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https://www.selleckchem.com/products/4sc-202.html lactis MG1363. This is the first report of the use of a food grade plasmid that confers the ability to efficiently catalyze the deglycosylation of lignans, isoflavonoids, flavones, and flavanones. The recombinant bacteria of this study would be of value for the development of fermented vegetal foods enriched in bioavailable forms of lignans and flavonoids.Variable domains of heavy chains of camelid heavy-chain antibodies (VHHs) are known as nanobodies. Nanobodies are approximately 15 kDa in size with high affinity to their antigens. They can be easily manipulated and produced in microorganisms. In this study, an alpaca was immunized with purified green fluorescence protein (GFP) and a VHH library from lymphocytes of the immunized alpaca was constructed with a capacity of 6.7 × 107. The library was biopanned against GFP by phage display technique and four unique DNA sequences coding for anti-GFP nanobodies were identified by enzyme-linked immunosorbent assay, named a12, e6, d5, and b9. The four DNA sequences were then cloned into pADL-10b-6×His or pBAD24-Flag-6×His for expression in bacteria. Purified A12, E6, D5, and B9 were demonstrated to bind GFP specifically both in vitro by enzyme-linked immunosorbent assay and native-PAGE analysis and in vivo by immunofluorescence and immunoprecipitation. Taken together, our results demonstrate that anti-GFP nanobodies are successfully selected from the immune library, are produced in bacteria, and are available for basic research.Key Points• Four different GFP binders were successfully obtained from an immune VHH library.• The four GFP binders were successfully purified from bacteria. • Purified GFP binders can bind GFP both in vitro and in vivo and are ready for use in basic research.In the last few decades, there has been a rapid increase in the discovery of drugs from natural products, particularly secondary metabolites. Various efforts have been undertaken to enhance and o

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