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利用ＤＮＡ重组技术在大肠杆菌中表达出白细胞介素８的Ｎ端４３氨基酸片段（ＩＬ８－Ｎ）和Ｃ端２４氨基酸片段（ＩＬ８－Ｃ），经过ＦＡＣＳ和趋化活性鉴定表明，ＩＬ８－Ｎ和ＩＬ８－Ｃ均能与中性粒细胞结合，其中ＩＬ８－Ｎ能部分封闭ＩＬ－８的趋化活性。
The N-terminal 43 amino acid fragment (IL8-N) and the C-terminal 24 amino acid fragment (IL8-C) of interleukin-8 were expressed in E.coli by using DNA recombination technology. FACS and chemotactic activity assays showed that IL8-N and IL8-C can bind to neutrophils, IL8-N partially blocked the chemotactic activity of IL-8.