| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | JPH1 |
| Uniprot No | Q9HDC5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-661aa |
| 氨基酸序列 | MTGGRFDFDDGGTYCGGWEEGKAHGHGICTGPKGQGEYSGSWSHGFEVVGGYTWPSGNTYQGYWAQGKRHGLGVETKGKWMYRGEWSHGFKGRYGVRQSLCTPARYEGTWSNGLQDGYGVETYGDGGTYQGQWAGGMRHGYGVRQSVPYGMATVIRSPLRTSLASLRSEQSNGSVLHDAAAAADSPAGTRGGFVLNFHADAELAGKKKGGLFRRGSLLGSMKLRKSESKSSISSKRSSVRSDAAMSRISSSDANSTISFGDVDCDFCPVEDHVDATTTETYMGEWKNDKRNGFGVSERSNGMKYEGEWANNKRHGYGCTVFPDGSKEEGKYKNNILVRGIRKQLIPIRHTKTREKVDRAIEGAQRAAAMARTKVEIANSRTAHARAKADAADQAALAARQECDIARAVARELSPDFYQPGPDYVKQRFQEGVDAKENPEEKVPEKPPTPKESPHFYRKGTTPPRSPEASPKHSHSPASSPKPLKKQNPSSGARLNQDKRSVADEQVTAIVNKPLMSKAPTKEAGAVVPQSKYSGRHHIPNPSNGELHSQYHGYYVKLNAPQHPPVDVEDGDGSSQSSSALVHKPSANKWSPSKSVTKPVAKESKAEPKAKKSELAIPKNPASNDSCPALEKEANSGPNSIMIVLVMLLNIGLAILFVHFLT |
| 预测分子量 | 71,6 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JPH1重组蛋白的模拟参考文献示例(注：部分信息为合理模拟，建议通过学术数据库核实具体文献)：
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1. **标题**：Recombinant Human Junctophilin-1 Expression and Its Role in Calcium Signaling
**作者**：T. Nakamura et al.
**摘要**：本研究成功在大肠杆菌系统中表达并纯化了重组人源JPH1蛋白，验证其与肌浆网RyR受体(Ryanodine Receptor)的相互作用。实验表明，JPH1重组蛋白可通过稳定细胞膜与内质网的连接，增强钙离子释放的协同性，为心律失常机制研究提供工具。
2. **标题**：Structural Insights into JPH1-Mediated Membrane Contact Sites
**作者**：L. Chen & M. Walters
**摘要**：通过冷冻电镜解析重组JPH1蛋白的晶体结构，揭示其N端膜结合域和C端α-螺旋结构域的构象变化。该研究提出JPH1通过双亲螺旋结构介导膜间锚定，为理解膜接触位点(MCS)的形成机制提供结构基础。
3. **标题**：JPH1 Deficiency and Cardiac Hypertrophy: Rescue by Recombinant Protein Delivery
**作者**：R. Gupta et al.
**摘要**：在JPH1基因敲除小鼠模型中，外源性重组JPH1蛋白通过腺病毒递送可部分恢复心肌细胞钙瞬变振幅，缓解病理性心脏肥厚。结果表明JPH1在维持心肌钙稳态中起关键作用。
4. **标题**：JPH1 Recombinant Protein Binds to β-Subunit of CaV1.2 in Neuronal Cells
**作者**：S. Park et al.
**摘要**：通过免疫共沉淀证实重组JPH1蛋白与神经元L型钙通道(CaV1.2)的β亚基直接结合，调控突触钙信号传递。该发现提示JPH1可能参与神经退行性疾病中的钙失调病理。
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**提示**：上述文献为示例性质，实际研究中建议通过PubMed或Google Scholar以关键词“JPH1 recombinant protein”、“Junctophilin-1 expression”等检索最新文献。
**Background of JPH1 Recombinant Protein**
Junctophilin-1 (JPH1) is a member of the junctophilin family, critical proteins involved in forming and stabilizing membrane contact sites between the endoplasmic/sarcoplasmic reticulum (ER/SR) and plasma membrane in excitable cells. Encoded by the *JPH1* gene, this protein is predominantly expressed in cardiac and skeletal muscle tissues, where it facilitates coordinated calcium signaling by physically coupling voltage-gated calcium channels on the cell surface with ryanodine receptors (RyRs) on the SR. Structurally, JPH1 contains an N-terminal membrane occupation and recognition nexus (MORN) domain for SR membrane binding and a C-terminal α-helical region that interacts with plasma membrane components.
Recombinant JPH1 protein is produced using biotechnological platforms, such as bacterial (*E. coli*) or mammalian expression systems, followed by purification via affinity chromatography. Its production enables detailed study of JPH1’s role in maintaining junctional membrane complexes, calcium homeostasis, and excitation-contraction coupling. Dysregulation of JPH1 has been implicated in cardiovascular diseases, including cardiomyopathies, and neuromuscular disorders. Research utilizing recombinant JPH1 also explores its potential as a therapeutic target or biomarker for conditions linked to calcium signaling defects.
Current challenges in JPH1 research include resolving its full 3D structure, understanding post-translational modifications, and elucidating its interactions with other regulatory proteins. Advances in recombinant protein technology continue to support investigations into JPH1’s pathophysiology and its applications in drug discovery or gene therapy strategies.
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