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Novablue

Manufactured by Merck Group
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Sourced in Germany, United States

NovaBlue is a lab equipment product from Merck Group. It is a high-performance competent cell, designed for efficient transformation of bacterial cells. NovaBlue facilitates the cloning and expression of recombinant proteins.

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Lab products found in correlation

Shuffle t7 express, by New England Biolabs (1 mentions) Minipreps, by Qiagen (1 mentions) Pet 41a, by Merck Group (1 mentions) Pet 41a, by New England Biolabs (1 mentions) Wizard plus sv minipreps dna purification system, by Promega (1 mentions) Pshai, by New England Biolabs (1 mentions) T4 dna ligase, by New England Biolabs (1 mentions) Bl21 de3 plys, by Thermo Fisher Scientific (1 mentions) Mouse c2c12 myoblast, by American Type Culture Collection (1 mentions) Bhk 21, by American Type Culture Collection (1 mentions) Bhi media, by Merck Group (1 mentions)

Close spelling variants of this product

Escherichia coli NovaBlue NovaBlue Singles Competent Cells

6 protocols using novablue

1

Recombinant protein production protocols

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The Escherichia coli strains NovaBlue (Novagen, Merck Millipore, Germany) and SHuffle®T7 Express (C3028H, New England Biolabs, Germany) were routinely grown as described previously [6 (link)]. Transformation and selection were carried out following protocols already published [6 (link)]. Experiments to produce WbgU were carried out using TB Medium supplemented with 0.5% d-glucose (Glc). For the production of unglycosylated T7Muc10 5010 Medium (50 g/L yeast extract, 10 g/L peptone, 0.492 g/L magnesium sulfate heptahydrate) was used. Glycosylated T7Muc10 was expressed as described previously in a 24-deepwell plate containing 2 mL EnPresso® B medium in each well and pooled for purification [6 (link)].
Mueller P., Gauttam R., Raab N., Handrick R., Wahl C., Leptihn S., Zorn M., Kussmaul M., Scheffold M., Eikmanns B., Elling L, & Gaisser S. (2018). High level in vivo mucin-type glycosylation in Escherichia coli. Microbial Cell Factories, 17, 168.
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2

Anaerobic Growth of Clostridium difficile

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Clostridium difficile 630 (Sebaihia et al., 2006) and its erythromycin‐sensitive derivative 630Δerm (Hussain et al., 2005) were grown under anaerobic conditions (80%N2, 10% CO2, 10% H2) in an anaerobic incubator (Don Whitley Scientific) on Brain Heart Infusion Supplemented (BHIS) plates or in broth [BHI supplemented with 5 g l−1 yeast extract (BD Bacto), and 1 g l−1 L‐cysteine]. E. coli strains were grown in LB broth and on LB agar supplemented with chloramphenicol (15 μg ml−1), kanamycin (50 μg ml−1) or carbenicillin (50 μg ml−1). E. coli strain NovaBlue (Merck) was used as a recipient for all recombinant plasmids, and strain CA434 (HB101 carrying R702) was used for conjugation of plasmids from E. coli into C. difficile. E. coli Rosetta carrying pLMW630 was described previously (Fagan et al., 2009).
Willing S.E., Candela T., Shaw H.A., Seager Z., Mesnage S., Fagan R.P, & Fairweather N.F. (2015). C lostridium difficile surface proteins are anchored to the cell wall using CWB2 motifs that recognise the anionic polymer PSII. Molecular Microbiology, 96(3), 596-608.
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3

Site-directed Mutagenesis of FabA

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The non-cleavable His6-tagged FabA template was generously provided by Dr. Hirotada at Keio University, Japan. The FabA gene was cloned into the pET28b expression vector and used as the DNA template for site-directed mutagenesis with the mutagenic primer listed in Table S2. Polymerase chain reactions (PCR) were performed using a combination of varying DMSO and magnesium concentration and “step down” annealing temperatures. FabA PCR products were digested with Dpn1 to eliminate template WT FabA. Digested PCR products were transformed into NovaBlue (EMD Millipore). Single colonies were isolated and their plasmids were extracted using Qiagen Minipreps. Site-directed mutagenesis was verified via DNA sequencing (IDT).
Finzel K., Nguyen C., Jackson D.R., Gupta A., Tsai S.C, & Burkart M.D. (2015). Probing the Substrate Specificity and Protein-Protein Interactions of the E. coli Fatty Acid Dehydratase, FabA. Chemistry & biology, 22(11), 1453-1460.
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4

Overexpression of FolE protein from Rickettsia monacensis in E. coli

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To overexpress FolE protein of R. monacensis in E. coli, the expression vector used was pET-41a(+) (EMD Millipore, Billerica, MA), which facilitates the expression of the protein as a fusion product tagged with N-terminal GST. The cloning procedure has been described previously (Bodnar et al., 2018 (link)). Briefly, the folE PCR fragment of R. monacensis and pET-41a(+) plasmid was digested with PshAI (New England Biolabs, Ipswich, MA). Ligation of the gel-purified rickettsial folE PCR amplicon in the plasmid was completed with T4 DNA ligase (New England Biolabs, Ipswich, MA), generating pET41a(+)−folE clone. After ligation, the reaction mix was transformed into competent E. coli strain NovaBlue (EMD Millipore, Billerica, MA). Kanamycin resistant colonies were then cultured in LB broth plus 100 mg/L kanamycin. The Wizard Plus SV Minipreps DNA Purification System (Promega, Madison, WI) was used for plasmid purification. The insert of the pET41a(+)-folE clone was sequenced at Elim Biopharmaceuticals (Elim Biopharmaceuticals, Hayward, CA) with the following vector specific primers: forward primer 5’- AAGAAACCGCTGCTGCTAAA-3′ and reverse primer 5’- AGCTCCGTCGACAAGCTT-3’ (Elim Biopharmaceuticals, Hayward, CA).
Bodnar J., Fitch S., Sanchez J., Lesser M., Baston D.S, & Zhong J. (2020). GTP Cyclohydrolase I Activity from Rickettsia monacensis Strain Humboldt, a Rickettsial Endosymbiont of Ixodes pacificus. Ticks and tick-borne diseases, 11(4), 101434.
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5

Cell Culture Techniques for Protein Expression

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E. coli strains NovaBlue (EMD Millipore, USA) and BL21(DE3)pLysS (Thermo Fisher, USA) were used, respectively, to propagate plasmids and express proteins. BHK21 (#CCL-10) and C2C12 mouse myoblasts (#CRL-1772) cells were purchased from ATCC. BHK was cultured in Dulbecco’s Modified Eagles’ Medium supplemented with 10% fetal bovine serum, 4 mM glutamine, and 4.5 g/L glucose. Myoblasts were cultured as described [29 (link)].
Ngwa V.M., Axford D.S., Healey A.N., Nowak S.J., Chrestensen C.A, & McMurry J.L. (2017). A versatile cell-penetrating peptide-adaptor system for efficient delivery of molecular cargos to subcellular destinations. PLoS ONE, 12(5), e0178648.
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6

Bacterial Culturing Techniques for Meningitis

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E. coli strains DH5α (Invitrogen) and NovaBlue (Merck) were cultured at 37°C on Luria-Bertoni (LB) media. N. meningitidis strains used in this study are summarized in Table 1 and included H44/76 (B:15:P1.7,16:L3,7,9), mutants derived from strain MC58 (B:15:P1.7,16b, with disrupted lgtB[17] or lgtE[17] genes) and H44/76 (disrupted icsB gene [18] (link)), and the disease isolates 91/40 (B:4:P7-2,4) and BZ198 (B:NT:P1.7-2,4). Meningococci were cultured at 37°C in 5% CO2 (v/v) in modified liquid Frantz medium [19] (link) or solid brain heart infusion (BHI) media (Merck) supplemented with Levinthal's reagent (10% v/v).
Mehta O.H., Norheim G., Hoe J.C., Rollier C.S., Nagaputra J.C., Makepeace K., Saleem M., Chan H., Ferguson D.J., Jones C., Sadarangani M., Hood D.W., Feavers I., Derrick J.P., Pollard A.J, & Moxon E.R. (2014). Adjuvant Effects Elicited by Novel Oligosaccharide Variants of Detoxified Meningococcal Lipopolysaccharides on Neisseria meningitidis Recombinant PorA Protein: A Comparison in Mice. PLoS ONE, 9(12), e115713.
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