纯度 | >85%SDS-PAGE. |
种属 | Human |
靶点 | CASQ1 |
Uniprot No | P31415 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 35-396aa |
氨基酸序列 | QEGLDF PEYDGVDRVI NVNAKNYKNV FKKYEVLALL YHEPPEDDKA SQRQFEMEEL ILELAAQVLE DKGVGFGLVD SEKDAAVAKK LGLTEVDSMY VFKGDEVIEY DGEFSADTIV EFLLDVLEDP VELIEGEREL QAFENIEDEI KLIGYFKSKD SEHYKAFEDA AEEFHPYIPF FATFDSKVAK KLTLKLNEID FYEAFMEEPV TIPDKPNSEE EIVNFVEEHR RSTLRKLKPE SMYETWEDDM DGIHIVAFAE EADPDGFEFL ETLKAVAQDN TENPDLSIIW IDPDDFPLLV PYWEKTFDID LSAPQIGVVN VTDADSVWME MDDEEDLPSA EELEDWLEDV LEGEINTEDD DDDDDD |
预测分子量 | 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CASQ1重组蛋白的3篇参考文献及其摘要概括:
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1. **文献名称**:*"Characterization of human skeletal calsequestrin (CASQ1) recombinant protein in vitro"*
**作者**:Treves S., et al.
**摘要**:该研究通过大肠杆菌系统成功表达并纯化了人源CASQ1重组蛋白,分析了其钙离子结合能力及聚合特性。结果显示,CASQ1在低钙条件下为单体,高钙浓度下形成多聚体,证实其在肌质网钙缓冲中的动态调控作用。
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2. **文献名称**:*"Structural and functional analysis of CASQ1 mutations linked to malignant hyperthermia"*
**作者**:Kalyanasundaram A., et al.
**摘要**:本研究通过哺乳动物细胞表达系统获得CASQ1重组蛋白,探讨与恶性高热相关的多个突变体(如R54H)对钙亲和力及蛋白稳定性的影响,发现部分突变导致钙结合能力显著下降,提示其病理机制与钙调控异常相关。
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3. **文献名称**:*"Calsequestrin polymerization: Role of recombinant CASQ1 in sarcoplasmic reticulum luminal organization"*
**作者**:Dirksen R.T., et al.
**摘要**:利用重组CASQ1蛋白结合电子显微镜技术,揭示其在高钙环境下形成线性聚合物的结构特征,并证明这种聚合能力对维持肌质网管腔结构和钙存储容量至关重要。
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**备注**:以上文献为示例,实际引用需核对具体作者及期刊信息。如需更近期研究,建议通过PubMed或Google Scholar检索关键词“CASQ1 recombinant protein”。
CASQ1 (Calsequestrin-1) is a calcium-binding protein predominantly expressed in the sarcoplasmic reticulum (SR) of skeletal muscle cells. As a low-affinity, high-capacity calcium buffer, it plays a critical role in regulating intracellular calcium homeostasis during excitation-contraction coupling. CASQ1 polymerizes into linear filaments, forming a dynamic calcium reservoir that sequesters free Ca²⁺ ions during muscle relaxation and releases them rapidly upon depolarization to trigger contraction. Its structure includes acidic residues that coordinate calcium ions and a thioredoxin-like domain implicated in polymerization.
Recombinant CASQ1 is produced using heterologous expression systems (e.g., *E. coli* or mammalian cells) to study its biophysical properties, calcium-handling mechanisms, and interactions with partner proteins like junctophilins and triadin. This engineered protein retains native structural and functional features, enabling *in vitro* investigations into calcium buffering kinetics, polymerization dynamics, and redox sensitivity. Researchers utilize recombinant CASQ1 to model skeletal muscle calcium signaling pathologies, including malignant hyperthermia and tubular aggregate myopathy linked to CASQ1 mutations.
The development of recombinant CASQ1 has advanced understanding of SR calcium storage mechanisms and disease mechanisms caused by its dysfunction. It also serves as a tool for drug screening targeting calcium-related muscle disorders. Recent studies explore its potential role beyond muscle cells, such as in neurodegenerative conditions involving calcium dysregulation. However, challenges remain in mimicking post-translational modifications and SR-like microenvironments *in vitro*. Ongoing research aims to refine recombinant CASQ1 systems to better replicate its native context, facilitating translational studies for therapeutic interventions.
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