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x gal  (Gold Biotechnology Inc)


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  • 96

    Structured Review

    Gold Biotechnology Inc x gal
    Tagging a nanobody to the N-terminus <t>of</t> <t>β-gal</t> does not affect its activity. (A) Colonies of dH5α bacteria transformed with a plasmid containing the coding sequence for β-gal with Nb16 fused to its N-terminus via a 4AA (GSHV) linker and plated on an LB/Kan plate with IPTG and <t>X-gal.</t> The plate was photographed 24 h after incubation at 37 °C for 16 h. (B), (C), and (D) are the same as (A), except that the bacteria were induced to express β-gal with Nb16 fused to its N-terminus via a longer flexible peptide (GSGASGSHV), a Strep-tag-containing peptide (GSWSHPQFEKHV), or β-gal with purification tags, respectively.
    X Gal, supplied by Gold Biotechnology Inc, used in various techniques. Bioz Stars score: 96/100, based on 304 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/x+gal/X-Gal/pmc12860646-45-27-31
    Average 96 stars, based on 304 article reviews
    x gal - by Bioz Stars, 2026-09
    96/100 stars

    Images

    1) Product Images from "Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen"

    Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen

    Journal: Food Chemistry: Molecular Sciences

    doi: 10.1016/j.fochms.2026.100357

    Tagging a nanobody to the N-terminus of β-gal does not affect its activity. (A) Colonies of dH5α bacteria transformed with a plasmid containing the coding sequence for β-gal with Nb16 fused to its N-terminus via a 4AA (GSHV) linker and plated on an LB/Kan plate with IPTG and X-gal. The plate was photographed 24 h after incubation at 37 °C for 16 h. (B), (C), and (D) are the same as (A), except that the bacteria were induced to express β-gal with Nb16 fused to its N-terminus via a longer flexible peptide (GSGASGSHV), a Strep-tag-containing peptide (GSWSHPQFEKHV), or β-gal with purification tags, respectively.
    Figure Legend Snippet: Tagging a nanobody to the N-terminus of β-gal does not affect its activity. (A) Colonies of dH5α bacteria transformed with a plasmid containing the coding sequence for β-gal with Nb16 fused to its N-terminus via a 4AA (GSHV) linker and plated on an LB/Kan plate with IPTG and X-gal. The plate was photographed 24 h after incubation at 37 °C for 16 h. (B), (C), and (D) are the same as (A), except that the bacteria were induced to express β-gal with Nb16 fused to its N-terminus via a longer flexible peptide (GSGASGSHV), a Strep-tag-containing peptide (GSWSHPQFEKHV), or β-gal with purification tags, respectively.

    Techniques Used: Activity Assay, Bacteria, Transformation Assay, Plasmid Preparation, Sequencing, Incubation, Strep-tag, Purification

    Related Articles

    Transformation Assay:

    Article Title: Haplotype editing with CRISPR/Cas9 as a therapeutic approach for dominant-negative missense mutations in NEFL.
    Article Snippet: This is a PDF of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability.. This version will undergo additional copyediting, typesetting and review before it is published in its final form.. As such, this version is no longer the Accepted Manuscript, but it is not yet the definitive Version of Record; we are providing this early version to give early visibility of the article.

    Article Title: Haplotype editing with CRISPR/Cas9 as a therapeutic approach for dominant-negative missense mutations in NEFL
    Article Snippet: The resulting amplicon was cloned into competent bacteria using the TOPO-TA Cloning Kit (Thermo Fisher Scientific, 450641). .. The transformation reaction was plated on LB-Agar with ampicillin and supplied with 120 μl X-Gal (20 mg/ml) Xgal (Ape Bio A2539) and 40 μl 100 mM IPTG (Gold Bio I2481C). .. After overnight incubation, white colonies were picked and grown in 5 mL LB Broth supplemented with ampicillin (Fisher BioReagents BP176025).

    Article Title: Synthetic ethylene-responsive binding element and uses thereof
    Article Snippet: The fragments containing the promoter sequences and their GB overhangs were cloned into the pUPD2 entry vector following the GB instructions (Sarrion-Perdigones, et al., 2014; Vazquez-Vilar, et al., 2015) with some modifications: the digestion-ligation cycle started with an initial BsmBI (NEB) digestion step at 55° C. for 20 min, followed by the addition of the DNA T4 ligase (NEB) prior to the full GB cycle (4 min at 37° C. and 5 min at 16° C., 25 times) and a final digestion step at 55° C. for 20 min with freshly added BsmBI and the inactivation of both enzymes at 80° C. for 20 min. .. The reactions were transformed into homemade chemically competent E. coli TOP10 cells (ThermoFisher) and the transformed colonies were selected in LB Agar (Genessee Scientific) supplemented with chloramphenicol (25 μL mg−1) (GoldBio) and X-Gal (20 μL mg−1) (GoldBio). .. Plasmid DNA from white colonies was extracted using alkaline lysis, verified by restriction digest and Sanger sequencing, and stored at −20° C. Confirmed pUPD2 plasmids containing the distal-proximal ethylene-inducible promoters (A1-A2 grammar) were assembled into the destination vector pDGB3alpha1 along with the following GB bricks harbored in pUPD2: a −46 minimal 35S promoter (A3-B1), a triple nuclear localization signal (3×NLS, B2), a triple yellow fluorescent protein (3×YPet) or a β-Glucoronidase CDS (GUS) (B3-B5), and the 35S terminator (B6-C1 grammar) to build two different types of transcriptional reporters (FIG. 4, Panels C-D).

    Plasmid Preparation:

    Article Title: Supporting Information for Measuring prion propagation in single bacteria elucidates mechanism of loss
    Article Snippet: .. After 16 hours, the cells were plated on indicator plates: LB agar containing 10 μM IPTG, X-gal (40 μg/mL), Phenylethyl-β-D-thiogalactopyranoside (TPEG) (Gold Biotechnology) (500 μM), Km and Carb at 37◦C for 24 hours to cure the New1 plasmid (temperature sensitive). ..

    Purification:

    Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen
    Article Snippet: .. Milli-Q water was purified in-house using a Milli-Q Advantage A10 system (Millipore, Bedford, MA, USA) and used throughout. o -Nitrophenyl-β-galactoside (ONPG), Isopropyl β-D-1-thiogalactopyranoside (IPTG), Kanamycin (Kan), and X-Gal were purchased from GoldBio (St Louis, MO, USA). ..

    Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen
    Article Snippet: .. Milli-Q water was purified in-house using a Milli-Q Advantage A10 system (Millipore, Bedford, MA, USA) and used throughout. o-Nitrophenyl-β-galactoside (ONPG), Isopropyl β-D-1-thiogalactopyranoside (IPTG), Kanamycin (Kan), and X-Gal were purchased from GoldBio (St Louis, MO, USA). ..

    Selection:

    Article Title: LIPID DROPLET PROTEIN OF SEEDS is involved in the control of lipid droplet size in Arabidopsis seeds and seedlings.
    Article Snippet: © The Author(s) 2025.. Published by Oxford University Press on behalf of American Society of Plant Biologists.. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

    Activation Assay:

    Article Title: LIPID DROPLET PROTEIN OF SEEDS is involved in the control of lipid droplet size in Arabidopsis seeds and seedlings.
    Article Snippet: © The Author(s) 2025.. Published by Oxford University Press on behalf of American Society of Plant Biologists.. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

    Article Title: LIPID DROPLET PROTEIN OF SEEDS is involved in the control of lipid droplet size in Arabidopsis seeds and seedlings
    Article Snippet: .. In addition, high-selection plates included 100 μ g/mL X-Gal (5-bromo-4-chloro-3-indolyl β- D- galactopyranoside, Gold Biotechnology), which provided an additional qualitative measure of protein–protein interaction, based on the blue coloration of yeast due to activation of the β-galactosidase reporter gene ( ). ..



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    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch <t>biosensor</t> <t>with</t> <t>5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside</t> (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.
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    Image Search Results


    Tagging a nanobody to the N-terminus of β-gal does not affect its activity. (A) Colonies of dH5α bacteria transformed with a plasmid containing the coding sequence for β-gal with Nb16 fused to its N-terminus via a 4AA (GSHV) linker and plated on an LB/Kan plate with IPTG and X-gal. The plate was photographed 24 h after incubation at 37 °C for 16 h. (B), (C), and (D) are the same as (A), except that the bacteria were induced to express β-gal with Nb16 fused to its N-terminus via a longer flexible peptide (GSGASGSHV), a Strep-tag-containing peptide (GSWSHPQFEKHV), or β-gal with purification tags, respectively.

    Journal: Food Chemistry: Molecular Sciences

    Article Title: Usage of nanobody-beta-galactosidase fusion in immunoassays and its application in detecting a peanut allergen

    doi: 10.1016/j.fochms.2026.100357

    Figure Lengend Snippet: Tagging a nanobody to the N-terminus of β-gal does not affect its activity. (A) Colonies of dH5α bacteria transformed with a plasmid containing the coding sequence for β-gal with Nb16 fused to its N-terminus via a 4AA (GSHV) linker and plated on an LB/Kan plate with IPTG and X-gal. The plate was photographed 24 h after incubation at 37 °C for 16 h. (B), (C), and (D) are the same as (A), except that the bacteria were induced to express β-gal with Nb16 fused to its N-terminus via a longer flexible peptide (GSGASGSHV), a Strep-tag-containing peptide (GSWSHPQFEKHV), or β-gal with purification tags, respectively.

    Article Snippet: Milli-Q water was purified in-house using a Milli-Q Advantage A10 system (Millipore, Bedford, MA, USA) and used throughout. o -Nitrophenyl-β-galactoside (ONPG), Isopropyl β-D-1-thiogalactopyranoside (IPTG), Kanamycin (Kan), and X-Gal were purchased from GoldBio (St Louis, MO, USA).

    Techniques: Activity Assay, Bacteria, Transformation Assay, Plasmid Preparation, Sequencing, Incubation, Strep-tag, Purification

    (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch biosensor with 5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.

    Journal: bioRxiv

    Article Title: Selective Hydrolytic Defluorination of Branched Perfluorooctanoic Acid Isomers by a Haloacid Dehalogenase

    doi: 10.64898/2026.04.19.719434

    Figure Lengend Snippet: (a) Docking model showing PFOA bound within the active-site pocket of 4A. (b) Enlarged view of the PFOA-binding site, illustrating predicted hydrogen-bonding interactions between the PFOA carboxylate group and surrounding active-site residues. (c) Two-dimensional interaction map of the PFOA–4A complex, highlighting hydrogen-bonding interactions involving the carboxylate group (green dashed lines) and hydrophobic or polar contacts between PFOA and active-site residues. (d) Biosensor-based plate assay detecting fluoride release following high-concentration, scaled-up reactions. PFOA (0.5 mM) was incubated with purified 4A (500 µM) at 20℃ for 120 h prior to analysis. Following incubation, aliquots from the reaction mixture were analyzed using a fluoride-responsive riboswitch biosensor with 5-bromo-4-chloro-3-indolyl-β-D-galactopyranoside (X-gal) as the chromogenic substrate. Enzyme-only, substrate-only, buffer-only controls, and fluoride standards (10 and 500 μM KF) are shown.

    Article Snippet: 5-Bromo-4-chloro-3-indolyl-β-D-galactopyranoside (X-gal) solution (20 mg/mL; Thermo Fisher Scientific, RO941) and 10 mM Tris buffer (pH 8.0, prepared from a 1 M stock; Thermo Fisher Scientific, AM9855G) were used for enzyme assays.

    Techniques: Binding Assay, Concentration Assay, Incubation, Purification