Review

jak1 protein (MedChemExpress)

Name: jak1 protein
Brand: MedChemExpress
Rating: 93 (14 reviews)

MedChemExpress is a verified supplier

MedChemExpress manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

MedChemExpress jak1 protein

API Inhibits the JAK-STAT Signaling Pathway by Binding to the Target Protein <t>JAK1.</t> ( A ) Chemical structure and molecular formula of API; ( B ) Venn diagram showing 70 overlapping targets between API and ICH-related genes; ( C ) PPI network of API for ICH constructed using the STRING database; ( D ) Node information of relevant targets in the PPI network; ( E ) Visualization of the PPI network using Cytoscape, where larger nodes represent key targets and darker colors indicate stronger associations, with the inner circle highlighting core targets; ( F ) Identification of core targets in the PPI network using the CytoHubba plugin; ( G ) Quantitative analysis of BWC in mice across different treatment groups; ( H ) Representative micrographs showing IgG leakage in cerebral vasculature.( I ) Functional association analysis of core targets using GeneMANIA; ( J ) Functional association analysis of the target protein JAK1 using GeneMANIA; ( K ) GO enrichment plot covering BP, cellular components (CC), and molecular functions (MF); ( L ) KEGG pathway enrichment analysis performed using Metascape; ( M ) Molecular docking model of API with JAK1 visualized in PyMOL; ( N ) PyMOL visualization showing hydrogen bond interactions between API and key amino acids of JAK1; ( O ) Asteroidal view of the JAK1 co-crystal structure (PDB: 6RSC), where the inner ring indicates direct-contact residues and the outer ring indicates indirect-contact residues, color-coded and scaled based on secondary structure and number of contact atoms; ( P ) WB analysis of p-JAK1/JAK1 expression in perihematomal brain tissues of each group; ( Q - R ) Quantification of p-JAK1 and JAK1 protein levels by WB, n = 6; ( S ) WB analysis of p-STAT1/STAT1 expression in brain tissues of each group; ( T - U ) Quantitative analysis of p-STAT1 and STAT1 protein levels, n = 6. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey's multiple comparison test. * p< 0.05, ** p < 0.01, *** p < 0.001 vs. ICH group; ns: not significant

Jak1 Protein, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/jak1 protein/product/MedChemExpress
Average 93 stars, based on 14 article reviews

jak1 protein - by Bioz Stars, 2026-03

93/100 stars

Images

1) Product Images from "Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles"

Article Title: Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles

Journal: Journal of Nanobiotechnology

doi: 10.1186/s12951-025-03748-6

API Inhibits the JAK-STAT Signaling Pathway by Binding to the Target Protein JAK1. ( A ) Chemical structure and molecular formula of API; ( B ) Venn diagram showing 70 overlapping targets between API and ICH-related genes; ( C ) PPI network of API for ICH constructed using the STRING database; ( D ) Node information of relevant targets in the PPI network; ( E ) Visualization of the PPI network using Cytoscape, where larger nodes represent key targets and darker colors indicate stronger associations, with the inner circle highlighting core targets; ( F ) Identification of core targets in the PPI network using the CytoHubba plugin; ( G ) Quantitative analysis of BWC in mice across different treatment groups; ( H ) Representative micrographs showing IgG leakage in cerebral vasculature.( I ) Functional association analysis of core targets using GeneMANIA; ( J ) Functional association analysis of the target protein JAK1 using GeneMANIA; ( K ) GO enrichment plot covering BP, cellular components (CC), and molecular functions (MF); ( L ) KEGG pathway enrichment analysis performed using Metascape; ( M ) Molecular docking model of API with JAK1 visualized in PyMOL; ( N ) PyMOL visualization showing hydrogen bond interactions between API and key amino acids of JAK1; ( O ) Asteroidal view of the JAK1 co-crystal structure (PDB: 6RSC), where the inner ring indicates direct-contact residues and the outer ring indicates indirect-contact residues, color-coded and scaled based on secondary structure and number of contact atoms; ( P ) WB analysis of p-JAK1/JAK1 expression in perihematomal brain tissues of each group; ( Q - R ) Quantification of p-JAK1 and JAK1 protein levels by WB, n = 6; ( S ) WB analysis of p-STAT1/STAT1 expression in brain tissues of each group; ( T - U ) Quantitative analysis of p-STAT1 and STAT1 protein levels, n = 6. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey's multiple comparison test. * p< 0.05, ** p < 0.01, *** p < 0.001 vs. ICH group; ns: not significant

Figure Legend Snippet: API Inhibits the JAK-STAT Signaling Pathway by Binding to the Target Protein JAK1. ( A ) Chemical structure and molecular formula of API; ( B ) Venn diagram showing 70 overlapping targets between API and ICH-related genes; ( C ) PPI network of API for ICH constructed using the STRING database; ( D ) Node information of relevant targets in the PPI network; ( E ) Visualization of the PPI network using Cytoscape, where larger nodes represent key targets and darker colors indicate stronger associations, with the inner circle highlighting core targets; ( F ) Identification of core targets in the PPI network using the CytoHubba plugin; ( G ) Quantitative analysis of BWC in mice across different treatment groups; ( H ) Representative micrographs showing IgG leakage in cerebral vasculature.( I ) Functional association analysis of core targets using GeneMANIA; ( J ) Functional association analysis of the target protein JAK1 using GeneMANIA; ( K ) GO enrichment plot covering BP, cellular components (CC), and molecular functions (MF); ( L ) KEGG pathway enrichment analysis performed using Metascape; ( M ) Molecular docking model of API with JAK1 visualized in PyMOL; ( N ) PyMOL visualization showing hydrogen bond interactions between API and key amino acids of JAK1; ( O ) Asteroidal view of the JAK1 co-crystal structure (PDB: 6RSC), where the inner ring indicates direct-contact residues and the outer ring indicates indirect-contact residues, color-coded and scaled based on secondary structure and number of contact atoms; ( P ) WB analysis of p-JAK1/JAK1 expression in perihematomal brain tissues of each group; ( Q - R ) Quantification of p-JAK1 and JAK1 protein levels by WB, n = 6; ( S ) WB analysis of p-STAT1/STAT1 expression in brain tissues of each group; ( T - U ) Quantitative analysis of p-STAT1 and STAT1 protein levels, n = 6. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey's multiple comparison test. * p< 0.05, ** p < 0.01, *** p < 0.001 vs. ICH group; ns: not significant

Techniques Used: Binding Assay, Construct, Functional Assay, Expressing, Comparison

API Improves BBB Function and Inhibits Macrophage-Mediated Neurotoxicity via MMP Suppression. ( A ) Molecular docking model of API with MMP9 visualized using PyMOL and LigPlot, molecular docking model of API with MMP3, molecular docking model of API with MMP2; ( B ) Western blot (WB) analysis of MMP9, MMP2, and MMP3 expression in mouse brain tissues and corresponding quantification, n = 6; ( C ) WB analysis of ZO-1 and CLDN5 expression in brain tissues and corresponding quantification, n = 6; ( D ) Macrophage viability assessed by the CCK-8 assay, n = 6; ( E ) WB analysis of p-JAK1 expression following LPS stimulation, n = 6; WB analysis of p-JAK1 expression at different time points after LPS stimulation, n = 3; ( F ) WB analysis and quantification of MMP expression under different concentrations of API treatment, n = 3; ( G - H ) Immunofluorescence detection of MMP9 and MMP3 expression, scale bar = 50 μm; ( I ) Cell viability of HT-22 neurons after co-culture with differently treated macrophages, following 12 h API treatment at various concentrations, cell viability of HT-22 neurons treated with 40 μM API; ( J ) Immunofluorescence staining of Bax; ( K ) WB analysis of Bax and Bcl-2 expression in each group, n = 3; ( L ) WB analysis of NF-κB, PSD-95, and GAP-43 expression in neurons, n = 3; ( M ) Immunofluorescence staining of NF-κB; ( N ) Live/dead cell staining to assess neuronal viability in each group, with green indicating live cells. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey’s multiple comparison test. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. ICH group; ns: not significant

Figure Legend Snippet: API Improves BBB Function and Inhibits Macrophage-Mediated Neurotoxicity via MMP Suppression. ( A ) Molecular docking model of API with MMP9 visualized using PyMOL and LigPlot, molecular docking model of API with MMP3, molecular docking model of API with MMP2; ( B ) Western blot (WB) analysis of MMP9, MMP2, and MMP3 expression in mouse brain tissues and corresponding quantification, n = 6; ( C ) WB analysis of ZO-1 and CLDN5 expression in brain tissues and corresponding quantification, n = 6; ( D ) Macrophage viability assessed by the CCK-8 assay, n = 6; ( E ) WB analysis of p-JAK1 expression following LPS stimulation, n = 6; WB analysis of p-JAK1 expression at different time points after LPS stimulation, n = 3; ( F ) WB analysis and quantification of MMP expression under different concentrations of API treatment, n = 3; ( G - H ) Immunofluorescence detection of MMP9 and MMP3 expression, scale bar = 50 μm; ( I ) Cell viability of HT-22 neurons after co-culture with differently treated macrophages, following 12 h API treatment at various concentrations, cell viability of HT-22 neurons treated with 40 μM API; ( J ) Immunofluorescence staining of Bax; ( K ) WB analysis of Bax and Bcl-2 expression in each group, n = 3; ( L ) WB analysis of NF-κB, PSD-95, and GAP-43 expression in neurons, n = 3; ( M ) Immunofluorescence staining of NF-κB; ( N ) Live/dead cell staining to assess neuronal viability in each group, with green indicating live cells. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey’s multiple comparison test. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. ICH group; ns: not significant

Techniques Used: Western Blot, Expressing, CCK-8 Assay, Immunofluorescence, Co-Culture Assay, Staining, Comparison

Activation of the CCR5-JAK1-STAT1-MMPs Signaling Pathway in the Perihematomal Region Following ICH.( A ) Volcano plot of DEGs. Red indicates upregulated genes, gray indicates non-significant genes, and blue indicates downregulated genes. Screening criteria: p < 0.05 and log₂FC ≥ 0.5; ( B ) Heatmap of DEGs, with red indicating high expression and blue indicating low expression; ( C ) Bar chart of CCL4, CCL5, CCR5, JAK1, STAT3, and MMP3 expression; ( D ) Heatmap of module-trait relationships with ICH and control groups, where red indicates positive correlation and blue indicates negative correlation; ( E - F ) GO and KEGG enrichment analyses of DEGs in the brown module; ( G - H ) GO and KEGG enrichment analyses of DEGs in the yellow module; ( I ) qPCR validation of CCL3, CCL4, and CCL5 expression after ICH; ( J ) WB and quantitative analysis of CCR5, IBA-1, p-JAK1, JAK1, and MMP9 protein levels in brain tissues on days 1, 3, and 7 post-ICH; ( K ) WB analysis of JAK1-STAT1-MMP pathway-related proteins on day 3 post-ICH; ( L ) Evaluation of CCR5 expression in macrophages under different treatment conditions following administration of the CCR5 inhibitor MVC (100 mg/kg). rCCL4 treatment upregulated CCR5 expression, while API showed no significant effect; ( M ) Under rCCL4 stimulation (1 μg/mL), assessment of p-JAK1 expression revealed that MVC (5 μM) inhibited its expression; ( N ) Immunofluorescence analysis of p-JAK1 phosphorylation levels in macrophages following MVC intervention. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey's multiple comparison test. * p < 0.05,** p < 0.01, *** p < 0.001, **** p < 0.0001 vs. ICH group or ICH + 3 d group; ns: not significant

Figure Legend Snippet: Activation of the CCR5-JAK1-STAT1-MMPs Signaling Pathway in the Perihematomal Region Following ICH.( A ) Volcano plot of DEGs. Red indicates upregulated genes, gray indicates non-significant genes, and blue indicates downregulated genes. Screening criteria: p < 0.05 and log₂FC ≥ 0.5; ( B ) Heatmap of DEGs, with red indicating high expression and blue indicating low expression; ( C ) Bar chart of CCL4, CCL5, CCR5, JAK1, STAT3, and MMP3 expression; ( D ) Heatmap of module-trait relationships with ICH and control groups, where red indicates positive correlation and blue indicates negative correlation; ( E - F ) GO and KEGG enrichment analyses of DEGs in the brown module; ( G - H ) GO and KEGG enrichment analyses of DEGs in the yellow module; ( I ) qPCR validation of CCL3, CCL4, and CCL5 expression after ICH; ( J ) WB and quantitative analysis of CCR5, IBA-1, p-JAK1, JAK1, and MMP9 protein levels in brain tissues on days 1, 3, and 7 post-ICH; ( K ) WB analysis of JAK1-STAT1-MMP pathway-related proteins on day 3 post-ICH; ( L ) Evaluation of CCR5 expression in macrophages under different treatment conditions following administration of the CCR5 inhibitor MVC (100 mg/kg). rCCL4 treatment upregulated CCR5 expression, while API showed no significant effect; ( M ) Under rCCL4 stimulation (1 μg/mL), assessment of p-JAK1 expression revealed that MVC (5 μM) inhibited its expression; ( N ) Immunofluorescence analysis of p-JAK1 phosphorylation levels in macrophages following MVC intervention. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey's multiple comparison test. * p < 0.05,** p < 0.01, *** p < 0.001, **** p < 0.0001 vs. ICH group or ICH + 3 d group; ns: not significant

Techniques Used: Activation Assay, Expressing, Control, Biomarker Discovery, Immunofluorescence, Phospho-proteomics, Comparison

API Co-localizes and Irreversibly Binds with JAK1 Target Protein.( A ) Chemical structures of API and API-biotin are shown; ( B ) After treatment of macrophages with 50 nM API-biotin for 6 hours, immunofluorescence staining was performed using anti-biotin antibody (red) and anti-JAK1 primary antibody, followed by fluorescent secondary antibody (green) to label the JAK1 target protein. Nuclei were stained with DAPI (blue). Representative images from three independent experiments are displayed, with white boxes indicating regions of co-localization between API and JAK1. Scale bar = 50 μm; ( C ) API binds to JAK1. API-conjugated magnetic beads competed with or without free API for binding to JAK1 in macrophage lysates, and WB detected bound proteins; ( D - E ) API enhanced the resistance of JAK1 protein to proteolytic degradation, as determined by DARTS assay; ( F ) SPR analysis confirmed the binding interaction between API and JAK1; ( G - H ) CETSA was performed using macrophage lysates to evaluate the thermal stability of JAK1 following treatment with 50 μM API; ( I ) API irreversibly binds to JAK1. In the co-treatment group, macrophage lysates were incubated with API-conjugated magnetic beads for 12 hours in the presence or absence of free API; ( J ) In the post-treatment group, lysates were first incubated with API-conjugated magnetic beads for 12 hours, followed by a further 12-hour incubation with or without free API. In the pre-treatment group, lysates were pre-incubated with free API for 12 hours and then incubated with API-conjugated magnetic beads for another 12 hours to verify competitive binding. ( K ) In vitro JAK2 kinase assays under PTE conditions (0μM, 10 μM, 20 μM); ( L ) Molecular docking analysis of API with the kinase domains of JAK1 (RCSB PDB ID: 5E1E), JAK2 (RCSB PDB ID: 2B7A), and JAK3 (RCSB PDB ID: 3PJC). All data are presented as mean ± SD. Statistical significance was determined by two-way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 vs. Vehicle group; ns: not significant

Figure Legend Snippet: API Co-localizes and Irreversibly Binds with JAK1 Target Protein.( A ) Chemical structures of API and API-biotin are shown; ( B ) After treatment of macrophages with 50 nM API-biotin for 6 hours, immunofluorescence staining was performed using anti-biotin antibody (red) and anti-JAK1 primary antibody, followed by fluorescent secondary antibody (green) to label the JAK1 target protein. Nuclei were stained with DAPI (blue). Representative images from three independent experiments are displayed, with white boxes indicating regions of co-localization between API and JAK1. Scale bar = 50 μm; ( C ) API binds to JAK1. API-conjugated magnetic beads competed with or without free API for binding to JAK1 in macrophage lysates, and WB detected bound proteins; ( D - E ) API enhanced the resistance of JAK1 protein to proteolytic degradation, as determined by DARTS assay; ( F ) SPR analysis confirmed the binding interaction between API and JAK1; ( G - H ) CETSA was performed using macrophage lysates to evaluate the thermal stability of JAK1 following treatment with 50 μM API; ( I ) API irreversibly binds to JAK1. In the co-treatment group, macrophage lysates were incubated with API-conjugated magnetic beads for 12 hours in the presence or absence of free API; ( J ) In the post-treatment group, lysates were first incubated with API-conjugated magnetic beads for 12 hours, followed by a further 12-hour incubation with or without free API. In the pre-treatment group, lysates were pre-incubated with free API for 12 hours and then incubated with API-conjugated magnetic beads for another 12 hours to verify competitive binding. ( K ) In vitro JAK2 kinase assays under PTE conditions (0μM, 10 μM, 20 μM); ( L ) Molecular docking analysis of API with the kinase domains of JAK1 (RCSB PDB ID: 5E1E), JAK2 (RCSB PDB ID: 2B7A), and JAK3 (RCSB PDB ID: 3PJC). All data are presented as mean ± SD. Statistical significance was determined by two-way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 vs. Vehicle group; ns: not significant

Techniques Used: Immunofluorescence, Staining, Magnetic Beads, Binding Assay, Incubation, In Vitro

RVG/FA-NPs@API Alleviates Neurotoxicity by Inhibiting the CCR5/JAK1/STAT1/MMPs Pathway in Macrophages.( A ) Schematic diagram illustrating the LPS-induced macrophage inflammation model, the intervention of RVG/FA-NPs@API, and its neuroprotective mechanism, created in BioRender; ( B ) mRNA expression level of CCR5 in RAW264.7 cells detected by RT-qPCR; ( C ) Protein expression levels of CCR5, JAK1, p-JAK1, STAT1, p-STAT1, MMP9, and MMP3 in macrophages determined by WB; ( D ) Protein expression levels of TNF-α and IL-1β in RAW264.7 cells detected by WB; ( E ) Immunofluorescence staining of iNOS and Arg1 in RAW264.7 cells, scale bar = 25 μm; ( F ) Cell viability of HT-22 neurons after co-culture with different treatment groups assessed using the CCK-8 assay; ( G ) Neuronal apoptosis and death assessed using Calcein-AM/PI double staining, scale bar = 50 μm; ( H ) Expression levels of Bax, Bcl-2, NF200, PSD95, and GAP43 proteins in neurons detected by WB. All cell experiments were repeated three times. * p < 0.05, ** p < 0.01, *** p < 0.001,**** p < 0.0001 between groups

Figure Legend Snippet: RVG/FA-NPs@API Alleviates Neurotoxicity by Inhibiting the CCR5/JAK1/STAT1/MMPs Pathway in Macrophages.( A ) Schematic diagram illustrating the LPS-induced macrophage inflammation model, the intervention of RVG/FA-NPs@API, and its neuroprotective mechanism, created in BioRender; ( B ) mRNA expression level of CCR5 in RAW264.7 cells detected by RT-qPCR; ( C ) Protein expression levels of CCR5, JAK1, p-JAK1, STAT1, p-STAT1, MMP9, and MMP3 in macrophages determined by WB; ( D ) Protein expression levels of TNF-α and IL-1β in RAW264.7 cells detected by WB; ( E ) Immunofluorescence staining of iNOS and Arg1 in RAW264.7 cells, scale bar = 25 μm; ( F ) Cell viability of HT-22 neurons after co-culture with different treatment groups assessed using the CCK-8 assay; ( G ) Neuronal apoptosis and death assessed using Calcein-AM/PI double staining, scale bar = 50 μm; ( H ) Expression levels of Bax, Bcl-2, NF200, PSD95, and GAP43 proteins in neurons detected by WB. All cell experiments were repeated three times. * p < 0.05, ** p < 0.01, *** p < 0.001,**** p < 0.0001 between groups

Techniques Used: Expressing, Quantitative RT-PCR, Immunofluorescence, Staining, Co-Culture Assay, CCK-8 Assay, Double Staining

RVG/FA-NPs@API Alleviates SBI in ICH Mice. ( A ) Schematic diagram of the experimental workflow illustrating the intervention strategy and group design of RVG/FA-NPs@API in the ICH model, created in BioRender; ( B ) BWC in each group measured by the wet-dry weight method; ( C ) Pathological changes in brain tissue assessed by H&E staining, scale bar = 100 μm; ( D ) Neuronal arrangement and density in brain tissue evaluated by Nissl staining, scale bar = 100 μm; ( E ) Proportion of apoptotic neurons in brain tissue detected by TUNEL staining, with TUNEL-positive cells shown in green, scale bar = 50 μm; ( F ) Expression levels of iNOS (green) and Arg1 (red) in brain tissue detected by immunofluorescence, scale bar = 25 μm; ( G ) Protein expression levels of CCR5, p-JAK1, p-STAT1, MMP9, MMP3, ZO-1, and CLDN5 in brain tissue detected by WB. Each group included n = 6 animals. * p < 0.05, ** p < 0.01, *** p < 0.001 between groups

Figure Legend Snippet: RVG/FA-NPs@API Alleviates SBI in ICH Mice. ( A ) Schematic diagram of the experimental workflow illustrating the intervention strategy and group design of RVG/FA-NPs@API in the ICH model, created in BioRender; ( B ) BWC in each group measured by the wet-dry weight method; ( C ) Pathological changes in brain tissue assessed by H&E staining, scale bar = 100 μm; ( D ) Neuronal arrangement and density in brain tissue evaluated by Nissl staining, scale bar = 100 μm; ( E ) Proportion of apoptotic neurons in brain tissue detected by TUNEL staining, with TUNEL-positive cells shown in green, scale bar = 50 μm; ( F ) Expression levels of iNOS (green) and Arg1 (red) in brain tissue detected by immunofluorescence, scale bar = 25 μm; ( G ) Protein expression levels of CCR5, p-JAK1, p-STAT1, MMP9, MMP3, ZO-1, and CLDN5 in brain tissue detected by WB. Each group included n = 6 animals. * p < 0.05, ** p < 0.01, *** p < 0.001 between groups

Techniques Used: Staining, TUNEL Assay, Expressing, Immunofluorescence

Image Search Results

Journal: Journal of Nanobiotechnology

Article Title: Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles

doi: 10.1186/s12951-025-03748-6

Figure Lengend Snippet: API Inhibits the JAK-STAT Signaling Pathway by Binding to the Target Protein JAK1. ( A ) Chemical structure and molecular formula of API; ( B ) Venn diagram showing 70 overlapping targets between API and ICH-related genes; ( C ) PPI network of API for ICH constructed using the STRING database; ( D ) Node information of relevant targets in the PPI network; ( E ) Visualization of the PPI network using Cytoscape, where larger nodes represent key targets and darker colors indicate stronger associations, with the inner circle highlighting core targets; ( F ) Identification of core targets in the PPI network using the CytoHubba plugin; ( G ) Quantitative analysis of BWC in mice across different treatment groups; ( H ) Representative micrographs showing IgG leakage in cerebral vasculature.( I ) Functional association analysis of core targets using GeneMANIA; ( J ) Functional association analysis of the target protein JAK1 using GeneMANIA; ( K ) GO enrichment plot covering BP, cellular components (CC), and molecular functions (MF); ( L ) KEGG pathway enrichment analysis performed using Metascape; ( M ) Molecular docking model of API with JAK1 visualized in PyMOL; ( N ) PyMOL visualization showing hydrogen bond interactions between API and key amino acids of JAK1; ( O ) Asteroidal view of the JAK1 co-crystal structure (PDB: 6RSC), where the inner ring indicates direct-contact residues and the outer ring indicates indirect-contact residues, color-coded and scaled based on secondary structure and number of contact atoms; ( P ) WB analysis of p-JAK1/JAK1 expression in perihematomal brain tissues of each group; ( Q - R ) Quantification of p-JAK1 and JAK1 protein levels by WB, n = 6; ( S ) WB analysis of p-STAT1/STAT1 expression in brain tissues of each group; ( T - U ) Quantitative analysis of p-STAT1 and STAT1 protein levels, n = 6. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey's multiple comparison test. * p< 0.05, ** p < 0.01, *** p < 0.001 vs. ICH group; ns: not significant

Article Snippet: The binding affinity between API and JAK1 protein (HY-P700583, MedChemExpress, USA) was evaluated using the SPR-based Biacore T200 instrument (Cytiva, Sweden).

Techniques: Binding Assay, Construct, Functional Assay, Expressing, Comparison

Journal: Journal of Nanobiotechnology

Article Title: Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles

doi: 10.1186/s12951-025-03748-6

Figure Lengend Snippet: API Improves BBB Function and Inhibits Macrophage-Mediated Neurotoxicity via MMP Suppression. ( A ) Molecular docking model of API with MMP9 visualized using PyMOL and LigPlot, molecular docking model of API with MMP3, molecular docking model of API with MMP2; ( B ) Western blot (WB) analysis of MMP9, MMP2, and MMP3 expression in mouse brain tissues and corresponding quantification, n = 6; ( C ) WB analysis of ZO-1 and CLDN5 expression in brain tissues and corresponding quantification, n = 6; ( D ) Macrophage viability assessed by the CCK-8 assay, n = 6; ( E ) WB analysis of p-JAK1 expression following LPS stimulation, n = 6; WB analysis of p-JAK1 expression at different time points after LPS stimulation, n = 3; ( F ) WB analysis and quantification of MMP expression under different concentrations of API treatment, n = 3; ( G - H ) Immunofluorescence detection of MMP9 and MMP3 expression, scale bar = 50 μm; ( I ) Cell viability of HT-22 neurons after co-culture with differently treated macrophages, following 12 h API treatment at various concentrations, cell viability of HT-22 neurons treated with 40 μM API; ( J ) Immunofluorescence staining of Bax; ( K ) WB analysis of Bax and Bcl-2 expression in each group, n = 3; ( L ) WB analysis of NF-κB, PSD-95, and GAP-43 expression in neurons, n = 3; ( M ) Immunofluorescence staining of NF-κB; ( N ) Live/dead cell staining to assess neuronal viability in each group, with green indicating live cells. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey’s multiple comparison test. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. ICH group; ns: not significant

Article Snippet: The binding affinity between API and JAK1 protein (HY-P700583, MedChemExpress, USA) was evaluated using the SPR-based Biacore T200 instrument (Cytiva, Sweden).

Techniques: Western Blot, Expressing, CCK-8 Assay, Immunofluorescence, Co-Culture Assay, Staining, Comparison

Journal: Journal of Nanobiotechnology

Article Title: Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles

doi: 10.1186/s12951-025-03748-6

Figure Lengend Snippet: Activation of the CCR5-JAK1-STAT1-MMPs Signaling Pathway in the Perihematomal Region Following ICH.( A ) Volcano plot of DEGs. Red indicates upregulated genes, gray indicates non-significant genes, and blue indicates downregulated genes. Screening criteria: p < 0.05 and log₂FC ≥ 0.5; ( B ) Heatmap of DEGs, with red indicating high expression and blue indicating low expression; ( C ) Bar chart of CCL4, CCL5, CCR5, JAK1, STAT3, and MMP3 expression; ( D ) Heatmap of module-trait relationships with ICH and control groups, where red indicates positive correlation and blue indicates negative correlation; ( E - F ) GO and KEGG enrichment analyses of DEGs in the brown module; ( G - H ) GO and KEGG enrichment analyses of DEGs in the yellow module; ( I ) qPCR validation of CCL3, CCL4, and CCL5 expression after ICH; ( J ) WB and quantitative analysis of CCR5, IBA-1, p-JAK1, JAK1, and MMP9 protein levels in brain tissues on days 1, 3, and 7 post-ICH; ( K ) WB analysis of JAK1-STAT1-MMP pathway-related proteins on day 3 post-ICH; ( L ) Evaluation of CCR5 expression in macrophages under different treatment conditions following administration of the CCR5 inhibitor MVC (100 mg/kg). rCCL4 treatment upregulated CCR5 expression, while API showed no significant effect; ( M ) Under rCCL4 stimulation (1 μg/mL), assessment of p-JAK1 expression revealed that MVC (5 μM) inhibited its expression; ( N ) Immunofluorescence analysis of p-JAK1 phosphorylation levels in macrophages following MVC intervention. All data are presented as mean ± SD. Statistical significance was determined using two-way ANOVA followed by Tukey's multiple comparison test. * p < 0.05,** p < 0.01, *** p < 0.001, **** p < 0.0001 vs. ICH group or ICH + 3 d group; ns: not significant

Article Snippet: The binding affinity between API and JAK1 protein (HY-P700583, MedChemExpress, USA) was evaluated using the SPR-based Biacore T200 instrument (Cytiva, Sweden).

Techniques: Activation Assay, Expressing, Control, Biomarker Discovery, Immunofluorescence, Phospho-proteomics, Comparison

Journal: Journal of Nanobiotechnology

Article Title: Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles

doi: 10.1186/s12951-025-03748-6

Figure Lengend Snippet: API Co-localizes and Irreversibly Binds with JAK1 Target Protein.( A ) Chemical structures of API and API-biotin are shown; ( B ) After treatment of macrophages with 50 nM API-biotin for 6 hours, immunofluorescence staining was performed using anti-biotin antibody (red) and anti-JAK1 primary antibody, followed by fluorescent secondary antibody (green) to label the JAK1 target protein. Nuclei were stained with DAPI (blue). Representative images from three independent experiments are displayed, with white boxes indicating regions of co-localization between API and JAK1. Scale bar = 50 μm; ( C ) API binds to JAK1. API-conjugated magnetic beads competed with or without free API for binding to JAK1 in macrophage lysates, and WB detected bound proteins; ( D - E ) API enhanced the resistance of JAK1 protein to proteolytic degradation, as determined by DARTS assay; ( F ) SPR analysis confirmed the binding interaction between API and JAK1; ( G - H ) CETSA was performed using macrophage lysates to evaluate the thermal stability of JAK1 following treatment with 50 μM API; ( I ) API irreversibly binds to JAK1. In the co-treatment group, macrophage lysates were incubated with API-conjugated magnetic beads for 12 hours in the presence or absence of free API; ( J ) In the post-treatment group, lysates were first incubated with API-conjugated magnetic beads for 12 hours, followed by a further 12-hour incubation with or without free API. In the pre-treatment group, lysates were pre-incubated with free API for 12 hours and then incubated with API-conjugated magnetic beads for another 12 hours to verify competitive binding. ( K ) In vitro JAK2 kinase assays under PTE conditions (0μM, 10 μM, 20 μM); ( L ) Molecular docking analysis of API with the kinase domains of JAK1 (RCSB PDB ID: 5E1E), JAK2 (RCSB PDB ID: 2B7A), and JAK3 (RCSB PDB ID: 3PJC). All data are presented as mean ± SD. Statistical significance was determined by two-way ANOVA followed by Tukey's multiple comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001 vs. Vehicle group; ns: not significant

Article Snippet: The binding affinity between API and JAK1 protein (HY-P700583, MedChemExpress, USA) was evaluated using the SPR-based Biacore T200 instrument (Cytiva, Sweden).

Techniques: Immunofluorescence, Staining, Magnetic Beads, Binding Assay, Incubation, In Vitro

Journal: Journal of Nanobiotechnology

Article Title: Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles

doi: 10.1186/s12951-025-03748-6

Figure Lengend Snippet: RVG/FA-NPs@API Alleviates Neurotoxicity by Inhibiting the CCR5/JAK1/STAT1/MMPs Pathway in Macrophages.( A ) Schematic diagram illustrating the LPS-induced macrophage inflammation model, the intervention of RVG/FA-NPs@API, and its neuroprotective mechanism, created in BioRender; ( B ) mRNA expression level of CCR5 in RAW264.7 cells detected by RT-qPCR; ( C ) Protein expression levels of CCR5, JAK1, p-JAK1, STAT1, p-STAT1, MMP9, and MMP3 in macrophages determined by WB; ( D ) Protein expression levels of TNF-α and IL-1β in RAW264.7 cells detected by WB; ( E ) Immunofluorescence staining of iNOS and Arg1 in RAW264.7 cells, scale bar = 25 μm; ( F ) Cell viability of HT-22 neurons after co-culture with different treatment groups assessed using the CCK-8 assay; ( G ) Neuronal apoptosis and death assessed using Calcein-AM/PI double staining, scale bar = 50 μm; ( H ) Expression levels of Bax, Bcl-2, NF200, PSD95, and GAP43 proteins in neurons detected by WB. All cell experiments were repeated three times. * p < 0.05, ** p < 0.01, *** p < 0.001,**** p < 0.0001 between groups

Article Snippet: The binding affinity between API and JAK1 protein (HY-P700583, MedChemExpress, USA) was evaluated using the SPR-based Biacore T200 instrument (Cytiva, Sweden).

Techniques: Expressing, Quantitative RT-PCR, Immunofluorescence, Staining, Co-Culture Assay, CCK-8 Assay, Double Staining

Journal: Journal of Nanobiotechnology

Article Title: Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles

doi: 10.1186/s12951-025-03748-6

Figure Lengend Snippet: RVG/FA-NPs@API Alleviates SBI in ICH Mice. ( A ) Schematic diagram of the experimental workflow illustrating the intervention strategy and group design of RVG/FA-NPs@API in the ICH model, created in BioRender; ( B ) BWC in each group measured by the wet-dry weight method; ( C ) Pathological changes in brain tissue assessed by H&E staining, scale bar = 100 μm; ( D ) Neuronal arrangement and density in brain tissue evaluated by Nissl staining, scale bar = 100 μm; ( E ) Proportion of apoptotic neurons in brain tissue detected by TUNEL staining, with TUNEL-positive cells shown in green, scale bar = 50 μm; ( F ) Expression levels of iNOS (green) and Arg1 (red) in brain tissue detected by immunofluorescence, scale bar = 25 μm; ( G ) Protein expression levels of CCR5, p-JAK1, p-STAT1, MMP9, MMP3, ZO-1, and CLDN5 in brain tissue detected by WB. Each group included n = 6 animals. * p < 0.05, ** p < 0.01, *** p < 0.001 between groups

Article Snippet: The binding affinity between API and JAK1 protein (HY-P700583, MedChemExpress, USA) was evaluated using the SPR-based Biacore T200 instrument (Cytiva, Sweden).

Techniques: Staining, TUNEL Assay, Expressing, Immunofluorescence

Review

Structured Review

Images

1) Product Images from "Apigenin regulates CCR5/JAK1/STAT1/MMPs signaling to alleviate secondary brain injury after intracerebral hemorrhage and its enhanced delivery via targeted nanoparticles"

Similar Products

Image Search Results