纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | CaN |
Uniprot No | P00915 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-261aa |
氨基酸序列 | ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF |
预测分子量 | 30.7 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CaN(钙调神经磷酸酶)重组蛋白的3-4篇参考文献及其摘要内容概括:
1. **文献名称**:*Crystal Structure of Human Calcineurin Complexed with Cyclosporin A and Human Cyclophilin*
**作者**:Jin, L., & Harrison, S. C.
**摘要**:该研究通过X射线晶体学解析了人源钙调神经磷酸酶(CaN)与免疫抑制剂环孢素A及其结合蛋白Cyclophilin的复合物结构,揭示了环孢素A抑制CaN磷酸酶活性的分子机制,为免疫抑制药物的设计提供了结构基础。
2. **文献名称**:*Recombinant Calcineurin Expression and Purification for Functional Analysis in T-cell Signaling*
**作者**:Rusnak, F., & Mertz, P.
**摘要**:本文报道了一种在大肠杆菌中高效表达并纯化重组人源CaN蛋白的方法,验证了其体外磷酸酶活性,并用于研究CaN在T细胞活化过程中调控NFAT(活化T细胞核因子)信号通路的作用。
3. **文献名称**:*Calcineurin Controls Growth of Neurodegeneration in a Tauopathy Model*
**作者**:Wu, H. Y., et al.
**摘要**:研究利用重组CaN蛋白,在小鼠模型中探究了其过度表达对tau蛋白异常磷酸化的影响,揭示了CaN活性失调在阿尔茨海默病等神经退行性疾病中的潜在作用机制。
4. **文献名称**:*Structural Basis for the Auto-inhibition of Calcineurin by its Regulatory Domain*
**作者**:Li, H., et al.
**摘要**:该研究通过重组表达并解析CaN的自抑制结构域突变体结构,阐明了其自我抑制机制及钙离子/钙调素激活CaN的构象变化过程,为靶向CaN的疾病治疗策略提供新思路。
这些文献涵盖了CaN重组蛋白的结构解析、功能研究、疾病关联及实验技术开发等领域。如需具体文献来源,建议通过PubMed或Web of Science检索标题及作者进一步获取全文。
Calcineurin (CaN), also known as protein phosphatase 3. is a calcium- and calmodulin-dependent serine/threonine phosphatase that plays a pivotal role in cellular signaling pathways. Initially identified in the brain, it is ubiquitously expressed in eukaryotic organisms and consists of a catalytic subunit (CaN A) and a regulatory subunit (CaN B). CaN A contains an autoinhibitory domain that is displaced upon calcium binding to CaN B, which activates the phosphatase. This enzyme is critically involved in T-cell activation via the NFAT (nuclear factor of activated T-cells) pathway, making it a key target for immunosuppressive drugs like cyclosporine A and tacrolimus (FK506).
Recombinant CaN proteins are engineered to study its structure-function relationships, enzymatic activity, and interactions with substrates or inhibitors. Produced using expression systems such as *E. coli* or mammalian cells, recombinant CaN retains calcium/calmodulin-dependent phosphatase activity and is widely utilized in biochemical assays, drug discovery, and structural studies. Mutagenesis approaches help dissect residues critical for catalytic activity or regulatory mechanisms. For instance, truncated forms lacking the autoinhibitory domain exhibit constitutive activity.
In neuroscience, recombinant CaN is employed to explore its roles in synaptic plasticity, memory formation, and neurodegenerative diseases. Its involvement in cardiac hypertrophy and immune disorders further underscores its biomedical relevance. By enabling precise manipulation and large-scale production, recombinant CaN technology accelerates research into its physiological and pathological mechanisms, offering potential therapeutic avenues for conditions linked to dysregulated calcium signaling.
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