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中文摘要：
促分裂原活化蛋白激酶（MAPK）在信号传导过程中发挥着重要的作用。以高山离子芥叶片为材料,利用RT-PCR法克隆到全长CbMAPK3基因cDNA,将其与大肠杆菌表达载体pET-30a连接,构建原核表达载体pET-30a-CbMAPK3,并转化大肠杆菌BL21,经IPTG诱导表达后,SDS-PAGE以及Western blot检测结果表明该基因表达了1个约46kD的蛋白,为进一步研究目的蛋白的结构和功能提供了实验基础。
英文摘要：
Mitogen-activated protein kinase （MAPK） plays a central role in transfer information from diverse receptors/sensors to a wide range of cellular responses in plants. CbMAPK3 cDNA was amplified by RT-PCR from Chorispora bungeana leaf, then was cloned into pET-30a vector to construct recombinant prokaryotic expression vector pET-30a-CbMAPK3. The pET-30a-CbMAPK3 was transformed to E. coli strain of BL21. After induced by IPTG, a 46 kD recombinant protein was expressed and separated by SDS-PAGE electrophoresis and detected by western blot. The research provides a base for further studying on the protein structure and function of CbMAPK3.
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