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chemically synthesized nucleotide sequence  (Sangon Biotech)

 
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    Sangon Biotech chemically synthesized nucleotide sequence
    Chemically Synthesized Nucleotide Sequence, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/chemically+synthesized+nucleotide+sequence/synthesized+hem+nucleotide+sequence/pm39378924-54-1-12
    Average 90 stars, based on 1 article reviews
    chemically synthesized nucleotide sequence - by Bioz Stars, 2026-10
    90/100 stars

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    Related Articles

    Sequencing:

    Article Title: Cofactor-dependence alteration of 7β-hydroxysteroid dehydrogenase: Enhancing one-pot synthesis efficiency of chenodeoxycholic acid to ursodeoxycholic acid through cofactor self-recycling.
    Article Snippet: NAD-dependent 7α-hydroxysteroid dehydrogenase (7α-HSDH) and NADPH-dependent 7β-hydroxysteroid dehydrogenase (7β-HSDH) are involved in the biosynthesis of chenodeoxycholic acid (CDCA) to ursodeoxycholic acid (UDCA).. To realize the one-pot synthesis of CDCA to UDCA through NAD-NADH cycling, we aimed to improve the binding ability of Hyphomicrobium sp. 7β-HSDH to NADH.. The 7β-HSDH structure was modeled and some potential residues to improve NADH affinity near conserved cofactor binding regions were screened, including Ala22, Gln23, Asn24, Asp44, Leu45, and Asn46.

    Synthesized:

    Article Title: Cofactor-dependence alteration of 7β-hydroxysteroid dehydrogenase: Enhancing one-pot synthesis efficiency of chenodeoxycholic acid to ursodeoxycholic acid through cofactor self-recycling.
    Article Snippet: NAD-dependent 7α-hydroxysteroid dehydrogenase (7α-HSDH) and NADPH-dependent 7β-hydroxysteroid dehydrogenase (7β-HSDH) are involved in the biosynthesis of chenodeoxycholic acid (CDCA) to ursodeoxycholic acid (UDCA).. To realize the one-pot synthesis of CDCA to UDCA through NAD-NADH cycling, we aimed to improve the binding ability of Hyphomicrobium sp. 7β-HSDH to NADH.. The 7β-HSDH structure was modeled and some potential residues to improve NADH affinity near conserved cofactor binding regions were screened, including Ala22, Gln23, Asn24, Asp44, Leu45, and Asn46.



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    Construction of stable and functional <t>Nluc‐based</t> luciferase‐producing Staphylococcus aureus reporter strains. (A) Western blot analysis of the expression of PBP2a, Eno, CobB, and SarA in S. aureus USA300 over time. The protein gel served as a loading control (Lc), and the molecular weights of the protein markers (M) are indicated on the left. (B) Semi‐quantitative analysis of the gray values of the indicated bands in each lane of (A) using ImageJ software. Data are presented as mean ± SEM. Statistical significance was calculated by two‐way analysis of variance (ANOVA); ns indicates no significance, ** p < 0.01, and *** p < 0.001. (C) Western blot analysis of Eno fusion proteins in the total cell lysates using mouse anti‐Eno polyclonal antibodies. (D) Bioluminescence (BL) photographs of different S. aureus reporter strain and substrate combinations. (E) Representative BL images of 50 µl of S. aureus reporter strains (1 × 10 7 CFU/ml) mixed with 50 µl of different doses of HFZ, FUR, or DTZ (3.125–100 µM). (F) Quantification of total flux produced from S. aureus reporter strains with different concentrations of substrates. Data are presented as mean ± SEM. Statistical significance was analyzed by two‐way ANOVA; ns indicates no significance, * p < 0.05, ** p < 0.01, and *** p < 0.001. (G) Images of BL signals from <t>USA300/Eno‐Nluc,</t> <t>USA300/Eno‐Teluc,</t> and USA300/Eno‐Antares2 over a range of bacterial loads with 50 µl of HFZ (100 µM) in the black 96‐well plates. (H) Good correlation between the BL intensity and bacterial number of S. aureus USA300/Eno‐Nluc, USA300/Eno‐Teluc, or USA300/Eno‐Antares2. The experiment was repeated at least three times in triplicate. Data are presented as mean ± SEM. x , bacterial number; y , BL intensity.
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    Image Search Results


    Construction of stable and functional Nluc‐based luciferase‐producing Staphylococcus aureus reporter strains. (A) Western blot analysis of the expression of PBP2a, Eno, CobB, and SarA in S. aureus USA300 over time. The protein gel served as a loading control (Lc), and the molecular weights of the protein markers (M) are indicated on the left. (B) Semi‐quantitative analysis of the gray values of the indicated bands in each lane of (A) using ImageJ software. Data are presented as mean ± SEM. Statistical significance was calculated by two‐way analysis of variance (ANOVA); ns indicates no significance, ** p < 0.01, and *** p < 0.001. (C) Western blot analysis of Eno fusion proteins in the total cell lysates using mouse anti‐Eno polyclonal antibodies. (D) Bioluminescence (BL) photographs of different S. aureus reporter strain and substrate combinations. (E) Representative BL images of 50 µl of S. aureus reporter strains (1 × 10 7 CFU/ml) mixed with 50 µl of different doses of HFZ, FUR, or DTZ (3.125–100 µM). (F) Quantification of total flux produced from S. aureus reporter strains with different concentrations of substrates. Data are presented as mean ± SEM. Statistical significance was analyzed by two‐way ANOVA; ns indicates no significance, * p < 0.05, ** p < 0.01, and *** p < 0.001. (G) Images of BL signals from USA300/Eno‐Nluc, USA300/Eno‐Teluc, and USA300/Eno‐Antares2 over a range of bacterial loads with 50 µl of HFZ (100 µM) in the black 96‐well plates. (H) Good correlation between the BL intensity and bacterial number of S. aureus USA300/Eno‐Nluc, USA300/Eno‐Teluc, or USA300/Eno‐Antares2. The experiment was repeated at least three times in triplicate. Data are presented as mean ± SEM. x , bacterial number; y , BL intensity.

    Journal: Mlife

    Article Title: Optimizing a high‐sensitivity NanoLuc‐based bioluminescence system for in vivo evaluation of antimicrobial treatment

    doi: 10.1002/mlf2.12091

    Figure Lengend Snippet: Construction of stable and functional Nluc‐based luciferase‐producing Staphylococcus aureus reporter strains. (A) Western blot analysis of the expression of PBP2a, Eno, CobB, and SarA in S. aureus USA300 over time. The protein gel served as a loading control (Lc), and the molecular weights of the protein markers (M) are indicated on the left. (B) Semi‐quantitative analysis of the gray values of the indicated bands in each lane of (A) using ImageJ software. Data are presented as mean ± SEM. Statistical significance was calculated by two‐way analysis of variance (ANOVA); ns indicates no significance, ** p < 0.01, and *** p < 0.001. (C) Western blot analysis of Eno fusion proteins in the total cell lysates using mouse anti‐Eno polyclonal antibodies. (D) Bioluminescence (BL) photographs of different S. aureus reporter strain and substrate combinations. (E) Representative BL images of 50 µl of S. aureus reporter strains (1 × 10 7 CFU/ml) mixed with 50 µl of different doses of HFZ, FUR, or DTZ (3.125–100 µM). (F) Quantification of total flux produced from S. aureus reporter strains with different concentrations of substrates. Data are presented as mean ± SEM. Statistical significance was analyzed by two‐way ANOVA; ns indicates no significance, * p < 0.05, ** p < 0.01, and *** p < 0.001. (G) Images of BL signals from USA300/Eno‐Nluc, USA300/Eno‐Teluc, and USA300/Eno‐Antares2 over a range of bacterial loads with 50 µl of HFZ (100 µM) in the black 96‐well plates. (H) Good correlation between the BL intensity and bacterial number of S. aureus USA300/Eno‐Nluc, USA300/Eno‐Teluc, or USA300/Eno‐Antares2. The experiment was repeated at least three times in triplicate. Data are presented as mean ± SEM. x , bacterial number; y , BL intensity.

    Article Snippet: The nucleotide sequences of nluc, teluc , and antares2 according to the codon usage bias of S. aureus USA300 were chemically synthesized by BGI‐Shenzhen (China) and cloned into the pUC18 plasmid to achieve pUC‐ nluc , pUC‐ teluc , and pUC‐ antares2 , respectively (Table ).

    Techniques: Functional Assay, Luciferase, Western Blot, Expressing, Control, Software, Produced