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Removing a difficult-to-separate byproduct by Capto L affinity chromatography during the purification of a WuXiBody-based bispecific antibody.
Protein Expression and Purification ( IF 1.4 ) Pub Date : 2020-07-29 , DOI: 10.1016/j.pep.2020.105713
Ying Wang 1 , Xiujuan Chen 1 , Ying Wang 1 , Yifeng Li 1
Affiliation  

For IgG-like bispecific antibodies (bsAbs) whose construction involves sequence engineering to promote desired heavy chain-light chain pairing, ¾ antibody (antibody lacking one light chain) is a frequent byproduct during their recombinant production. As this byproduct shares high similarity in physicochemical properties with the target bsAb, its removal poses a challenge to downstream purification. Capto L is an affinity resin based on Protein L, which binds to the variable region of kappa light chain without interfering with the antigen binding site. In this work, we demonstrated that Capto L provides a convenient means for separating ¾ antibody from the bsAb product.



中文翻译:

在基于WuXiBody的双特异性抗体的纯化过程中,通过Capto L亲和色谱去除难以分离的副产物。

对于其构建涉及序列工程以促进所需的重链-轻链配对的IgG样双特异性抗体(bsAbs),3/4抗体(缺乏一个轻链的抗体)是其重组生产中的常见副产物。由于该副产物在理化特性上与目标bsAb具有高度相似性,因此其去除对下游纯化提出了挑战。Capto L是一种基于蛋白质L的亲和树脂,可与κ轻链可变区结合而不会干扰抗原结合位点。在这项工作中,我们证明了Capto L为从bsAb产物中分离出¾抗体提供了一种方便的方法。

更新日期:2020-08-05
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