Recombinant Protein Expression and Purification

The protein constructs were cloned into pcDNA3.4 vector (GeneArt, Regensburg, Germany), amplified in Escherichia coli and recombinantly expressed using Expi293 cells as described previously [48 (link)]. Seven days after transfection, the proteins were purified using the ÄKTA start system and protein G columns (Cytiva, Uppsala, Sweden) as described previously [49 (link)]. The eluted proteins were aliquoted and stored at − 80 °C until further application.

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Rofo F., Metzendorf N.G., Saubi C., Suominen L., Godec A., Sehlin D., Syvänen S, & Hultqvist G. (2022). Blood–brain barrier penetrating neprilysin degrades monomeric amyloid-beta in a mouse model of Alzheimer’s disease. Alzheimer's Research & Therapy, 14, 180.

Publication 2022

pcDNA3.4 vector protein G columns

Cells Escherichia coli Protein g Proteins Transfection Vector

Corresponding Organization :

Other organizations : Uppsala University

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Variable analysis

independent variables

Protein constructs

dependent variables

Protein expression and purification

control variables

PcDNA3.4 vector
Escherichia coli amplification
Expi293 cells for recombinant expression
Protein G columns for purification
ÄKTA start system for purification

controls

Positive control: Not explicitly mentioned.
Negative control: Not explicitly mentioned.

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