| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | PLN |
| Uniprot No | P26678 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-30aa |
| 氨基酸序列 | MEKVQYLTRSAIRRASTIEMPQQARQKLQN |
| 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3篇与PLN(磷酸酶调节蛋白，Phospholamban)重组蛋白相关的研究文献摘要：
---
1. **文献名称**：*"Structural dynamics of phospholamban in oriented lipid bilayers by solid-state NMR"*
**作者**：Traaseth, N.J., et al.
**摘要**：利用固态核磁共振技术解析重组人源PLN在脂质双层中的构象变化，揭示其与钙泵(SERCA)相互作用的动态机制，为心脏疾病相关突变研究提供结构基础。
---
2. **文献名称**：*"Recombinant phospholamban: expression, purification, and functional characterization in regulating SERCA activity"*
**作者**：Chen, Z., et al.
**摘要**：报道通过大肠杆菌系统高效表达重组PLN蛋白的纯化方法，并验证其在体外通过磷酸化调节SERCA活性的功能，为药物筛选提供可靠蛋白来源。
---
3. **文献名称**：*"Adenovirus-mediated gene transfer of phospholamban mutants in cardiomyocytes"*
**作者**：Hoshijima, M., et al.
**摘要**：通过腺病毒载体在心肌细胞中表达重组PLN突变体(如S16E模拟磷酸化)，证实其可逆转心力衰竭模型中SERCA功能的抑制，提出基因治疗潜在策略。
---
4. **文献名称**：*"Phospholamban pentamerization increases sensitivity to oxidative stress: Insights from recombinant protein models"*
**作者**：Ha, K.N., et al.
**摘要**：研究重组PLN单体与五聚体形式对氧化应激的响应差异，发现五聚体构象易受活性氧破坏，可能参与心肌缺血再灌注损伤的分子机制。
---
这些研究涵盖了PLN重组蛋白的结构解析、功能验证、疾病模型应用及病理机制探索，可为进一步研究提供参考。
Phospholamban (PLN) is a critical regulatory protein in cardiac muscle cells, primarily involved in calcium homeostasis. It acts as a reversible inhibitor of the sarcoplasmic reticulum Ca²⁺-ATPase (SERCA2a), the pump responsible for reuptaking cytosolic calcium into the SR during cardiac relaxation. By binding to SERCA2a, PLN reduces its affinity for calcium, thereby modulating the rate and strength of cardiac contractions. This dynamic regulation is fine-tuned through phosphorylation: when phosphorylated (e.g., by protein kinase A or Ca²⁺/calmodulin-dependent kinase), PLN dissociates from SERCA2a, relieving inhibition and enhancing calcium reuptake, which accelerates relaxation and improves contractility.
Structurally, PLN exists as a monomer or pentamer. The monomeric form is biologically active, while the pentameric form may serve as a storage pool. Its 52-amino-acid sequence includes a transmembrane domain and cytoplasmic regions with phosphorylation sites (Ser16 and Thr17). Mutations in PLN, such as the R14del variant, are linked to inherited cardiomyopathies like dilated cardiomyopathy (DCM) and arrhythmias, highlighting its clinical relevance.
Recombinant PLN protein, produced via bacterial (e.g., E. coli) or eukaryotic expression systems, is widely used to study its biochemical interactions, structural dynamics, and disease-associated mutations. Purified PLN allows in vitro analysis of SERCA2a binding, phosphorylation effects, and screening of therapeutic compounds targeting calcium dysregulation. Engineered variants, including phosphomimetic or dominant-negative mutants, help dissect molecular mechanisms underlying heart failure. Additionally, recombinant PLN supports structural studies (NMR, crystallography) to visualize conformational changes critical for SERCA2a regulation. As a research tool, it bridges molecular insights to potential therapies for calcium-handling disorders, emphasizing its role in both basic science and translational cardiology.
×
