| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | plc |
| Uniprot No | P98160 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 4197-4391aa |
| 氨基酸序列 | DAPGQYGAYFHDDGFLAFPGHVFSRSLPEVPETIELEVRTSTASGLLLWQGVEVGEAGQGKDFISLGLQDGHLVFRYQLGSGEARLVSEDPINDGEWHRVTALREGRRGSIQVDGEELVSGRSPGPNVAVNAKGSVYIGGAPDVATLTGGRFSSGITGCVKNLVLHSARPGAPPPQPLDLQHRAQAGANTRPCPS |
| 预测分子量 | 27.5 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PLC重组蛋白的3篇参考文献摘要示例：
1. **《Heterologous Expression and Functional Characterization of PLC-β3 in E. coli》**
- 作者：Smith J. et al.
- 摘要：研究通过大肠杆菌表达系统成功克隆并纯化人源PLC-β3重组蛋白，验证其水解磷脂酰肌醇的酶活性，为信号转导研究提供工具。
2. **《Optimization of PLC-γ1 Production in Insect Cells Using Baculovirus System》**
- 作者：Taylor R. & Lee C.
- 摘要：利用杆状病毒-昆虫细胞系统高效表达PLC-γ1.通过亲和层析纯化获得高活性蛋白，并应用于癌症模型中酪氨酸磷酸化调控机制分析。
3. **《Structural Insights into PLC-δ1 via Recombinant Protein Crystallography》**
- 作者：Katan M. et al.
- 摘要：通过哺乳动物细胞表达重组PLC-δ1.解析其PH结构域与IP3结合的晶体结构，揭示其膜定位及钙离子信号激活机制。
注：以上文献信息为示例性质，实际引用需查询具体数据库(如PubMed)获取真实文献。
**Background of PLC Recombinant Proteins**
Phospholipase C (PLC) is a critical enzyme family involved in intracellular signaling, primarily hydrolyzing phosphatidylinositol 4.5-bisphosphate (PIP₂) into two secondary messengers: inositol 1.4.5-trisphosphate (IP₃) and diacylglycerol (DAG). These molecules regulate calcium release and protein kinase C activation, influencing processes like cell proliferation, differentiation, and apoptosis. PLC isoforms (e.g., PLC-β, PLC-γ, PLC-δ) exhibit distinct tissue distribution and regulatory mechanisms, making them vital targets for studying signal transduction pathways.
Recombinant PLC proteins are engineered using genetic cloning and expression systems (e.g., *E. coli*, yeast, or mammalian cells*) to produce purified, functional enzymes for research and industrial applications. Traditional methods of isolating PLC from native tissues are limited by low yield and purity, whereas recombinant technology ensures scalability, consistency, and customization (e.g., tagging for detection or affinity purification).
PLC recombinant proteins are widely used to investigate enzyme kinetics, structure-function relationships, and interactions with regulators like G proteins or receptors. They also serve as tools in drug discovery, particularly for diseases linked to dysregulated signaling (e.g., cancer, immune disorders). Additionally, industrial applications include biocatalysis for synthesizing bioactive molecules.
Advances in protein engineering, such as site-directed mutagenesis, enable the study of PLC isoforms’ specific domains or pathogenic mutations. Furthermore, recombinant systems allow modifications to enhance stability or activity under specific conditions. These innovations underscore the importance of PLC recombinant proteins in both basic research and translational biotechnology, bridging mechanistic insights with therapeutic or biomanufacturing advancements.
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