纯度 | > 85 % SDS-PAGE. |
种属 | Human |
靶点 | CALM2 |
Uniprot No | P0DP24 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-149aa |
氨基酸序列 | MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK |
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3篇关于CALM2重组蛋白的文献摘要概括(示例为虚构内容,实际文献需通过学术数据库检索):
1. **《Functional Characterization of Recombinant CALM2 in Cardiac Arrhythmia Models》**
- 作者:Zhang Y. et al.
- 摘要:研究通过大肠杆菌表达系统纯化CALM2重组蛋白,分析其与RyR2通道的相互作用,揭示CALM2突变体导致心律失常的分子机制。
2. **《Structural Insights into CALM2 Recombinant Protein Binding with Target Peptides》**
- 作者:Lee S. et al.
- 摘要:利用X射线晶体学解析CALM2重组蛋白结构,阐明其与Ca²⁺结合后构象变化及与下游靶蛋白的结合模式,为钙信号调控提供结构基础。
3. **《High-Yield Production of Recombinant CALM2 in Mammalian Cells for Drug Screening》**
- 作者:Müller F. et al.
- 摘要:优化哺乳动物细胞中CALM2重组蛋白的表达和纯化工艺,验证其在高通量药物筛选中的应用,用于靶向钙调蛋白的抑制剂开发。
4. **《CALM2 Recombinant Protein Rescue of Calcium Dysregulation in Neurodegenerative Disease Models》**
- 作者:Gomez-Ramos A. et al.
- 摘要:在阿尔茨海默病细胞模型中,外源性CALM2重组蛋白恢复钙稳态,抑制tau蛋白过度磷酸化,提示其潜在治疗价值。
**提示**:实际文献需通过PubMed、Web of Science等平台检索关键词“CALM2 recombinant protein”获取,建议结合具体研究方向筛选。
CALM2 (Calmodulin 2) is a calcium-binding protein critical for regulating cellular calcium signaling. Encoded by the CALM2 gene in humans, it belongs to a family of three conserved calmodulin isoforms (CALM1. CALM2. CALM3) that share nearly identical amino acid sequences but differ in gene regulation and tissue-specific expression. Calmodulin functions as a multifunctional sensor, binding intracellular calcium ions (Ca²⁺) via four EF-hand motifs, which triggers conformational changes enabling interactions with diverse target proteins. These interactions regulate enzymes (e.g., kinases, phosphatases), ion channels, and transcription factors, influencing processes like muscle contraction, neurotransmission, and cell cycle progression.
Recombinant CALM2 protein is produced using biotechnological systems, such as E. coli or mammalian cell cultures, to ensure high purity and functionality. Its production enables detailed in vitro studies of calcium-dependent signaling mechanisms, protein-protein interactions, and structural dynamics. Researchers employ recombinant CALM2 in fluorescence-based Ca²⁺ binding assays, electrophysiology, and structural analyses (e.g., X-ray crystallography, NMR). It also serves as a tool to investigate CALM2 mutations linked to severe cardiac arrhythmias, such as catecholaminergic polymorphic ventricular tachycardia (CPVT) and long QT syndrome (LQTS), where altered Ca²⁺ sensing disrupts cardiac ion channel regulation (e.g., RyR2. CaV1.2). By studying mutant recombinant CALM2 proteins (e.g., N98S, D96G), scientists aim to unravel pathological mechanisms and develop targeted therapies. Its applications extend to drug screening and validating calmodulin-targeting compounds, highlighting its importance in both basic research and translational medicine.
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