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bea concentration  (MedChemExpress)


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    Structured Review

    MedChemExpress bea concentration
    Inhibition of CTSB activity by <t>BEA</t> in <t>mouse</t> <t>BMDCs.</t> (a) 1 × 10 6 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (b, c) 5 × 10 5 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA or the known CTSB inhibitor CA‐074 for 16 h. CTSB activity was detected in BMDCs by flow cytometry. (d) 1 × 10 6 iDCs were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (e, f) 5 × 10 5 iDCs were stimulated with the indicated concentrations of BEA or CA‐074 for 16 h. CTSB activity was detected in iDCs by flow cytometry. Data is shown as means ± SEM. Results shown are representative of two to three independent experiments. * p < 0.05, ** p < 0.01, **** p < 0.0001, ns, not significant.
    Bea Concentration, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bea concentration/product/MedChemExpress
    Average 93 stars, based on 3 article reviews
    bea concentration - by Bioz Stars, 2026-02
    93/100 stars

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    1) Product Images from "The mycotoxin Beauvericin is an uncompetitive inhibitor of Cathepsin B"

    Article Title: The mycotoxin Beauvericin is an uncompetitive inhibitor of Cathepsin B

    Journal: Protein Science : A Publication of the Protein Society

    doi: 10.1002/pro.70173

    Inhibition of CTSB activity by BEA in mouse BMDCs. (a) 1 × 10 6 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (b, c) 5 × 10 5 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA or the known CTSB inhibitor CA‐074 for 16 h. CTSB activity was detected in BMDCs by flow cytometry. (d) 1 × 10 6 iDCs were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (e, f) 5 × 10 5 iDCs were stimulated with the indicated concentrations of BEA or CA‐074 for 16 h. CTSB activity was detected in iDCs by flow cytometry. Data is shown as means ± SEM. Results shown are representative of two to three independent experiments. * p < 0.05, ** p < 0.01, **** p < 0.0001, ns, not significant.
    Figure Legend Snippet: Inhibition of CTSB activity by BEA in mouse BMDCs. (a) 1 × 10 6 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (b, c) 5 × 10 5 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA or the known CTSB inhibitor CA‐074 for 16 h. CTSB activity was detected in BMDCs by flow cytometry. (d) 1 × 10 6 iDCs were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (e, f) 5 × 10 5 iDCs were stimulated with the indicated concentrations of BEA or CA‐074 for 16 h. CTSB activity was detected in iDCs by flow cytometry. Data is shown as means ± SEM. Results shown are representative of two to three independent experiments. * p < 0.05, ** p < 0.01, **** p < 0.0001, ns, not significant.

    Techniques Used: Inhibition, Activity Assay, Flow Cytometry

    Identification of a putative BEA binding site using molecular docking. (a) Different proteins inhibited by BEA (Cathepsin B: blue, Cathepsin V: white, Papain: yellow) display Phe‐Val‐rich regions in their proenzyme autoinhibitory peptides (Cathepsin B: beige, Cathepsin V: purple, Papain: cyan). The residues are shown as red sticks, and the region is highlighted with a gray circle. (b) Docking score distribution for the generated binding poses of BEA. (c) Binding mode consistent with the placement of the autoinhibitory peptide. BEA is shown as yellow sticks, nearby residues are shown as blue sticks, and the catalytic cysteine is shown in cyan. The center of mass of the side chains of the autoinhibitory peptide is shown as red spheres. (d) Superimposition of the binding mode shown in (c) (protein shown as blue cartoon, BEA shown as yellow van der Waals spheres), against the structure of rat CTSB bound to the tripeptide‐mimetic covalent inhibitor benzyloxycarbonyl‐Arg‐Ser(O‐Bzl) chloromethylketone (PDB ID 1THE ) (protein shown as green cartoon, inhibitor shown as purple van der Waals spheres).
    Figure Legend Snippet: Identification of a putative BEA binding site using molecular docking. (a) Different proteins inhibited by BEA (Cathepsin B: blue, Cathepsin V: white, Papain: yellow) display Phe‐Val‐rich regions in their proenzyme autoinhibitory peptides (Cathepsin B: beige, Cathepsin V: purple, Papain: cyan). The residues are shown as red sticks, and the region is highlighted with a gray circle. (b) Docking score distribution for the generated binding poses of BEA. (c) Binding mode consistent with the placement of the autoinhibitory peptide. BEA is shown as yellow sticks, nearby residues are shown as blue sticks, and the catalytic cysteine is shown in cyan. The center of mass of the side chains of the autoinhibitory peptide is shown as red spheres. (d) Superimposition of the binding mode shown in (c) (protein shown as blue cartoon, BEA shown as yellow van der Waals spheres), against the structure of rat CTSB bound to the tripeptide‐mimetic covalent inhibitor benzyloxycarbonyl‐Arg‐Ser(O‐Bzl) chloromethylketone (PDB ID 1THE ) (protein shown as green cartoon, inhibitor shown as purple van der Waals spheres).

    Techniques Used: Binding Assay, Generated



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    bea concentration  (MedChemExpress)
    93
    MedChemExpress bea concentration
    Inhibition of CTSB activity by <t>BEA</t> in <t>mouse</t> <t>BMDCs.</t> (a) 1 × 10 6 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (b, c) 5 × 10 5 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA or the known CTSB inhibitor CA‐074 for 16 h. CTSB activity was detected in BMDCs by flow cytometry. (d) 1 × 10 6 iDCs were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (e, f) 5 × 10 5 iDCs were stimulated with the indicated concentrations of BEA or CA‐074 for 16 h. CTSB activity was detected in iDCs by flow cytometry. Data is shown as means ± SEM. Results shown are representative of two to three independent experiments. * p < 0.05, ** p < 0.01, **** p < 0.0001, ns, not significant.
    Bea Concentration, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/bea concentration/product/MedChemExpress
    Average 93 stars, based on 1 article reviews
    bea concentration - by Bioz Stars, 2026-02
    93/100 stars
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    Image Search Results


    Inhibition of CTSB activity by BEA in mouse BMDCs. (a) 1 × 10 6 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (b, c) 5 × 10 5 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA or the known CTSB inhibitor CA‐074 for 16 h. CTSB activity was detected in BMDCs by flow cytometry. (d) 1 × 10 6 iDCs were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (e, f) 5 × 10 5 iDCs were stimulated with the indicated concentrations of BEA or CA‐074 for 16 h. CTSB activity was detected in iDCs by flow cytometry. Data is shown as means ± SEM. Results shown are representative of two to three independent experiments. * p < 0.05, ** p < 0.01, **** p < 0.0001, ns, not significant.

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: The mycotoxin Beauvericin is an uncompetitive inhibitor of Cathepsin B

    doi: 10.1002/pro.70173

    Figure Lengend Snippet: Inhibition of CTSB activity by BEA in mouse BMDCs. (a) 1 × 10 6 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (b, c) 5 × 10 5 BMDCs from C57BL/6N mice were stimulated with the indicated concentrations of BEA or the known CTSB inhibitor CA‐074 for 16 h. CTSB activity was detected in BMDCs by flow cytometry. (d) 1 × 10 6 iDCs were stimulated with the indicated concentrations of BEA for 16 h. CTSB activity was measured in cell lysates. (e, f) 5 × 10 5 iDCs were stimulated with the indicated concentrations of BEA or CA‐074 for 16 h. CTSB activity was detected in iDCs by flow cytometry. Data is shown as means ± SEM. Results shown are representative of two to three independent experiments. * p < 0.05, ** p < 0.01, **** p < 0.0001, ns, not significant.

    Article Snippet: On Day 9, BMDCs were seeded on a 24‐well plate and subjected to a specified BEA concentration or to 30 μM of the control inhibitor, CA074 (MedChemExpress, Cat# HY‐103350), for 24 h. The stimulated cells were collected for FACS or CTSB activity assays.

    Techniques: Inhibition, Activity Assay, Flow Cytometry

    Identification of a putative BEA binding site using molecular docking. (a) Different proteins inhibited by BEA (Cathepsin B: blue, Cathepsin V: white, Papain: yellow) display Phe‐Val‐rich regions in their proenzyme autoinhibitory peptides (Cathepsin B: beige, Cathepsin V: purple, Papain: cyan). The residues are shown as red sticks, and the region is highlighted with a gray circle. (b) Docking score distribution for the generated binding poses of BEA. (c) Binding mode consistent with the placement of the autoinhibitory peptide. BEA is shown as yellow sticks, nearby residues are shown as blue sticks, and the catalytic cysteine is shown in cyan. The center of mass of the side chains of the autoinhibitory peptide is shown as red spheres. (d) Superimposition of the binding mode shown in (c) (protein shown as blue cartoon, BEA shown as yellow van der Waals spheres), against the structure of rat CTSB bound to the tripeptide‐mimetic covalent inhibitor benzyloxycarbonyl‐Arg‐Ser(O‐Bzl) chloromethylketone (PDB ID 1THE ) (protein shown as green cartoon, inhibitor shown as purple van der Waals spheres).

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: The mycotoxin Beauvericin is an uncompetitive inhibitor of Cathepsin B

    doi: 10.1002/pro.70173

    Figure Lengend Snippet: Identification of a putative BEA binding site using molecular docking. (a) Different proteins inhibited by BEA (Cathepsin B: blue, Cathepsin V: white, Papain: yellow) display Phe‐Val‐rich regions in their proenzyme autoinhibitory peptides (Cathepsin B: beige, Cathepsin V: purple, Papain: cyan). The residues are shown as red sticks, and the region is highlighted with a gray circle. (b) Docking score distribution for the generated binding poses of BEA. (c) Binding mode consistent with the placement of the autoinhibitory peptide. BEA is shown as yellow sticks, nearby residues are shown as blue sticks, and the catalytic cysteine is shown in cyan. The center of mass of the side chains of the autoinhibitory peptide is shown as red spheres. (d) Superimposition of the binding mode shown in (c) (protein shown as blue cartoon, BEA shown as yellow van der Waals spheres), against the structure of rat CTSB bound to the tripeptide‐mimetic covalent inhibitor benzyloxycarbonyl‐Arg‐Ser(O‐Bzl) chloromethylketone (PDB ID 1THE ) (protein shown as green cartoon, inhibitor shown as purple van der Waals spheres).

    Article Snippet: On Day 9, BMDCs were seeded on a 24‐well plate and subjected to a specified BEA concentration or to 30 μM of the control inhibitor, CA074 (MedChemExpress, Cat# HY‐103350), for 24 h. The stimulated cells were collected for FACS or CTSB activity assays.

    Techniques: Binding Assay, Generated