重组DAN技术已经可以用来生产无潜在人类传染因子的合成蛋白。尽管这些蛋白从异质细胞中产生,但其与天然蛋白在结构上与功能上有可比性。重组凝血因子Ⅷ、Ⅸ、Ⅶa和von Willebrand因子与它们在血浆中的相应物的DAN有相同的一级序列,其二级和三级结构相似。经转译修饰后,包括蛋白水解过程,二硫键添加和N-和O-位连接聚糖,γ-位的谷氨酸残基羧化,β-位的天门冬氨酸残基羟化,酪氨酸残基的磺化,和丝氨酸残基的磷酸化,这些转译后的修饰相似但不尽相同。在一些实例中,这些差异会导致重要功能上的不同。如降低重组因子 Recombinant DAN technology has been used to produce synthetic proteins without potential human infectious agents. Although these proteins are produced from heterogeneous cells, they are structurally and functionally comparable to native proteins. Recombinant factor VIII, IX, VIIa and von Willebrand factors have the same primary sequence as their counterparts in plasma, with similar secondary and tertiary structures. After translational modification, including proteolysis, disulfide bond addition and N-and O- linked glycans, carboxylation of glutamic acid residues in the γ-position, hydroxylation of aspartic acid residues in the β-position, Sulfonation of tyrosine residues, and phosphorylation of serine residues, these posttranslational modifications are similar but not identical. In some instances, these differences result in important functional differences. Such as reducing the recombination factor