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chitin binding domain intein bmgcl fusion protein  (New England Biolabs)


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    New England Biolabs chitin binding domain intein bmgcl fusion protein
    Chitin Binding Domain Intein Bmgcl Fusion Protein, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/intein+fusions/pm36637620-46-18-29
    Average 86 stars, based on 1 article reviews
    chitin binding domain intein bmgcl fusion protein - by Bioz Stars, 2026-10
    86/100 stars

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    Related Articles

    Expressing:

    Article Title: Hedgehog Pathway Activation Requires Coreceptor-Catalyzed, Lipid-Dependent Relay of the Sonic Hedgehog Ligand
    Article Snippet: .. Bacterial Expression and Purification of Proteins Proteins were expressed in E. coli (BL21 DE3 pLysS, Novagen) as 6×His-tagged (pET, Millipore), MBP-tagged (pMAL, NEB), or GST-tagged (pGEX, GE Healthcare) variants, or as intein fusions (IMPACT-TWIN system, NEB). ..

    Purification:

    Article Title: Hedgehog Pathway Activation Requires Coreceptor-Catalyzed, Lipid-Dependent Relay of the Sonic Hedgehog Ligand
    Article Snippet: .. Bacterial Expression and Purification of Proteins Proteins were expressed in E. coli (BL21 DE3 pLysS, Novagen) as 6×His-tagged (pET, Millipore), MBP-tagged (pMAL, NEB), or GST-tagged (pGEX, GE Healthcare) variants, or as intein fusions (IMPACT-TWIN system, NEB). ..

    Article Title: Structure-Function Dissection of Myxococcus xanthus CarD N-Terminal Domain, a Defining Member of the CarD_CdnL_TRCF Family of RNA Polymerase Interacting Proteins
    Article Snippet: .. CarDNt and CarD 1–72 were overexpressed as intein fusions and purified using chitin resin with the intein tag removed by on-column intramolecular cleavage in the presence of 50 mM dithiothreitol using the IMPACT kit and protocols (New England Biolabs). ..



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    Bacterial strains and plasmids used in this study.

    Journal: Frontiers in Immunology

    Article Title: Specificities and redundancies in the NEL family of bacterial E3 ubiquitin ligases of Salmonella enterica serovar Typhimurium

    doi: 10.3389/fimmu.2024.1328707

    Figure Lengend Snippet: Bacterial strains and plasmids used in this study.

    Article Snippet: pTYB21 , Vector for generation of intein fusions , New England Biolabs.

    Techniques: Expressing, Plasmid Preparation

    H-NS physically binds to the promoter region of rfbT . (A) H-NS protein purification. Lane 1 is protein marker, and lanes 2–3 are purified H-NS proteins. The right arrow indicates purified bands. (B) EMSA of H-NS bound to rfbT promoter regions. EMSA was described in the “Materials and Methods.” Biotin-labeled 256-bp DNA probe (20 ng) was incubated with increasing amounts of purified H-NS protein. For competitive analysis, the identical but unlabelled probe was added at 10 or 50-fold concentration relative to the labeled one (5–6 channels). Lanes 7 and 8 are Probe-N7 with H-NS. The left arrow indicated the free probe, whereas the right arrow referred to H-NS- rfbT bound one. (C) DNase I footprinting assay of H-NS binding to the promoter region of rfbT . As described in the “Materials and Methods,” purified H-NS protein were incubated with FAM-labelled fragments of the rfbT promoter region, and then the fragments were digested with optimized DNase I. Finally, the digested fragments were analyzed, and the protected regions were boxed and marked. The colored traces representing the different concentrations of H-NS used (red, 0 μg and blue, 5 μg) are indicated separately and then merged, together with the DNA sequencing results (G, T, A, and C) displayed by four different colors. The region where the blue traces drop is the binding region of H-NS to the probe.

    Journal: Frontiers in Microbiology

    Article Title: Serotype conversion gene rfbT is directly regulated by histone-like nucleoid structuring protein (H-NS) in V. cholerae O1

    doi: 10.3389/fmicb.2023.1111895

    Figure Lengend Snippet: H-NS physically binds to the promoter region of rfbT . (A) H-NS protein purification. Lane 1 is protein marker, and lanes 2–3 are purified H-NS proteins. The right arrow indicates purified bands. (B) EMSA of H-NS bound to rfbT promoter regions. EMSA was described in the “Materials and Methods.” Biotin-labeled 256-bp DNA probe (20 ng) was incubated with increasing amounts of purified H-NS protein. For competitive analysis, the identical but unlabelled probe was added at 10 or 50-fold concentration relative to the labeled one (5–6 channels). Lanes 7 and 8 are Probe-N7 with H-NS. The left arrow indicated the free probe, whereas the right arrow referred to H-NS- rfbT bound one. (C) DNase I footprinting assay of H-NS binding to the promoter region of rfbT . As described in the “Materials and Methods,” purified H-NS protein were incubated with FAM-labelled fragments of the rfbT promoter region, and then the fragments were digested with optimized DNase I. Finally, the digested fragments were analyzed, and the protected regions were boxed and marked. The colored traces representing the different concentrations of H-NS used (red, 0 μg and blue, 5 μg) are indicated separately and then merged, together with the DNA sequencing results (G, T, A, and C) displayed by four different colors. The region where the blue traces drop is the binding region of H-NS to the probe.

    Article Snippet: The cell debris was removed by centrifugation, and H-NS-intein fusion protein with chitin binding domain (CBD) was purified using IMPACT™ Kit (New England Biolabs, United Kingdom) according to the manufacturer’s instructions.

    Techniques: Protein Purification, Marker, Purification, Labeling, Incubation, Concentration Assay, Footprinting, Binding Assay, DNA Sequencing