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195a  (Bethyl)


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    Structured Review

    Bethyl 195a
    195a, supplied by Bethyl, used in various techniques. Bioz Stars score: 90/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/195a/product/Bethyl
    Average 90 stars, based on 33 article reviews
    195a - by Bioz Stars, 2026-02
    90/100 stars

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    (A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and <t>MCM5</t> (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.
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    (A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and <t>MCM5</t> (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.
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    (A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and <t>MCM5</t> (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.
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    (A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and <t>MCM5</t> (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.
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    Image Search Results


    (A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and MCM5 (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.

    Journal: bioRxiv

    Article Title: Cryo-EM structure of DNA-unbound human MCM2–7 complex reveals new disease-relevant regulation

    doi: 10.1101/2025.05.31.656953

    Figure Lengend Snippet: (A) Schematic illustration of the domain organization of human MCM2–7 subunits. ZF, zinc finger; R-finger, arginine finger; WHD, winged helix domain. (B) Side views of the segmented cryo-EM density maps of the extended and compacted conformers of DNA-unbound human MCM2–7 double hexamer (DH), superimposed with the atomic models. (C) Side views of the two MCM2–7 DH conformers showing the open DNA-entry gate between MCM2 (yellow) and MCM5 (blue). (D) Side views of two MCM2–7 DH conformers with two subunits removed to display the DNA-binding central channel and the WHDs of MCM4 and MCM5, which occupy the central channel. (E) Top views of the two MCM2–7 DH conformers showing the DNA-entry gate.

    Article Snippet: The following antibodies against human proteins were used for immunoblotting and immunofluorescence: MCM2 (Bethyl Laboratories; A300-191A), MCM3 (Bethyl Laboratories; A300-192A), MCM3 (Santa Cruz; sc-390480), MCM5 (Bethyl Laboratories; A300-195A-2), CHK1 phospho-S345 (CST; 2341), CHK1 (Santa Cruz; sc-8408), RPA32 (Santa Cruz; sc-56770), CDC6 (Santa Cruz; sc-9964), FLAG (Sigma; F1804-200UG), HA (Sino Biology; 100028-MM10), HA (CST; 3724S), GAPDH (Proteintech; 10494-1-AP and 60004-1-Ig), Histone H3 (Abclonal; A2348).

    Techniques: Cryo-EM Sample Prep, Binding Assay

    (A) Cryo-EM density map of an MCM2–7 single hexamer (SH) superimposed with the atomic model, with a close-up view of the MCM3 WHD-MCM2 interface. (B and C) Close-up views of key interacting residues at the MCM3 WHD–MCM2 interface. (D) The closed DNA entry gate in DNA-bound MCM2–7 DH (PDB ID: 7W1Y) with only MCM2 and MCM5 shown. A close-up view of the MCM2-MCM5 interface is shown on the right. (E) Cryo-EM density maps of recombinant human MCM2–7 SH that contains either MCM3 wild type (WT; top) or the MCM3 3A mutant (bottom). The density of MCM3 WHD (top) and its corresponding location (bottom) are boxed by red dashed lines. (F) Schematic diagram depicting the closed MCM3 WHD latch, which is expected to block DNA entry. (G) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the recombinant MCM2–7 complex containing MCM3 with its WHD deleted (MCM3 ΔWHD ). The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE and Coomassie staining. The experiment was repeated three times with similar results. (H) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the ORC1-6–CDC6 complex. The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE followed by Coomassie staining (bottom panel) and immunoblotting with anti-ORC1 and anti-CDC6 antibodies (top panels). The experiment was repeated three times with similar results.

    Journal: bioRxiv

    Article Title: Cryo-EM structure of DNA-unbound human MCM2–7 complex reveals new disease-relevant regulation

    doi: 10.1101/2025.05.31.656953

    Figure Lengend Snippet: (A) Cryo-EM density map of an MCM2–7 single hexamer (SH) superimposed with the atomic model, with a close-up view of the MCM3 WHD-MCM2 interface. (B and C) Close-up views of key interacting residues at the MCM3 WHD–MCM2 interface. (D) The closed DNA entry gate in DNA-bound MCM2–7 DH (PDB ID: 7W1Y) with only MCM2 and MCM5 shown. A close-up view of the MCM2-MCM5 interface is shown on the right. (E) Cryo-EM density maps of recombinant human MCM2–7 SH that contains either MCM3 wild type (WT; top) or the MCM3 3A mutant (bottom). The density of MCM3 WHD (top) and its corresponding location (bottom) are boxed by red dashed lines. (F) Schematic diagram depicting the closed MCM3 WHD latch, which is expected to block DNA entry. (G) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the recombinant MCM2–7 complex containing MCM3 with its WHD deleted (MCM3 ΔWHD ). The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE and Coomassie staining. The experiment was repeated three times with similar results. (H) Binding between GST-MCM3 WHD proteins (WT, 3A, and Q761L) and the ORC1-6–CDC6 complex. The input proteins and proteins bound to GST beads were analyzed by SDS-PAGE followed by Coomassie staining (bottom panel) and immunoblotting with anti-ORC1 and anti-CDC6 antibodies (top panels). The experiment was repeated three times with similar results.

    Article Snippet: The following antibodies against human proteins were used for immunoblotting and immunofluorescence: MCM2 (Bethyl Laboratories; A300-191A), MCM3 (Bethyl Laboratories; A300-192A), MCM3 (Santa Cruz; sc-390480), MCM5 (Bethyl Laboratories; A300-195A-2), CHK1 phospho-S345 (CST; 2341), CHK1 (Santa Cruz; sc-8408), RPA32 (Santa Cruz; sc-56770), CDC6 (Santa Cruz; sc-9964), FLAG (Sigma; F1804-200UG), HA (Sino Biology; 100028-MM10), HA (CST; 3724S), GAPDH (Proteintech; 10494-1-AP and 60004-1-Ig), Histone H3 (Abclonal; A2348).

    Techniques: Cryo-EM Sample Prep, Recombinant, Mutagenesis, Blocking Assay, Binding Assay, SDS Page, Staining, Western Blot

    (A) Immunoblots of whole-cell extracts (left panels) or chromatin fractions (right panels) of the indicated 293FT cells treated with DMSO or dTAG-13 (1 µM) for 16 h. GAPDH and histone H3 are used as loading controls. Relative intensities of HA-MCM3 and the endogenous MCM2 are quantified and shown below respective panels. (B) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) without pre-extraction before fixation. The HA signals in this staining protocol represent total cellular HA-MCM3. (C) Quantification of HA-MCM3 intensities of cells in (B). Each dot in the graph represents a single cell. (D) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) with pre-extraction before fixation. The HA signals in this staining protocol represent chromatin-bound HA-MCM3. (E) Quantification of HA-MCM3 intensities of cells in (D). (F) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) without pre-extraction before fixation. (G) Quantification of MCM5 intensities of cells in (F). (H) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) with pre-extraction before fixation. (I) Quantification of MCM5 intensities of cells in (H). For all relevant panels, the scale bar indicates 10 µm. Mean ± SD are shown.

    Journal: bioRxiv

    Article Title: Cryo-EM structure of DNA-unbound human MCM2–7 complex reveals new disease-relevant regulation

    doi: 10.1101/2025.05.31.656953

    Figure Lengend Snippet: (A) Immunoblots of whole-cell extracts (left panels) or chromatin fractions (right panels) of the indicated 293FT cells treated with DMSO or dTAG-13 (1 µM) for 16 h. GAPDH and histone H3 are used as loading controls. Relative intensities of HA-MCM3 and the endogenous MCM2 are quantified and shown below respective panels. (B) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) without pre-extraction before fixation. The HA signals in this staining protocol represent total cellular HA-MCM3. (C) Quantification of HA-MCM3 intensities of cells in (B). Each dot in the graph represents a single cell. (D) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-HA (magenta) and DAPI (blue) with pre-extraction before fixation. The HA signals in this staining protocol represent chromatin-bound HA-MCM3. (E) Quantification of HA-MCM3 intensities of cells in (D). (F) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) without pre-extraction before fixation. (G) Quantification of MCM5 intensities of cells in (F). (H) Images of indicated 293FT cells treated with dTAG-13 and stained with anti-MCM5 (green) and DAPI (blue) with pre-extraction before fixation. (I) Quantification of MCM5 intensities of cells in (H). For all relevant panels, the scale bar indicates 10 µm. Mean ± SD are shown.

    Article Snippet: The following antibodies against human proteins were used for immunoblotting and immunofluorescence: MCM2 (Bethyl Laboratories; A300-191A), MCM3 (Bethyl Laboratories; A300-192A), MCM3 (Santa Cruz; sc-390480), MCM5 (Bethyl Laboratories; A300-195A-2), CHK1 phospho-S345 (CST; 2341), CHK1 (Santa Cruz; sc-8408), RPA32 (Santa Cruz; sc-56770), CDC6 (Santa Cruz; sc-9964), FLAG (Sigma; F1804-200UG), HA (Sino Biology; 100028-MM10), HA (CST; 3724S), GAPDH (Proteintech; 10494-1-AP and 60004-1-Ig), Histone H3 (Abclonal; A2348).

    Techniques: Western Blot, Staining, Extraction