中文摘要：

[目的]原核表达和纯化人多胺调节因子-1（PMF-1）并以此为抗原制备多克隆抗体。[方法]PCR扩增人PMF-1编码序列并构建原核表达质粒。将此质粒转化大肠杆菌后，IPTG诱导PMF-1蛋白表达并在变性条件下用Ni—NTA树脂纯化。将纯化的PMF-1用作抗原免疫大耳白兔以制备抗PMF-1多克隆抗体。ELISA法检测抗体效价，免疫印迹法和细胞免疫化学法分析抗体特异性。[结果]成功构建PMF-1原核表达质粒，在大肠杆菌中IPTG可诱导该质粒高效表达PMF-1蛋白。以纯化的PMF-1蛋白为抗原免疫大耳白兔后，获得高效价的抗PMF-1抗血清（抗体效价为1：128000）。该抗体能与PMF-1蛋白特异性结合，并可用于PMF-1的免疫印迹和细胞免疫化学分析。[结论]成功建立了人PMF-1原核表达和纯化技术，并制备出高特异性的抗PMF-1多克隆抗体，该抗体可用于PMF-1的免疫印迹分析和细胞免疫化学分析。

英文摘要：

[ Objective] To prokaryotic express and purify human polyamine modulated factor - 1 （PMF - 1 ） and to prepare polyclonal antibody against PMF- 1. [ Methods]The DNA sequence for PMF- 1 was amplified by PCR and used to construct prokaryotic expression plasmid. When the plasmid was transformed into E. coli, the expression of PMF- 1 was induced by IPTG and purified by Ni - NTA resin under denaturing condition. The purified PMF - 1 was then used as the antigen to immune flap - eared rabbit to prepare the polyclone antibody against PMF - 1. ELISA was used for detection of antibody titer. Western Blot and cellular immunochemistry analysis were performed to detect antibody specificity. [ Results ] The prokaryotic expression plasmid of PMF - 1 was constructed successfully. In E. coli, the plasmid was induced to express PMF - 1 efficiently by IPTG. When the purified PMF- 1 was used as the antigen to immune rabbit,the PMF- 1 polyclone antiserum with high titer （1：128 000） was obtained. This antibody could specifically bind with PMF - 1 and be used for PMF - 1 analysis in Western Blot and cellular immunohistochemistry. [ Conclusion ] The prokaryotic expression and purification techniques for human PMF - 1 were established successfully and a highly specific polyclonal antibody against PMF - 1 was obtained which can be used in Western Blot and cellular immunochemistry analysis for PMF - 1.