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neutrophil elastase  (R&D Systems)


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    Structured Review

    R&D Systems neutrophil elastase
    ( A ) Immunofluorescence staining of protease protein expression (red): cathepsin G (CTSG), caspase-1, and <t>neutrophil</t> elastase (ELANE), in 6-week KPS tumors. All sections counterstained with DAPI (blue). Scale bar 50um. ( B ) Schematic of antibody versus activity zymography probe (AZP) staining on frozen tissue sections. Protease cleavable substrates can be converted to AZPs that show cleavage locally on tissue. AZPs consist of a negatively charged reporter masked by a peptide substrate sequence that prevents it from binding to tissue until cleaved by localized target proteases. ( C ) Binding of activated AZPs (red) cleavable by CTSG (A1), caspase-1 (A10), and ELANE (A12) in lung tumor tissue. All sections counterstained with DAPI (blue). Scale bar 50um. ( D ) A10 AZP stained 7-week KPS lung sections significantly more in tumors and less in normal adjacent tissue (NAT) or healthy tissue. All sections counterstained with DAPI (blue). Scale bar 25um. Percentage of tissue regions that were positively stained for A10 were quantified. One-way ANOVA with Tukey’s multiple comparison test was performed (p < 0.05).
    Neutrophil Elastase, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/neutrophil elastase/product/R&D Systems
    Average 93 stars, based on 12 article reviews
    neutrophil elastase - by Bioz Stars, 2026-05
    93/100 stars

    Images

    1) Product Images from "Multimodal profiling of proinflammatory protease activity identifies caspase-1 as a target for lung cancer interception"

    Article Title: Multimodal profiling of proinflammatory protease activity identifies caspase-1 as a target for lung cancer interception

    Journal: bioRxiv

    doi: 10.1101/2025.07.01.662195

    ( A ) Immunofluorescence staining of protease protein expression (red): cathepsin G (CTSG), caspase-1, and neutrophil elastase (ELANE), in 6-week KPS tumors. All sections counterstained with DAPI (blue). Scale bar 50um. ( B ) Schematic of antibody versus activity zymography probe (AZP) staining on frozen tissue sections. Protease cleavable substrates can be converted to AZPs that show cleavage locally on tissue. AZPs consist of a negatively charged reporter masked by a peptide substrate sequence that prevents it from binding to tissue until cleaved by localized target proteases. ( C ) Binding of activated AZPs (red) cleavable by CTSG (A1), caspase-1 (A10), and ELANE (A12) in lung tumor tissue. All sections counterstained with DAPI (blue). Scale bar 50um. ( D ) A10 AZP stained 7-week KPS lung sections significantly more in tumors and less in normal adjacent tissue (NAT) or healthy tissue. All sections counterstained with DAPI (blue). Scale bar 25um. Percentage of tissue regions that were positively stained for A10 were quantified. One-way ANOVA with Tukey’s multiple comparison test was performed (p < 0.05).
    Figure Legend Snippet: ( A ) Immunofluorescence staining of protease protein expression (red): cathepsin G (CTSG), caspase-1, and neutrophil elastase (ELANE), in 6-week KPS tumors. All sections counterstained with DAPI (blue). Scale bar 50um. ( B ) Schematic of antibody versus activity zymography probe (AZP) staining on frozen tissue sections. Protease cleavable substrates can be converted to AZPs that show cleavage locally on tissue. AZPs consist of a negatively charged reporter masked by a peptide substrate sequence that prevents it from binding to tissue until cleaved by localized target proteases. ( C ) Binding of activated AZPs (red) cleavable by CTSG (A1), caspase-1 (A10), and ELANE (A12) in lung tumor tissue. All sections counterstained with DAPI (blue). Scale bar 50um. ( D ) A10 AZP stained 7-week KPS lung sections significantly more in tumors and less in normal adjacent tissue (NAT) or healthy tissue. All sections counterstained with DAPI (blue). Scale bar 25um. Percentage of tissue regions that were positively stained for A10 were quantified. One-way ANOVA with Tukey’s multiple comparison test was performed (p < 0.05).

    Techniques Used: Immunofluorescence, Staining, Expressing, Activity Assay, Zymography, Sequencing, Binding Assay, Comparison



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    Fig. 2 Neutrophil infiltration and NETs release within AAA lesions. A IF staining for neutrophil marker (Ly6G) was performed on tissue sections of the mouse abdominal aorta. B Hyalinization and IF labeling of the whole abdominal aorta and 3D tissue imaging were acquired with light-sheet microscopy. C–E Quantification of NETs markers <t>(ELANE</t> <t>and</t> <t>MPO)</t> in mouse abdominal aorta by western blotting (n = 3). **P < 0.01, ****P < 0.0001, indicating statistical significance between the two groups.
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    Evaluation of the HNE substrate sensor using <t>rmNE</t> and rhNE. A ) Representative MALDI-TOF mass spectra of the sensor and the cleavage products with different time points of reaction using rmNE. B ) The ratio of cleavage products to the sensor with different time points. C ) Specificity testing using a blank control, 15 µM of rhNE, 15 µM of cathepsin G (CTSG), and 15 µM of PR3. D ) LOD test at 37 °C for 24 h using different concentrations of rhNE.
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    Image Search Results


    ( A ) Immunofluorescence staining of protease protein expression (red): cathepsin G (CTSG), caspase-1, and neutrophil elastase (ELANE), in 6-week KPS tumors. All sections counterstained with DAPI (blue). Scale bar 50um. ( B ) Schematic of antibody versus activity zymography probe (AZP) staining on frozen tissue sections. Protease cleavable substrates can be converted to AZPs that show cleavage locally on tissue. AZPs consist of a negatively charged reporter masked by a peptide substrate sequence that prevents it from binding to tissue until cleaved by localized target proteases. ( C ) Binding of activated AZPs (red) cleavable by CTSG (A1), caspase-1 (A10), and ELANE (A12) in lung tumor tissue. All sections counterstained with DAPI (blue). Scale bar 50um. ( D ) A10 AZP stained 7-week KPS lung sections significantly more in tumors and less in normal adjacent tissue (NAT) or healthy tissue. All sections counterstained with DAPI (blue). Scale bar 25um. Percentage of tissue regions that were positively stained for A10 were quantified. One-way ANOVA with Tukey’s multiple comparison test was performed (p < 0.05).

    Journal: bioRxiv

    Article Title: Multimodal profiling of proinflammatory protease activity identifies caspase-1 as a target for lung cancer interception

    doi: 10.1101/2025.07.01.662195

    Figure Lengend Snippet: ( A ) Immunofluorescence staining of protease protein expression (red): cathepsin G (CTSG), caspase-1, and neutrophil elastase (ELANE), in 6-week KPS tumors. All sections counterstained with DAPI (blue). Scale bar 50um. ( B ) Schematic of antibody versus activity zymography probe (AZP) staining on frozen tissue sections. Protease cleavable substrates can be converted to AZPs that show cleavage locally on tissue. AZPs consist of a negatively charged reporter masked by a peptide substrate sequence that prevents it from binding to tissue until cleaved by localized target proteases. ( C ) Binding of activated AZPs (red) cleavable by CTSG (A1), caspase-1 (A10), and ELANE (A12) in lung tumor tissue. All sections counterstained with DAPI (blue). Scale bar 50um. ( D ) A10 AZP stained 7-week KPS lung sections significantly more in tumors and less in normal adjacent tissue (NAT) or healthy tissue. All sections counterstained with DAPI (blue). Scale bar 25um. Percentage of tissue regions that were positively stained for A10 were quantified. One-way ANOVA with Tukey’s multiple comparison test was performed (p < 0.05).

    Article Snippet: Recombinant proteases screened included caspase-1 (ALX-201-056-U025, Enzo), caspase-3 (707-C3, R&D Systems), caspase-7 (823-C7, R&D Systems), caspase-8 (ALX-201-163-C020, Enzo), cathepsin B (965-CY, R&D Systems), cathepsin G (BML-SE283-0100, Enzo), chymase-1 (4099-SE, R&D Systems), chymotrypsin (6907-SE, R&D Systems), granzyme B (1865-SE, R&D Systems), meprin A (4007-ZN, R&D Systems), meprin B (3300-ZN, R&D Systems), and neutrophil elastase (4517-SE, R&D Systems).

    Techniques: Immunofluorescence, Staining, Expressing, Activity Assay, Zymography, Sequencing, Binding Assay, Comparison

    Fig. 2 Neutrophil infiltration and NETs release within AAA lesions. A IF staining for neutrophil marker (Ly6G) was performed on tissue sections of the mouse abdominal aorta. B Hyalinization and IF labeling of the whole abdominal aorta and 3D tissue imaging were acquired with light-sheet microscopy. C–E Quantification of NETs markers (ELANE and MPO) in mouse abdominal aorta by western blotting (n = 3). **P < 0.01, ****P < 0.0001, indicating statistical significance between the two groups.

    Journal: Cell death discovery

    Article Title: Highly sensitive magnetic particle imaging of abdominal aortic aneurysm NETosis with anti-Ly6G iron oxide nanoparticles.

    doi: 10.1038/s41420-024-02156-3

    Figure Lengend Snippet: Fig. 2 Neutrophil infiltration and NETs release within AAA lesions. A IF staining for neutrophil marker (Ly6G) was performed on tissue sections of the mouse abdominal aorta. B Hyalinization and IF labeling of the whole abdominal aorta and 3D tissue imaging were acquired with light-sheet microscopy. C–E Quantification of NETs markers (ELANE and MPO) in mouse abdominal aorta by western blotting (n = 3). **P < 0.01, ****P < 0.0001, indicating statistical significance between the two groups.

    Article Snippet: Protein expression was detected using primary antibodies against ELANE (Boster Biotech, Wuhan, China), MPO (Proteintech, Wuhan, China) and GAPDH (Servicebio, Wuhan, China).

    Techniques: Staining, Marker, Labeling, Imaging, Microscopy, Western Blot

    Evaluation of the HNE substrate sensor using rmNE and rhNE. A ) Representative MALDI-TOF mass spectra of the sensor and the cleavage products with different time points of reaction using rmNE. B ) The ratio of cleavage products to the sensor with different time points. C ) Specificity testing using a blank control, 15 µM of rhNE, 15 µM of cathepsin G (CTSG), and 15 µM of PR3. D ) LOD test at 37 °C for 24 h using different concentrations of rhNE.

    Journal: PNAS Nexus

    Article Title: A breath-based in vitro diagnostic assay for the detection of lower respiratory tract infections

    doi: 10.1093/pnasnexus/pgae350

    Figure Lengend Snippet: Evaluation of the HNE substrate sensor using rmNE and rhNE. A ) Representative MALDI-TOF mass spectra of the sensor and the cleavage products with different time points of reaction using rmNE. B ) The ratio of cleavage products to the sensor with different time points. C ) Specificity testing using a blank control, 15 µM of rhNE, 15 µM of cathepsin G (CTSG), and 15 µM of PR3. D ) LOD test at 37 °C for 24 h using different concentrations of rhNE.

    Article Snippet: Recombinant mouse neutrophil elastase (rmNE) (Catalog # 4517-SE), recombinant human neutrophil elastase (rhNE) (Catalog # 9167-SE), and recombinant mouse active cathepsin C/DPPI (rmCatC, Catalog # 2336-CY) were purchased from R&D Systems (Minneapolis, MN).

    Techniques: Control