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Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).
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The plasmid pET16b containing the Costa Rica Fluc gene was used to transform <t>E.</t> <t>coli</t> <t>BL21</t> <t>(DE3)</t> and the colonies were transferred to nitrocellulose, induced with IPTG and screened with luciferin. Bioluminescence was detected on a PhotonIMAGER Optima and the bioluminescent intensity displayed from blue (low intensity) to red (high intensity). The bioluminescent activity of the plated transformants from the primary screen over a 20 second intergral is shown in (A). In (B) randomly picked colonies from the primary screen, were screened for bioluminescent activity. Images were produced using M3 Vision software and the intensity scaling between (A) and (B) is not directly comparable.
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Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).

Journal: Frontiers in Veterinary Science

Article Title: Construction and immunogenicity evaluation of a bivalent nanoparticle based on mi3 displaying porcine circovirus type 2 and type 3 capsid proteins

doi: 10.3389/fvets.2026.1862938

Figure Lengend Snippet: Construction of engineered E. coli strains and protein purification. (A) PCR identification of positive E. coli clones. Lanes 1–3 correspond to BL21-pET28-ST-PCV2 Cap, BL21-pET28-ST-PCV3 Cap, and BL21-pET28-SC-mi3, respectively. (B–D) Expression and purification of recombinant proteins ST-PCV2 Cap, ST-PCV3 Cap, and SC-mi3, respectively. Lanes 1–6 represent whole bacterial lysate, pellet after sonication, supernatant after sonication, Ni column flow-through, wash fraction, and purified protein, respectively. (E) Western blot validation of antigen proteins. Lanes 1, 2 correspond to ST-PCV2 Cap and ST-PCV3 Cap, respectively. (F) Endotoxin removal from recombinant protein solutions. Color intensity represents endotoxin content; numbers indicate endotoxin content (EU/mL).

Article Snippet: The pET28a(+) plasmid for recombinant protein expression and BL21(DE3) E. coli competent cells were purchased from Sangon Biotech (Shanghai) Co., Ltd.

Techniques: Protein Purification, Clone Assay, Expressing, Purification, Recombinant, Sonication, Western Blot, Biomarker Discovery

The plasmid pET16b containing the Costa Rica Fluc gene was used to transform E. coli BL21 (DE3) and the colonies were transferred to nitrocellulose, induced with IPTG and screened with luciferin. Bioluminescence was detected on a PhotonIMAGER Optima and the bioluminescent intensity displayed from blue (low intensity) to red (high intensity). The bioluminescent activity of the plated transformants from the primary screen over a 20 second intergral is shown in (A). In (B) randomly picked colonies from the primary screen, were screened for bioluminescent activity. Images were produced using M3 Vision software and the intensity scaling between (A) and (B) is not directly comparable.

Journal: bioRxiv

Article Title: Bioprospecting Novel Luciferase Genes from Museum Coleoptera

doi: 10.64898/2026.04.21.719859

Figure Lengend Snippet: The plasmid pET16b containing the Costa Rica Fluc gene was used to transform E. coli BL21 (DE3) and the colonies were transferred to nitrocellulose, induced with IPTG and screened with luciferin. Bioluminescence was detected on a PhotonIMAGER Optima and the bioluminescent intensity displayed from blue (low intensity) to red (high intensity). The bioluminescent activity of the plated transformants from the primary screen over a 20 second intergral is shown in (A). In (B) randomly picked colonies from the primary screen, were screened for bioluminescent activity. Images were produced using M3 Vision software and the intensity scaling between (A) and (B) is not directly comparable.

Article Snippet: A gene encoding the proposed Costa Rica Fluc was designed as codon optimised for E. coli and was synthesized by IDT and incorporated into a pET16b vector (Sigma-Aldrich) to enable transformation of E. coli BL21 (DE3) competent cells (Fisher Scientific).

Techniques: Plasmid Preparation, Activity Assay, Produced, Software