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Production of integrin αIIbβ3 in stably transfected and clonal Chinese hamster ovary cells for functional and structural studies.
Acta Biochimica et Biophysica Sinica ( IF 3.3 ) Pub Date : 2020-05-23 , DOI: 10.1093/abbs/gmaa055 Li Pan 1 , Ying Lu 2 , Yongmei Zuo 3 , Kechang Qu 1 , Wenlei Ma 1 , Jiafu Liu 1
Acta Biochimica et Biophysica Sinica ( IF 3.3 ) Pub Date : 2020-05-23 , DOI: 10.1093/abbs/gmaa055 Li Pan 1 , Ying Lu 2 , Yongmei Zuo 3 , Kechang Qu 1 , Wenlei Ma 1 , Jiafu Liu 1
Affiliation
The essential prelude for structural biologists is to choose the reasonable expression methods, which are categorized into eukaryotic and prokaryotic expression systems, to obtain sufficient amount of protein for structure determination [1]. For many human proteins, especially membrane receptors, the prokaryotic system cannot be amenable for target-protein expression. It is often difficult to generate properly folded, fully functional eukaryotic proteins in prokaryotes. A variety of eukaryotic expression systems have been explored to overcome this problem, including yeast, insect cells, and mammalian cells [2,3]. The mammalian cell expression system is popular now for the overexpression of mammalian proteins for functional and structural studies. For the expression and purification of heterodimeric membrane proteins, subunit topology and construct design are the other important aspects. The subunits can be expressed in different host cells separately and then reconstituted in vitro. They also can be expressed in the same host cell to form the dimeric proteins in vivo [4–6].
更新日期：2020-05-23
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