Purification of Recombinant SA01-OmpA Protein

The production of the recombinant SA01-OmpA was described in an earlier study (10 (link)). After the induction of E. coli BL21 (DE3) containing pET26b-SA01-OmpA, cells were sonicated, and SA01-OmpA was purified with Ni-NTA (Nickel Nitrilotriacetic acid) resin using standard protocols from Qiagen. Then, the purified protein was subjected to SDS-PAGE, and the concentration of SA01-OmpA was determined using a bicinchoninic acid (BCA) assay (Parstous, Iran).

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Mohseni Sani N., Talaee M., Akbari A., Ashoori F., Zamani J., Kermani A.A., Shahbani Zahiri H., Presley J., Vali H, & Akbari Noghabi K. (2024). Unveiling the structure-emulsifying function relationship of truncated recombinant forms of the SA01-OmpA protein opens up a new vista in bioemulsifiers. Microbiology Spectrum, 12(2), e03465-23.

Publication 2024

Ni-NTA

Corresponding Organization :

Other organizations : National Institute of Genetic Engineering and Biotechnology, St. Jude Children's Research Hospital, McGill University

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Variable analysis

independent variables

Induction of E. coli BL21 (DE3) containing pET26b-SA01-OmpA

dependent variables

Production and purification of recombinant SA01-OmpA protein
Concentration of SA01-OmpA protein determined using BCA assay

control variables

Sonication of cells
Purification of SA01-OmpA protein using Ni-NTA resin
SDS-PAGE analysis of purified protein

controls

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

Annotations

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