MabSelect VH3 蛋白 A 亲和树脂能有效分离含有不同数量 VH3 结构域的抗体种类,并显示出更强的聚集分离能力。

IF 1.4 4区 生物学 Q4 BIOCHEMICAL RESEARCH METHODS
Wanyuan Dong, Rongrong Wang, Yifeng Li
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引用次数: 0

摘要

MabSelect VH3是Cytiva公司最近推出的一种新型蛋白a树脂。根据制造商的说法,MabSelect VH3的蛋白A配体已经被设计成分别破坏和增强其Fc和VH3的结合能力。因此,与常规的蛋白A树脂不同,这种新型蛋白A树脂仅对VH3结构域具有亲和力。供应商建议MabSelect VH3,由于其独特的选择性,可以分离出与产品在VH3结构域数量上不同的副产物。在目前的工作中,通过两个具体的案例,我们证明了MabSelect VH3确实可以有效地分离含有不同数量VH3结构域的物种。此外,我们发现,与常规的蛋白A树脂相比,MabSelect VH3也表现出更好的聚集体分离潜力。因此,对于产品和副产物在VH3结构域数量不同和/或培养收获含有高比例聚集体的情况,MabSelect VH3是比常规蛋白a更好的产品捕获选择,因为它允许同时去除副产物和聚集体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
MabSelect VH3 Protein A affinity resin effectively separates antibody species containing different numbers of VH3 domain and shows improved aggregate separation capability
MabSelect VH3 is a new Protein A resin recently launched by Cytiva. According to the manufacturer, the Protein A ligand of MabSelect VH3 has been engineered to disrupt and reinforce its Fc and VH3 binding capabilities, respectively. Thus, different from regular Protein A resins, this new Protein A resin has affinity for VH3 domain only. The vendor has suggested that MabSelect VH3, owing to its unique selectivity, can separate byproducts that are different from the product in the number of VH3 domain. In the current work, with two concrete cases, we demonstrated that MabSelect VH3 indeed allows effective separation of species containing different numbers of VH3 domain. In addition, we showed that, in comparison to regular Protein A resins, MabSelect VH3 also exhibits improved aggregate separation potential. Thus, for cases where product and byproduct differ in the number of VH3 domain and/or culture harvest contains high percentage of aggregates, MabSelect VH3 is a better alternative than regular Protein A for product capture as it allows simultaneous removal of byproducts and aggregates.
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来源期刊
Protein expression and purification
Protein expression and purification 生物-生化研究方法
CiteScore
3.70
自引率
6.20%
发文量
120
审稿时长
32 days
期刊介绍: Protein Expression and Purification is an international journal providing a forum for the dissemination of new information on protein expression, extraction, purification, characterization, and/or applications using conventional biochemical and/or modern molecular biological approaches and methods, which are of broad interest to the field. The journal does not typically publish repetitive examples of protein expression and purification involving standard, well-established, methods. However, exceptions might include studies on important and/or difficult to express and/or purify proteins and/or studies that include extensive protein characterization, which provide new, previously unpublished information.
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