CAJ | 학술논문

为了在小鼠模型中更深入地研究 nulp1蛋白在心脏发育中的功能，采用PCR技术扩增出小鼠 nulp1基因的部分编码区并连接入pET-28a表达载体中，之后将重组质粒转入大肠杆菌（ E. coli ）通过IPTG诱导表达His-nulp1融合蛋白，对该融合蛋白采用Ni -IDA凝胶柱层析纯化后，免疫新西兰兔制备了多克隆抗体，并用western blotting对抗体进行分析.结果表明，获得了高效价的特异性兔抗 nulp1多克隆抗体.这为 nulp1功能的进一步研究奠定了基础.
위료재소서모형중경심입지연구 nulp1단백재심장발육중적공능，채용PCR기술확증출소서 nulp1기인적부분편마구병련접입pET-28a표체재체중，지후장중조질립전입대장간균（ E. coli ）통과IPTG유도표체His-nulp1융합단백，대해융합단백채용Ni -IDA응효주층석순화후，면역신서란토제비료다극륭항체，병용western blotting대항체진행분석.결과표명，획득료고효개적특이성토항 nulp1다극륭항체.저위 nulp1공능적진일보연구전정료기출.
To better understand the function of the nulp1 protein in heart development by using Mouse as a model , here , a fraction of the encoded region in the Mouse nulp1 was obtained by PCR amplification , then the fragment was inserted into pET -28a vector to establish the expressing system . The recombinant plasmid was transformed into E . coli and fusion protein was induced by IPTG . The purified protein was obtained by treating New Zealand white rabbits to prepare antibody . The antibody was assayed by Western blotting . The result show that the polyclonal antibody is of high sensitivity and specificity , which lays a solid foundation for the further studies of nulp1 function .