺ dysregulation in neurological disorders, cancer, and cardiovascular diseases. Recent cryo-EM studies using recombinant ITPR1 have revealed conformational changes during activation, advancing our understanding of its allosteric regulation and therapeutic targeting potential.
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