野类型的人的联系船边交货的死亡领域(FADD ) 蛋白质在 Escherichia coli 被表示为他的标签熔化蛋白质。Recombinant FADD 蛋白质在使中毒的条件下面被净化。在使中毒的蛋白质纯化以后,它是 refolded 并且在大约 23 mg/L 的收益获得了。净化了作为相应于 31 kDa 的分子的重量的一个同质的乐队展出的 FADD。对 refolded FADD 蛋白质的兔子的免疫被给予高 titre polyclonal 抗血清的生产。这新 polyclonal 抗体能在西方的污点认出 recombinant FADD 蛋白质。Immunoreactivity 也在 immunofluorescence 试金被观察。低费用 polyclonal 抗血清对在各种各样的免疫分析的 FADD 的广泛的察觉适用。
The wild-type human Fas-associated death domain (FADD) protein was expressed as a His-tag fusion protein in Escherichia coll. Recombinant FADD proteins were purified under the denatured condition. After denatured protein purification, it was refolded and obtained at a yield of about 23 mg/L. Purified FADD exhibited as a homogenous band corresponding to the molecular weight of 31 kDa. Immunization of rabbits against the refolded FADD protein was allowed the production of high titre polyclonal antiserum. This new polyelonal antibody could recognize recombinant FADD protein in Western blot. Immunoreactivity was also observed in immunofiuorescence assay. The low cost polyclonal antiserum was applicable to extensive detection of FADD in various immunoassays. Cellular & Molecular Immunology. 2008;5(6):471-474.