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human heparan sulfate  (Cusabio)


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    Structured Review

    Cusabio human heparan sulfate
    Endothelial glycocalyx degradation in HFRS patients in plasma and association with acute severe injury or need of oxygen HFRS patients were stratified into two groups of severe AKI (stage 2/3) or not (AKI stage 0/1) according to KDIGO criteria and in two groups need of oxygen or not. The estimated mean and standard error for each group were calculated using generalized estimating equation (GEE) and adjusted for sex and age. Receiver operating characteristics curve (ROC) analysis were performed using maximum values of eGLX markers and minimal values of albumin. The timeline kinetics and ROC curves are shown for syndecan-1 (A), <t>heparan</t> sulfate (B), soluble thrombomodulin (C), albumin (D) MMP-9 (E), and NGAL (F). Significant differences within the same time point between marker levels are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). AKI, acute kidney injury; HFRS, hemorrhagic fever with renal syndrome; HS, heparan sulfate; KDIGO, Kidney Disease Improval Global Outcomes; SDC-1, syndecan-1; P, plasma; sTM, soluble thrombomodulin; MMP9, matrix metalloproteinase 9; NGAL, neutrophil gelatinase-associated lipocalin.
    Human Heparan Sulfate, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/human heparan sulfate/product/Cusabio
    Average 93 stars, based on 7 article reviews
    human heparan sulfate - by Bioz Stars, 2026-03
    93/100 stars

    Images

    1) Product Images from "Matrix metalloproteinase-9 mediates endothelial glycocalyx degradation and correlates with severity of hemorrhagic fever with renal syndrome"

    Article Title: Matrix metalloproteinase-9 mediates endothelial glycocalyx degradation and correlates with severity of hemorrhagic fever with renal syndrome

    Journal: iScience

    doi: 10.1016/j.isci.2025.113262

    Endothelial glycocalyx degradation in HFRS patients in plasma and association with acute severe injury or need of oxygen HFRS patients were stratified into two groups of severe AKI (stage 2/3) or not (AKI stage 0/1) according to KDIGO criteria and in two groups need of oxygen or not. The estimated mean and standard error for each group were calculated using generalized estimating equation (GEE) and adjusted for sex and age. Receiver operating characteristics curve (ROC) analysis were performed using maximum values of eGLX markers and minimal values of albumin. The timeline kinetics and ROC curves are shown for syndecan-1 (A), heparan sulfate (B), soluble thrombomodulin (C), albumin (D) MMP-9 (E), and NGAL (F). Significant differences within the same time point between marker levels are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). AKI, acute kidney injury; HFRS, hemorrhagic fever with renal syndrome; HS, heparan sulfate; KDIGO, Kidney Disease Improval Global Outcomes; SDC-1, syndecan-1; P, plasma; sTM, soluble thrombomodulin; MMP9, matrix metalloproteinase 9; NGAL, neutrophil gelatinase-associated lipocalin.
    Figure Legend Snippet: Endothelial glycocalyx degradation in HFRS patients in plasma and association with acute severe injury or need of oxygen HFRS patients were stratified into two groups of severe AKI (stage 2/3) or not (AKI stage 0/1) according to KDIGO criteria and in two groups need of oxygen or not. The estimated mean and standard error for each group were calculated using generalized estimating equation (GEE) and adjusted for sex and age. Receiver operating characteristics curve (ROC) analysis were performed using maximum values of eGLX markers and minimal values of albumin. The timeline kinetics and ROC curves are shown for syndecan-1 (A), heparan sulfate (B), soluble thrombomodulin (C), albumin (D) MMP-9 (E), and NGAL (F). Significant differences within the same time point between marker levels are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). AKI, acute kidney injury; HFRS, hemorrhagic fever with renal syndrome; HS, heparan sulfate; KDIGO, Kidney Disease Improval Global Outcomes; SDC-1, syndecan-1; P, plasma; sTM, soluble thrombomodulin; MMP9, matrix metalloproteinase 9; NGAL, neutrophil gelatinase-associated lipocalin.

    Techniques Used: Clinical Proteomics, Marker

    In vitro glycocalyx degradation mediated by heparanase and MMP-9 followed by QCM-D (A) b-HS and (B) rhSDC-1 protein were absorbed on synthetic membrane composed by POPC-DOPE (95:5) lipids and streptavidin, plus Tris-NTA linker for rhSDC-1. After incubation with albumin at 40, 20, or 10 mg/mL, real-time degradation of b-HS by HPSE at 250 ng/mL (C) and rhSDC1 by MMP-9 at 500 ng/mL (D). Arrow indicates when the enzyme is injected. Shift in frequency (Δf) and dissipation (ΔD) due to enzyme activity was measured after enzyme activity in enzyme buffer. Percentage of Δf and ΔD signal reduction for b-HS (E) and rhSDC1 (F) after enzymatic treatment ( n = 4) were calculated from the b-HS or rhSDC-1 signal in enzyme buffer (corresponding to 100%). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). QCM-D, quartz crystal microbalance with dissipation; b-HS, biotinylated heparan sulfate; rhSDC-1, recombinant human syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.
    Figure Legend Snippet: In vitro glycocalyx degradation mediated by heparanase and MMP-9 followed by QCM-D (A) b-HS and (B) rhSDC-1 protein were absorbed on synthetic membrane composed by POPC-DOPE (95:5) lipids and streptavidin, plus Tris-NTA linker for rhSDC-1. After incubation with albumin at 40, 20, or 10 mg/mL, real-time degradation of b-HS by HPSE at 250 ng/mL (C) and rhSDC1 by MMP-9 at 500 ng/mL (D). Arrow indicates when the enzyme is injected. Shift in frequency (Δf) and dissipation (ΔD) due to enzyme activity was measured after enzyme activity in enzyme buffer. Percentage of Δf and ΔD signal reduction for b-HS (E) and rhSDC1 (F) after enzymatic treatment ( n = 4) were calculated from the b-HS or rhSDC-1 signal in enzyme buffer (corresponding to 100%). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). QCM-D, quartz crystal microbalance with dissipation; b-HS, biotinylated heparan sulfate; rhSDC-1, recombinant human syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.

    Techniques Used: In Vitro, QCM-D, Membrane, Incubation, Injection, Activity Assay, Recombinant

    In vitro endothelial glycocalyx degradation and endothelial barrier disruption followed by impedance measurement (A) SDC-1 staining on ciGEnC cells after incubation with MMP-9 enzyme and increased concentration of albumin (scale bars 20 μm). (B) SDC-1 fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (C) HS staining on ciGEnC cells after incubation with HSPE enzyme and increased concentration of albumin (scale bars 20 μm). (D) HS fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (E) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with MMP-9 and albumin (averaged of 2 values per conditions, n = 3 assays). (F) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with HSPE and albumin (averaged of 2 values per conditions, n = 3 assays). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). HS, heparan sulfate; SDC-1, syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.
    Figure Legend Snippet: In vitro endothelial glycocalyx degradation and endothelial barrier disruption followed by impedance measurement (A) SDC-1 staining on ciGEnC cells after incubation with MMP-9 enzyme and increased concentration of albumin (scale bars 20 μm). (B) SDC-1 fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (C) HS staining on ciGEnC cells after incubation with HSPE enzyme and increased concentration of albumin (scale bars 20 μm). (D) HS fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (E) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with MMP-9 and albumin (averaged of 2 values per conditions, n = 3 assays). (F) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with HSPE and albumin (averaged of 2 values per conditions, n = 3 assays). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). HS, heparan sulfate; SDC-1, syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.

    Techniques Used: In Vitro, Disruption, Staining, Incubation, Concentration Assay, Fluorescence, Control



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    Image Search Results


    Endothelial glycocalyx degradation in HFRS patients in plasma and association with acute severe injury or need of oxygen HFRS patients were stratified into two groups of severe AKI (stage 2/3) or not (AKI stage 0/1) according to KDIGO criteria and in two groups need of oxygen or not. The estimated mean and standard error for each group were calculated using generalized estimating equation (GEE) and adjusted for sex and age. Receiver operating characteristics curve (ROC) analysis were performed using maximum values of eGLX markers and minimal values of albumin. The timeline kinetics and ROC curves are shown for syndecan-1 (A), heparan sulfate (B), soluble thrombomodulin (C), albumin (D) MMP-9 (E), and NGAL (F). Significant differences within the same time point between marker levels are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). AKI, acute kidney injury; HFRS, hemorrhagic fever with renal syndrome; HS, heparan sulfate; KDIGO, Kidney Disease Improval Global Outcomes; SDC-1, syndecan-1; P, plasma; sTM, soluble thrombomodulin; MMP9, matrix metalloproteinase 9; NGAL, neutrophil gelatinase-associated lipocalin.

    Journal: iScience

    Article Title: Matrix metalloproteinase-9 mediates endothelial glycocalyx degradation and correlates with severity of hemorrhagic fever with renal syndrome

    doi: 10.1016/j.isci.2025.113262

    Figure Lengend Snippet: Endothelial glycocalyx degradation in HFRS patients in plasma and association with acute severe injury or need of oxygen HFRS patients were stratified into two groups of severe AKI (stage 2/3) or not (AKI stage 0/1) according to KDIGO criteria and in two groups need of oxygen or not. The estimated mean and standard error for each group were calculated using generalized estimating equation (GEE) and adjusted for sex and age. Receiver operating characteristics curve (ROC) analysis were performed using maximum values of eGLX markers and minimal values of albumin. The timeline kinetics and ROC curves are shown for syndecan-1 (A), heparan sulfate (B), soluble thrombomodulin (C), albumin (D) MMP-9 (E), and NGAL (F). Significant differences within the same time point between marker levels are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). AKI, acute kidney injury; HFRS, hemorrhagic fever with renal syndrome; HS, heparan sulfate; KDIGO, Kidney Disease Improval Global Outcomes; SDC-1, syndecan-1; P, plasma; sTM, soluble thrombomodulin; MMP9, matrix metalloproteinase 9; NGAL, neutrophil gelatinase-associated lipocalin.

    Article Snippet: Human heparan sulfate,HS ELISA Kit , Cusabio , CSB-E09585h.

    Techniques: Clinical Proteomics, Marker

    In vitro glycocalyx degradation mediated by heparanase and MMP-9 followed by QCM-D (A) b-HS and (B) rhSDC-1 protein were absorbed on synthetic membrane composed by POPC-DOPE (95:5) lipids and streptavidin, plus Tris-NTA linker for rhSDC-1. After incubation with albumin at 40, 20, or 10 mg/mL, real-time degradation of b-HS by HPSE at 250 ng/mL (C) and rhSDC1 by MMP-9 at 500 ng/mL (D). Arrow indicates when the enzyme is injected. Shift in frequency (Δf) and dissipation (ΔD) due to enzyme activity was measured after enzyme activity in enzyme buffer. Percentage of Δf and ΔD signal reduction for b-HS (E) and rhSDC1 (F) after enzymatic treatment ( n = 4) were calculated from the b-HS or rhSDC-1 signal in enzyme buffer (corresponding to 100%). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). QCM-D, quartz crystal microbalance with dissipation; b-HS, biotinylated heparan sulfate; rhSDC-1, recombinant human syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.

    Journal: iScience

    Article Title: Matrix metalloproteinase-9 mediates endothelial glycocalyx degradation and correlates with severity of hemorrhagic fever with renal syndrome

    doi: 10.1016/j.isci.2025.113262

    Figure Lengend Snippet: In vitro glycocalyx degradation mediated by heparanase and MMP-9 followed by QCM-D (A) b-HS and (B) rhSDC-1 protein were absorbed on synthetic membrane composed by POPC-DOPE (95:5) lipids and streptavidin, plus Tris-NTA linker for rhSDC-1. After incubation with albumin at 40, 20, or 10 mg/mL, real-time degradation of b-HS by HPSE at 250 ng/mL (C) and rhSDC1 by MMP-9 at 500 ng/mL (D). Arrow indicates when the enzyme is injected. Shift in frequency (Δf) and dissipation (ΔD) due to enzyme activity was measured after enzyme activity in enzyme buffer. Percentage of Δf and ΔD signal reduction for b-HS (E) and rhSDC1 (F) after enzymatic treatment ( n = 4) were calculated from the b-HS or rhSDC-1 signal in enzyme buffer (corresponding to 100%). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). QCM-D, quartz crystal microbalance with dissipation; b-HS, biotinylated heparan sulfate; rhSDC-1, recombinant human syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.

    Article Snippet: Human heparan sulfate,HS ELISA Kit , Cusabio , CSB-E09585h.

    Techniques: In Vitro, QCM-D, Membrane, Incubation, Injection, Activity Assay, Recombinant

    In vitro endothelial glycocalyx degradation and endothelial barrier disruption followed by impedance measurement (A) SDC-1 staining on ciGEnC cells after incubation with MMP-9 enzyme and increased concentration of albumin (scale bars 20 μm). (B) SDC-1 fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (C) HS staining on ciGEnC cells after incubation with HSPE enzyme and increased concentration of albumin (scale bars 20 μm). (D) HS fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (E) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with MMP-9 and albumin (averaged of 2 values per conditions, n = 3 assays). (F) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with HSPE and albumin (averaged of 2 values per conditions, n = 3 assays). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). HS, heparan sulfate; SDC-1, syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.

    Journal: iScience

    Article Title: Matrix metalloproteinase-9 mediates endothelial glycocalyx degradation and correlates with severity of hemorrhagic fever with renal syndrome

    doi: 10.1016/j.isci.2025.113262

    Figure Lengend Snippet: In vitro endothelial glycocalyx degradation and endothelial barrier disruption followed by impedance measurement (A) SDC-1 staining on ciGEnC cells after incubation with MMP-9 enzyme and increased concentration of albumin (scale bars 20 μm). (B) SDC-1 fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (C) HS staining on ciGEnC cells after incubation with HSPE enzyme and increased concentration of albumin (scale bars 20 μm). (D) HS fluorescence quantification after treatment compared to control (no treatment) (averaged values of 3 sections per condition, n = 3 assays). (E) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with MMP-9 and albumin (averaged of 2 values per conditions, n = 3 assays). (F) Endothelial barrier resistance followed by impedance measurement (ECIS, APBiophysic) on ciGEnC after treatment with HSPE and albumin (averaged of 2 values per conditions, n = 3 assays). Data are represented as mean ± SD. Significant differences are indicated by asterisks (∗∗∗ p < 0.001; ∗∗ p < 0.01; and ∗ p < 0.05). HS, heparan sulfate; SDC-1, syndecan-1; MMP-9, matrix metalloproteinase 9; HPSE, human heparanase.

    Article Snippet: Human heparan sulfate,HS ELISA Kit , Cusabio , CSB-E09585h.

    Techniques: In Vitro, Disruption, Staining, Incubation, Concentration Assay, Fluorescence, Control