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myh9 inhibition assay  (TargetMol)


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    Structured Review

    TargetMol myh9 inhibition assay
    Identification of <t>Myh9</t> as a direct binding target of Sa and evaluation of complex stability. A: Schematic representation of the chemoproteomic workflow using a biotin-labeled Sa probe in NIH3T3 cells. B: Coomassie blue-stained SDS-PAGE gel showing differential protein bands between treatment groups. The band marked by a dashed box was excised for LC-MS/MS analysis. C: Molecular docking model displaying the binding conformation of Sa with Myh9 and key interacting residues. D: Two-dimensional interaction diagram illustrating hydrogen bonds and hydrophobic interactions between Sa and Myh9. E–G: Molecular dynamics simulation of the Sa–Myh9 complex: (E) RMSD, (F) RMSF of chain D, and (G) Rg plots, reflecting structural stability, residue flexibility, and compactness over 100 ns. H–K: CETSA evaluating Myh9 thermal stability in A253 (H and J) and NIH3T3 (I and K) cells treated with Sa (10 μg/ml). Melting curves derived from CETSA illustrate increased thermal stability of Myh9. Data are presented as mean ± SD. P < 0.05, P < 0.01 versus control group. CETSA, cellular thermal shift assay; RMSD, root mean square deviation; RMSF, root mean square fluctuation; Rg, radius of gyration.
    Myh9 Inhibition Assay, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/myh9+inhibition+assay/Myosin-9-MYH9+Protein%2C+Human%2C+Recombinant/pmc12814850-74-2-12
    Average 94 stars, based on 1 article reviews
    myh9 inhibition assay - by Bioz Stars, 2026-09
    94/100 stars

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    1) Product Images from "Sphinganine as a potentially relevant metabolite in pulmonary involvement of primary Sjögren’s syndrome"

    Article Title: Sphinganine as a potentially relevant metabolite in pulmonary involvement of primary Sjögren’s syndrome

    Journal: Journal of Lipid Research

    doi: 10.1016/j.jlr.2025.100961

    Identification of Myh9 as a direct binding target of Sa and evaluation of complex stability. A: Schematic representation of the chemoproteomic workflow using a biotin-labeled Sa probe in NIH3T3 cells. B: Coomassie blue-stained SDS-PAGE gel showing differential protein bands between treatment groups. The band marked by a dashed box was excised for LC-MS/MS analysis. C: Molecular docking model displaying the binding conformation of Sa with Myh9 and key interacting residues. D: Two-dimensional interaction diagram illustrating hydrogen bonds and hydrophobic interactions between Sa and Myh9. E–G: Molecular dynamics simulation of the Sa–Myh9 complex: (E) RMSD, (F) RMSF of chain D, and (G) Rg plots, reflecting structural stability, residue flexibility, and compactness over 100 ns. H–K: CETSA evaluating Myh9 thermal stability in A253 (H and J) and NIH3T3 (I and K) cells treated with Sa (10 μg/ml). Melting curves derived from CETSA illustrate increased thermal stability of Myh9. Data are presented as mean ± SD. P < 0.05, P < 0.01 versus control group. CETSA, cellular thermal shift assay; RMSD, root mean square deviation; RMSF, root mean square fluctuation; Rg, radius of gyration.
    Figure Legend Snippet: Identification of Myh9 as a direct binding target of Sa and evaluation of complex stability. A: Schematic representation of the chemoproteomic workflow using a biotin-labeled Sa probe in NIH3T3 cells. B: Coomassie blue-stained SDS-PAGE gel showing differential protein bands between treatment groups. The band marked by a dashed box was excised for LC-MS/MS analysis. C: Molecular docking model displaying the binding conformation of Sa with Myh9 and key interacting residues. D: Two-dimensional interaction diagram illustrating hydrogen bonds and hydrophobic interactions between Sa and Myh9. E–G: Molecular dynamics simulation of the Sa–Myh9 complex: (E) RMSD, (F) RMSF of chain D, and (G) Rg plots, reflecting structural stability, residue flexibility, and compactness over 100 ns. H–K: CETSA evaluating Myh9 thermal stability in A253 (H and J) and NIH3T3 (I and K) cells treated with Sa (10 μg/ml). Melting curves derived from CETSA illustrate increased thermal stability of Myh9. Data are presented as mean ± SD. P < 0.05, P < 0.01 versus control group. CETSA, cellular thermal shift assay; RMSD, root mean square deviation; RMSF, root mean square fluctuation; Rg, radius of gyration.

    Techniques Used: Binding Assay, Labeling, Staining, SDS Page, Liquid Chromatography with Mass Spectroscopy, Residue, Derivative Assay, Control, Thermal Shift Assay

    Functional role of Myh9 in Sa-induced epithelial injury and fibroblast activation. A: Relative mRNA expression of Myh9 in submandibular gland tissues as measured by qRT-PCR. B: Immunohistochemical staining analysis and (C) quantitative analysis of the expression of Myh9 in lung tissues. D and E: Western blot analysis (D) and corresponding quantification (E) of Myh9 protein expression in A253 cells treated with increasing concentrations of Sa. F and G: Western blot (F) and densitometric analysis (G) of Myh9 expression in NIH3T3 cells treated with Sa or TGF-β1 (positive control). H and I: Western blot (H) and quantification (I) of AQP5 expression in A253 cells treated with Sa, with or without the Myh9 inhibitor blebbistatin. J and K: Western blot (J) and quantification (K) of fibronectin and α-SMA protein levels in NIH3T3 cells treated with Sa, with or without blebbistatin. Data are presented as mean ± SD. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001; ns, not significant. # P < 0.05, ## P < 0.01 Sa group with 4-PBA treatment. α-SMA, alpha-smooth muscle actin; 4-PBA, 4-phenylbutyric acid; AQP5, aquaporin-5
    Figure Legend Snippet: Functional role of Myh9 in Sa-induced epithelial injury and fibroblast activation. A: Relative mRNA expression of Myh9 in submandibular gland tissues as measured by qRT-PCR. B: Immunohistochemical staining analysis and (C) quantitative analysis of the expression of Myh9 in lung tissues. D and E: Western blot analysis (D) and corresponding quantification (E) of Myh9 protein expression in A253 cells treated with increasing concentrations of Sa. F and G: Western blot (F) and densitometric analysis (G) of Myh9 expression in NIH3T3 cells treated with Sa or TGF-β1 (positive control). H and I: Western blot (H) and quantification (I) of AQP5 expression in A253 cells treated with Sa, with or without the Myh9 inhibitor blebbistatin. J and K: Western blot (J) and quantification (K) of fibronectin and α-SMA protein levels in NIH3T3 cells treated with Sa, with or without blebbistatin. Data are presented as mean ± SD. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001; ns, not significant. # P < 0.05, ## P < 0.01 Sa group with 4-PBA treatment. α-SMA, alpha-smooth muscle actin; 4-PBA, 4-phenylbutyric acid; AQP5, aquaporin-5

    Techniques Used: Functional Assay, Activation Assay, Expressing, Quantitative RT-PCR, Immunohistochemical staining, Staining, Western Blot, Positive Control

    Molecular mechanism of Sa induces salivary hyposecretion and pulmonary fibrosis in pSS through the ATF6–Myh9 signaling pathway. Sa, sphinganine; pSS, primary Sjögren’s syndrome.
    Figure Legend Snippet: Molecular mechanism of Sa induces salivary hyposecretion and pulmonary fibrosis in pSS through the ATF6–Myh9 signaling pathway. Sa, sphinganine; pSS, primary Sjögren’s syndrome.

    Techniques Used:

    Related Articles

    Inhibition:

    Article Title: Sphinganine as a potentially relevant metabolite in pulmonary involvement of primary Sjögren’s syndrome
    Article Snippet: In the endoplasmic reticulum (ER) stress inhibition assay, NIH3T3 cells underwent pretreatment with 5 μM 4-phenylbutyric acid (4-PBA, MedChem Express) for 4 h in a serum-free medium. .. For the Myh9 inhibition assay, cells were pretreated with 2 μM Blebbistatin (TargetMol, Shanghai, China) for 4 h in serum-free medium. .. Upon reaching 80% confluency, cells were washed with PBS and incubated for 4 h at 37°C with 5% CO 2 using either 10 μg of Sa-biotin probe (Echelon Biosciences, #S-110B) or control biotin (Sigma-Aldrich, #B4501).

    Article Title: Sphinganine as a potentially relevant metabolite in pulmonary involvement of primary Sjögren's syndrome.
    Article Snippet: In the ER stress inhibition assay, Jo urn al Pr e-p roo f NIH3T3 cells underwent pre-treatment with 5 μM 4-phenylbutyric acid (4-PBA, MedChem Express, USA) for 4 hours in a serum-free medium. .. For the Myh9 inhibition assay, cells were pre-treated with 2 μM Blebbistatin (TargetMol, Shanghai, China) for 4 hours in serum-free medium. .. 2.10 Sphinganine-biotin pulldown assays Upon reaching 80% confluency, cells were washed with PBS and incubated for 4 hours at 37 °C with 5% CO2 using either 10 μg of sphinganine-biotin probe (Echelon Biosciences, #S-110B) or control biotin (Sigma-Aldrich, #B4501).



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    TargetMol myh9 inhibition assay
    Identification of <t>Myh9</t> as a direct binding target of Sa and evaluation of complex stability. A: Schematic representation of the chemoproteomic workflow using a biotin-labeled Sa probe in NIH3T3 cells. B: Coomassie blue-stained SDS-PAGE gel showing differential protein bands between treatment groups. The band marked by a dashed box was excised for LC-MS/MS analysis. C: Molecular docking model displaying the binding conformation of Sa with Myh9 and key interacting residues. D: Two-dimensional interaction diagram illustrating hydrogen bonds and hydrophobic interactions between Sa and Myh9. E–G: Molecular dynamics simulation of the Sa–Myh9 complex: (E) RMSD, (F) RMSF of chain D, and (G) Rg plots, reflecting structural stability, residue flexibility, and compactness over 100 ns. H–K: CETSA evaluating Myh9 thermal stability in A253 (H and J) and NIH3T3 (I and K) cells treated with Sa (10 μg/ml). Melting curves derived from CETSA illustrate increased thermal stability of Myh9. Data are presented as mean ± SD. P < 0.05, P < 0.01 versus control group. CETSA, cellular thermal shift assay; RMSD, root mean square deviation; RMSF, root mean square fluctuation; Rg, radius of gyration.
    Myh9 Inhibition Assay, supplied by TargetMol, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/myh9+inhibition+assay/Myosin-9-MYH9+Protein%2C+Human%2C+Recombinant/pmc12814850-74-2-12
    Average 94 stars, based on 1 article reviews
    myh9 inhibition assay - by Bioz Stars, 2026-09
    94/100 stars
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    Identification of Myh9 as a direct binding target of Sa and evaluation of complex stability. A: Schematic representation of the chemoproteomic workflow using a biotin-labeled Sa probe in NIH3T3 cells. B: Coomassie blue-stained SDS-PAGE gel showing differential protein bands between treatment groups. The band marked by a dashed box was excised for LC-MS/MS analysis. C: Molecular docking model displaying the binding conformation of Sa with Myh9 and key interacting residues. D: Two-dimensional interaction diagram illustrating hydrogen bonds and hydrophobic interactions between Sa and Myh9. E–G: Molecular dynamics simulation of the Sa–Myh9 complex: (E) RMSD, (F) RMSF of chain D, and (G) Rg plots, reflecting structural stability, residue flexibility, and compactness over 100 ns. H–K: CETSA evaluating Myh9 thermal stability in A253 (H and J) and NIH3T3 (I and K) cells treated with Sa (10 μg/ml). Melting curves derived from CETSA illustrate increased thermal stability of Myh9. Data are presented as mean ± SD. P < 0.05, P < 0.01 versus control group. CETSA, cellular thermal shift assay; RMSD, root mean square deviation; RMSF, root mean square fluctuation; Rg, radius of gyration.

    Journal: Journal of Lipid Research

    Article Title: Sphinganine as a potentially relevant metabolite in pulmonary involvement of primary Sjögren’s syndrome

    doi: 10.1016/j.jlr.2025.100961

    Figure Lengend Snippet: Identification of Myh9 as a direct binding target of Sa and evaluation of complex stability. A: Schematic representation of the chemoproteomic workflow using a biotin-labeled Sa probe in NIH3T3 cells. B: Coomassie blue-stained SDS-PAGE gel showing differential protein bands between treatment groups. The band marked by a dashed box was excised for LC-MS/MS analysis. C: Molecular docking model displaying the binding conformation of Sa with Myh9 and key interacting residues. D: Two-dimensional interaction diagram illustrating hydrogen bonds and hydrophobic interactions between Sa and Myh9. E–G: Molecular dynamics simulation of the Sa–Myh9 complex: (E) RMSD, (F) RMSF of chain D, and (G) Rg plots, reflecting structural stability, residue flexibility, and compactness over 100 ns. H–K: CETSA evaluating Myh9 thermal stability in A253 (H and J) and NIH3T3 (I and K) cells treated with Sa (10 μg/ml). Melting curves derived from CETSA illustrate increased thermal stability of Myh9. Data are presented as mean ± SD. P < 0.05, P < 0.01 versus control group. CETSA, cellular thermal shift assay; RMSD, root mean square deviation; RMSF, root mean square fluctuation; Rg, radius of gyration.

    Article Snippet: For the Myh9 inhibition assay, cells were pretreated with 2 μM Blebbistatin (TargetMol, Shanghai, China) for 4 h in serum-free medium.

    Techniques: Binding Assay, Labeling, Staining, SDS Page, Liquid Chromatography with Mass Spectroscopy, Residue, Derivative Assay, Control, Thermal Shift Assay

    Functional role of Myh9 in Sa-induced epithelial injury and fibroblast activation. A: Relative mRNA expression of Myh9 in submandibular gland tissues as measured by qRT-PCR. B: Immunohistochemical staining analysis and (C) quantitative analysis of the expression of Myh9 in lung tissues. D and E: Western blot analysis (D) and corresponding quantification (E) of Myh9 protein expression in A253 cells treated with increasing concentrations of Sa. F and G: Western blot (F) and densitometric analysis (G) of Myh9 expression in NIH3T3 cells treated with Sa or TGF-β1 (positive control). H and I: Western blot (H) and quantification (I) of AQP5 expression in A253 cells treated with Sa, with or without the Myh9 inhibitor blebbistatin. J and K: Western blot (J) and quantification (K) of fibronectin and α-SMA protein levels in NIH3T3 cells treated with Sa, with or without blebbistatin. Data are presented as mean ± SD. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001; ns, not significant. # P < 0.05, ## P < 0.01 Sa group with 4-PBA treatment. α-SMA, alpha-smooth muscle actin; 4-PBA, 4-phenylbutyric acid; AQP5, aquaporin-5

    Journal: Journal of Lipid Research

    Article Title: Sphinganine as a potentially relevant metabolite in pulmonary involvement of primary Sjögren’s syndrome

    doi: 10.1016/j.jlr.2025.100961

    Figure Lengend Snippet: Functional role of Myh9 in Sa-induced epithelial injury and fibroblast activation. A: Relative mRNA expression of Myh9 in submandibular gland tissues as measured by qRT-PCR. B: Immunohistochemical staining analysis and (C) quantitative analysis of the expression of Myh9 in lung tissues. D and E: Western blot analysis (D) and corresponding quantification (E) of Myh9 protein expression in A253 cells treated with increasing concentrations of Sa. F and G: Western blot (F) and densitometric analysis (G) of Myh9 expression in NIH3T3 cells treated with Sa or TGF-β1 (positive control). H and I: Western blot (H) and quantification (I) of AQP5 expression in A253 cells treated with Sa, with or without the Myh9 inhibitor blebbistatin. J and K: Western blot (J) and quantification (K) of fibronectin and α-SMA protein levels in NIH3T3 cells treated with Sa, with or without blebbistatin. Data are presented as mean ± SD. ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001; ns, not significant. # P < 0.05, ## P < 0.01 Sa group with 4-PBA treatment. α-SMA, alpha-smooth muscle actin; 4-PBA, 4-phenylbutyric acid; AQP5, aquaporin-5

    Article Snippet: For the Myh9 inhibition assay, cells were pretreated with 2 μM Blebbistatin (TargetMol, Shanghai, China) for 4 h in serum-free medium.

    Techniques: Functional Assay, Activation Assay, Expressing, Quantitative RT-PCR, Immunohistochemical staining, Staining, Western Blot, Positive Control

    Molecular mechanism of Sa induces salivary hyposecretion and pulmonary fibrosis in pSS through the ATF6–Myh9 signaling pathway. Sa, sphinganine; pSS, primary Sjögren’s syndrome.

    Journal: Journal of Lipid Research

    Article Title: Sphinganine as a potentially relevant metabolite in pulmonary involvement of primary Sjögren’s syndrome

    doi: 10.1016/j.jlr.2025.100961

    Figure Lengend Snippet: Molecular mechanism of Sa induces salivary hyposecretion and pulmonary fibrosis in pSS through the ATF6–Myh9 signaling pathway. Sa, sphinganine; pSS, primary Sjögren’s syndrome.

    Article Snippet: For the Myh9 inhibition assay, cells were pretreated with 2 μM Blebbistatin (TargetMol, Shanghai, China) for 4 h in serum-free medium.

    Techniques: