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Expression, purification, and identification of the <t>V270</t> proteins of Y. pestis . (A) Lane M: the standard protein marker (Sangon Biotech, Shanghai, China). Lane 1 and 2: induction of rV270 expression at 42°C. Lane 3: uninduced at 37°C. (B) rV270 protein was purified by metal affinity chromatography using the AKTA system and analysed on a 12% SDS‐PAGE stained with coomassie blue. Lane 1–5: rV270 protein was eluted using 100, 150, 200, 250 and 300 mM of imidazole in PBS buffer. (C) Purified rV270 proteins were recognised by HRP‐anti‐HIS antibody using Western blot. Lane 1: control sample. Lane 2: rV270 protein.
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Expression, purification, and identification of the <t>V270</t> proteins of Y. pestis . (A) Lane M: the standard protein marker (Sangon Biotech, Shanghai, China). Lane 1 and 2: induction of rV270 expression at 42°C. Lane 3: uninduced at 37°C. (B) rV270 protein was purified by metal affinity chromatography using the AKTA system and analysed on a 12% SDS‐PAGE stained with coomassie blue. Lane 1–5: rV270 protein was eluted using 100, 150, 200, 250 and 300 mM of imidazole in PBS buffer. (C) Purified rV270 proteins were recognised by HRP‐anti‐HIS antibody using Western blot. Lane 1: control sample. Lane 2: rV270 protein.
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Expression, purification, and identification of the <t>V270</t> proteins of Y. pestis . (A) Lane M: the standard protein marker (Sangon Biotech, Shanghai, China). Lane 1 and 2: induction of rV270 expression at 42°C. Lane 3: uninduced at 37°C. (B) rV270 protein was purified by metal affinity chromatography using the AKTA system and analysed on a 12% SDS‐PAGE stained with coomassie blue. Lane 1–5: rV270 protein was eluted using 100, 150, 200, 250 and 300 mM of imidazole in PBS buffer. (C) Purified rV270 proteins were recognised by HRP‐anti‐HIS antibody using Western blot. Lane 1: control sample. Lane 2: rV270 protein.
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Expression, purification, and identification of the V270 proteins of Y. pestis . (A) Lane M: the standard protein marker (Sangon Biotech, Shanghai, China). Lane 1 and 2: induction of rV270 expression at 42°C. Lane 3: uninduced at 37°C. (B) rV270 protein was purified by metal affinity chromatography using the AKTA system and analysed on a 12% SDS‐PAGE stained with coomassie blue. Lane 1–5: rV270 protein was eluted using 100, 150, 200, 250 and 300 mM of imidazole in PBS buffer. (C) Purified rV270 proteins were recognised by HRP‐anti‐HIS antibody using Western blot. Lane 1: control sample. Lane 2: rV270 protein.

Journal: Veterinary Medicine and Science

Article Title: Isolation of camel single domain antibodies against Yersinia pestis V270 antigen based on a semi‐synthetic single domain antibody library and development of a VHH‐based lateral flow assay

doi: 10.1002/vms3.1532

Figure Lengend Snippet: Expression, purification, and identification of the V270 proteins of Y. pestis . (A) Lane M: the standard protein marker (Sangon Biotech, Shanghai, China). Lane 1 and 2: induction of rV270 expression at 42°C. Lane 3: uninduced at 37°C. (B) rV270 protein was purified by metal affinity chromatography using the AKTA system and analysed on a 12% SDS‐PAGE stained with coomassie blue. Lane 1–5: rV270 protein was eluted using 100, 150, 200, 250 and 300 mM of imidazole in PBS buffer. (C) Purified rV270 proteins were recognised by HRP‐anti‐HIS antibody using Western blot. Lane 1: control sample. Lane 2: rV270 protein.

Article Snippet: The cDNA encoding the Y. pestis V270 (GenBank accession number: AE017043.1) was codon optimised and synthesised (Sangon Biotech, Shanghai, China) for expression in E. coli DH5a.

Techniques: Expressing, Purification, Marker, Affinity Chromatography, SDS Page, Staining, Western Blot, Control