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copper i catalyzed azide alkyne cycloaddition  (Jena Bioscience)


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    Jena Bioscience copper i catalyzed azide alkyne cycloaddition
    Copper I Catalyzed Azide Alkyne Cycloaddition, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 94/100, based on 61 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/azide+alkyne+cycloaddition/CuSO4+-+click+chemistry+grade/bio_rxiv__2025__01__15__633177-367-11-27
    Average 94 stars, based on 61 article reviews
    copper i catalyzed azide alkyne cycloaddition - by Bioz Stars, 2026-10
    94/100 stars

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    Related Articles

    Synthesized:

    Article Title: The MYCN/Aurora-A complex is a cyclin activating kinase for CDK12
    Article Snippet: .. Newly synthesized DNA was visualized using click chemistry by performing a copper(I)-catalyzed azide-alkyne cycloaddition (100 mM Tris pH 8.5, 4 mM CuSO4, 10 mM AFDye 647 Azide (Jena Bioscience), 10 mM L-Ascorbic Acid). ..

    Conjugation Assay:

    Article Title: METTL1 promotes tumorigenesis through tRNA-derived fragment biogenesis in prostate cancer
    Article Snippet: The cells were washed in PBS and permeabilised with PBS supplemented with 3% fetal bovine serum (Sigma-Aldrich) and 0.1% saponin (Santa Cruz Biotechnology) for 5 min at room temperature. .. OP-puro conjugation to a fluorochrome was performed by azide-alkyne cycloaddition using the Click-iT Cell Reaction Buffer Kit (Jena Bioscience) and 5 μM of Alexa Cy5.5 conjugated to azide (Jena Bioscience). ..

    Article Title: METTL1 promotes tumorigenesis through tRNA-derived fragment biogenesis in prostate cancer.
    Article Snippet: The cells were washed in PBS and permeabilised with PBS supplemented with 3% fetal bovine serum (SigmaAldrich) and 0.1% saponin (Santa Cruz Biotechnology) for 5 min at room temperature. .. OP-puro conjugation to a fluorochrome was performed by azide-alkyne cycloaddition using the Click-iT Cell Reaction Buffer Kit (Jena Bioscience) and 5 μM of Alexa Cy5.5 conjugated to azide (Jena Bioscience). ..

    Immunocytochemistry:

    Article Title: High resolution imaging of nascent mitochondrial protein synthesis in cultured human cells
    Article Snippet: .. Cells were fully permeabilised with 0.5% (v/v) Triton X-100 in PBS (137 mM NaCl, 2.68 mM KCl and 10 mM Na 2 HPO 4 , pH 7.4) and subsequently blocked with 5% (w/v) BSA for 10 min. Pulse-labelled mitochondrial proteins were detected with a copper-catalysed azide–alkyne cycloaddition (600 uM copper sulphate, 1.2 mM BTTAA, 40 μM picolyl Alexa Fluor 555 (CLK-091-1) or 594 (CLK-1296-1) azide and 2 mM sodium ascorbate in PBS, all Jena Bioscience) click chemistry reaction for 40 min. Immunocytochemistry was used to co-label specific mitochondrial targets of interest. .. This involved incubation with a primary antibody diluted in 5% BSA for 1 hour at room temperature, followed by species-specific Alexa Fluor 532 (Thermo Fisher A-11009) or ATTO647N (Sigma M8645) secondary antibodies diluted 1:200 in 5% BSA for 40 min.

    Article Title: High-resolution imaging reveals compartmentalization of mitochondrial protein synthesis in cultured human cells
    Article Snippet: .. Cells were fully permeabilized with 0.5% (vol/vol) Triton X-100 in PBS (137 mM NaCl, 2.68 mM KCl, and 10 mM Na 2 HPO 4 , pH 7.4) and subsequently blocked with 5% (wt/vol) BSA for 10 min. Pulse-labeled mitochondrial proteins were detected with a copper-catalyzed azide–alkyne cycloaddition [600 μM copper sulfate, 1.2 mM BTTAA, 40 μM picolyl Alexa Fluor 555 (CLK-091-1) or 594 (CLK-1296-1) azide, and 2 mM sodium ascorbate in PBS; all Jena Bioscience] click-chemistry reaction for 40 min. Immunocytochemistry was used to colabel specific mitochondrial targets of interest. .. This involved incubation with a primary antibody diluted in 5% BSA for 1 h at room temperature, followed by species-specific Alexa Fluor 532 (Thermo Fisher A-11009) or ATTO647N (Sigma M8645) secondary antibodies diluted 1:200 in 5% BSA for 40 min.



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    a Chemical structure of eFSY. eFSY: enrichable fluorosulfate-L-tyrosine. ( b ) SDS-PAGE gel of His-tag purified MBP-Z(E24eFSY). c Western blot analysis showing MBP-Z(E24eFSY) labeled by biotin via click chemistry. <t>CuAAC:</t> Copper-catalyzed azide-alkyne cycloaddition. d Intact protein mass analysis of MBP-Z(E24eFSY). e Tandem mass spectrum of eFSY incorporated peptide of MBP-Z(E24eFSY) (‘U’ represents eFSY residue in this study, but not selenocysteine). f Tandem mass spectrum of a biotin-labeled peptide derived from MBP-Z(E24eFSY). g Proximal sites, Glu24 and Lys7, on the protein structure of affibody/Z complex (PDB ID 1LP1). Glu24 was used for eFSY incorporation, and Lys7 was used for target amino acid incorporation. ( h ) Western blot analysis showing cross-linking between MBP-Z(E24eFSY) and affibody(K7X). i Biotin labeling of cross-linked MBP-Z/affibody products. j MS/MS fragmentation patterns of cross-linked peptides and biotin-labeled peptides of MBP-Z/affibody cross-linking. k Extracted ion chromatograms (XICs) of cross-linked peptides from input sample (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). l XICs of cross-linked peptides from enriched sample, cross-linked peptides were effectively enriched by Monomeric Avidin beads (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). RT: retention time, MA: peak area. Source data are provided as a Source Data file.
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    a Chemical structure of eFSY. eFSY: enrichable fluorosulfate-L-tyrosine. ( b ) SDS-PAGE gel of His-tag purified MBP-Z(E24eFSY). c Western blot analysis showing MBP-Z(E24eFSY) labeled by biotin via click chemistry. <t>CuAAC:</t> Copper-catalyzed azide-alkyne cycloaddition. d Intact protein mass analysis of MBP-Z(E24eFSY). e Tandem mass spectrum of eFSY incorporated peptide of MBP-Z(E24eFSY) (‘U’ represents eFSY residue in this study, but not selenocysteine). f Tandem mass spectrum of a biotin-labeled peptide derived from MBP-Z(E24eFSY). g Proximal sites, Glu24 and Lys7, on the protein structure of affibody/Z complex (PDB ID 1LP1). Glu24 was used for eFSY incorporation, and Lys7 was used for target amino acid incorporation. ( h ) Western blot analysis showing cross-linking between MBP-Z(E24eFSY) and affibody(K7X). i Biotin labeling of cross-linked MBP-Z/affibody products. j MS/MS fragmentation patterns of cross-linked peptides and biotin-labeled peptides of MBP-Z/affibody cross-linking. k Extracted ion chromatograms (XICs) of cross-linked peptides from input sample (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). l XICs of cross-linked peptides from enriched sample, cross-linked peptides were effectively enriched by Monomeric Avidin beads (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). RT: retention time, MA: peak area. Source data are provided as a Source Data file.
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    Image Search Results


    a Chemical structure of eFSY. eFSY: enrichable fluorosulfate-L-tyrosine. ( b ) SDS-PAGE gel of His-tag purified MBP-Z(E24eFSY). c Western blot analysis showing MBP-Z(E24eFSY) labeled by biotin via click chemistry. CuAAC: Copper-catalyzed azide-alkyne cycloaddition. d Intact protein mass analysis of MBP-Z(E24eFSY). e Tandem mass spectrum of eFSY incorporated peptide of MBP-Z(E24eFSY) (‘U’ represents eFSY residue in this study, but not selenocysteine). f Tandem mass spectrum of a biotin-labeled peptide derived from MBP-Z(E24eFSY). g Proximal sites, Glu24 and Lys7, on the protein structure of affibody/Z complex (PDB ID 1LP1). Glu24 was used for eFSY incorporation, and Lys7 was used for target amino acid incorporation. ( h ) Western blot analysis showing cross-linking between MBP-Z(E24eFSY) and affibody(K7X). i Biotin labeling of cross-linked MBP-Z/affibody products. j MS/MS fragmentation patterns of cross-linked peptides and biotin-labeled peptides of MBP-Z/affibody cross-linking. k Extracted ion chromatograms (XICs) of cross-linked peptides from input sample (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). l XICs of cross-linked peptides from enriched sample, cross-linked peptides were effectively enriched by Monomeric Avidin beads (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). RT: retention time, MA: peak area. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Characterize direct protein interactions with enrichable, cleavable and latent bioreactive unnatural amino acids

    doi: 10.1038/s41467-024-49517-1

    Figure Lengend Snippet: a Chemical structure of eFSY. eFSY: enrichable fluorosulfate-L-tyrosine. ( b ) SDS-PAGE gel of His-tag purified MBP-Z(E24eFSY). c Western blot analysis showing MBP-Z(E24eFSY) labeled by biotin via click chemistry. CuAAC: Copper-catalyzed azide-alkyne cycloaddition. d Intact protein mass analysis of MBP-Z(E24eFSY). e Tandem mass spectrum of eFSY incorporated peptide of MBP-Z(E24eFSY) (‘U’ represents eFSY residue in this study, but not selenocysteine). f Tandem mass spectrum of a biotin-labeled peptide derived from MBP-Z(E24eFSY). g Proximal sites, Glu24 and Lys7, on the protein structure of affibody/Z complex (PDB ID 1LP1). Glu24 was used for eFSY incorporation, and Lys7 was used for target amino acid incorporation. ( h ) Western blot analysis showing cross-linking between MBP-Z(E24eFSY) and affibody(K7X). i Biotin labeling of cross-linked MBP-Z/affibody products. j MS/MS fragmentation patterns of cross-linked peptides and biotin-labeled peptides of MBP-Z/affibody cross-linking. k Extracted ion chromatograms (XICs) of cross-linked peptides from input sample (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). l XICs of cross-linked peptides from enriched sample, cross-linked peptides were effectively enriched by Monomeric Avidin beads (top panel: charge 3+ peptide precursor; bottom panel: charge 4+ peptide precursor). RT: retention time, MA: peak area. Source data are provided as a Source Data file.

    Article Snippet: CuAAC: Copper-catalyzed azide-alkyne cycloaddition. d Intact protein mass analysis of MBP-Z(E24eFSY). e Tandem mass spectrum of eFSY incorporated peptide of MBP-Z(E24eFSY) (‘U’ represents eFSY residue in this study, but not selenocysteine). f Tandem mass spectrum of a biotin-labeled peptide derived from MBP-Z(E24eFSY). g Proximal sites, Glu24 and Lys7, on the protein structure of affibody/Z complex (PDB ID 1LP1).

    Techniques: SDS Page, Purification, Western Blot, Labeling, Residue, Derivative Assay, Tandem Mass Spectroscopy, Avidin-Biotin Assay