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mmp2  (R&D Systems)


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    Structured Review

    R&D Systems mmp2
    Mmp2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 96 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+mmp2/Recombinant+Human+MMP-2+Protein%2C+CF/us12589164-2402-28-26
    Average 95 stars, based on 96 article reviews
    mmp2 - by Bioz Stars, 2026-09
    95/100 stars

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    Related Articles

    Recombinant:

    Article Title: Utility of Glycosylated TIMP3 molecules: Inhibition of MMPs and TACE to improve cardiac function in rat myocardial infarct model
    Article Snippet: For tissues, cardiac LV tissues were homogenized in RIPA Buffer Solution (Teknova, Hollister, CA) supplemented with PMSF. .. Tissue lysate (50 μg) or recombinant human MMP2, or MMP9 (10 ng, R&D Systems, Minneapolis, MN) was loaded per lane onto Novex 10% Zymogram Plus (Gelatin) Protein Gel (Thermo Fisher Scientific, Waltham, MA). .. After electrophoresis, gels were incubated with Novex Renaturing buffer (Thermo Fisher Scientific).

    Article Title: Dual Functionalized Liposomes for Selective Delivery of Poorly Soluble Drugs to Inflamed Brain Regions
    Article Snippet: .. Recombinant human MMP2 (rhMMP2, R&D system, Minneapolis, MN, USA) was diluted to 0.2 μg/mL in 200 μL assay buffer (50 mm Tris, 10 mM CaCl 2 , 150 mm NaCl, 0.05% ( w / v ) Brij 35, pH 7.5). ..

    Article Title: Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen
    Article Snippet: The blood cascade proteases α-Thrombin (HCT-0020), β-Thrombin (HCBT-0022), γ-Thrombin (HCGT-0021), Factor VIIa (HCVIIA-0031), IXa (HCIXA-0050), Xa (HCXA-0060), XIa (HCXIA-0160), Plasmin (HCPM-0140) and activated Protein C (HCAPC-0080) were purchased from Hematologic Technologies, Inc., (USA). .. Recombinant human MMP2 (902-MP-010) and recombinant West Nile Virus NS3 Protease Protein (2907-SE) were purchased from R&D systems (USA). .. Recombinant human MMP3 (SRP7783) was purchased from Sigma Aldrich (Germany).

    Article Title: Co-delivery of TRAIL and siHSP70 using hierarchically modular assembly formulations achieves enhanced TRAIL-resistant cancer therapy.
    Article Snippet: The combined therapy of tumor necrosis factor-related apoptosisinducing ligand (TRAIL) and heat shock protein 70-targeting siRNA (siHSP70) has shown an improved anti-tumor effect on TRAIL-resistant tumor.. However, vehicles to co-deliver these two biopharmaceuticals are challenging because of the distinct location of their targets on the cell surface and in the cytosol.. Here we developed a hierarchically modular assembly formulation (TH-s-RSC) via the copperfree click reaction to co-encapsulate the positively-charged TRAIL and negatively-charged siHSP70 and release them in the extracellular space and cytoplasm.

    Article Title: Dual Functionalized Liposomes for Selective Delivery of Poorly Soluble Drugs to Inflamed Brain Regions
    Article Snippet: .. Briefly, recombinant human MMP2 or MMP9 (R&D Systems) were activated using AMPA (amino-phenylmercuric acetate) following manufacturer’s instructions. ..

    Article Title: Intermittent Hypoxia Mediates Paraspeckle Protein-1 Upregulation in Sleep Apnea
    Article Snippet: Antibody binding was detected by ECL Western Blotting Detection Reagent (Amersham-Pharmacia-Biotech, Amersham, UK). .. Recombinant human MMP2 (R&D Systems) and PSPC1 were dissolved in 20-mM Tris buffer containing 2-mM CaCl 2 and 1-mM MgCl 2 (pH 7.3), at a concentration of 10 μg/100 L and 100 μg/100 μL, respectively. ..

    Article Title: Intermittent Hypoxia Mediates Paraspeckle Protein-1 Upregulation in Sleep Apnea.
    Article Snippet: .. Recombinant human MMP2 (R&D Systems) and PSPC1 were dissolved in 20-mM Tris buffer containing 2-mM CaCl2 and 1-mM MgCl2 (pH 7.3), at a concentration of 10 μg/100 L and 100 μg/100 μL, respectively. ..

    Article Title: Utility of Glycosylated TIMP3 molecules: Inhibition of MMPs and TACE to improve cardiac function in rat myocardial infarct model.
    Article Snippet: For tissues, cardiac LV tissues were homogenized in RIPA Buffer Solution (Teknova, Hollister, CA) supplemented with PMSF. .. Tissue lysate (50 μg) or recombinant human MMP2, or MMP9 (10 ng, R&D Systems, Minneapolis, MN) was loaded per lane onto Novex 10% Zymogram Plus (Gelatin) Protein Gel (Thermo Fisher Scientific, Waltham, MA). .. After electrophoresis, gels were incubated with Novex Renaturing buffer (Thermo Fisher Scientific).

    Virus:

    Article Title: Mapping specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen
    Article Snippet: The blood cascade proteases α-Thrombin (HCT-0020), β-Thrombin (HCBT-0022), γ-Thrombin (HCGT-0021), Factor VIIa (HCVIIA-0031), IXa (HCIXA-0050), Xa (HCXA-0060), XIa (HCXIA-0160), Plasmin (HCPM-0140) and activated Protein C (HCAPC-0080) were purchased from Hematologic Technologies, Inc., (USA). .. Recombinant human MMP2 (902-MP-010) and recombinant West Nile Virus NS3 Protease Protein (2907-SE) were purchased from R&D systems (USA). .. Recombinant human MMP3 (SRP7783) was purchased from Sigma Aldrich (Germany).

    Concentration Assay:

    Article Title: Intermittent Hypoxia Mediates Paraspeckle Protein-1 Upregulation in Sleep Apnea
    Article Snippet: Antibody binding was detected by ECL Western Blotting Detection Reagent (Amersham-Pharmacia-Biotech, Amersham, UK). .. Recombinant human MMP2 (R&D Systems) and PSPC1 were dissolved in 20-mM Tris buffer containing 2-mM CaCl 2 and 1-mM MgCl 2 (pH 7.3), at a concentration of 10 μg/100 L and 100 μg/100 μL, respectively. ..

    Article Title: Intermittent Hypoxia Mediates Paraspeckle Protein-1 Upregulation in Sleep Apnea.
    Article Snippet: .. Recombinant human MMP2 (R&D Systems) and PSPC1 were dissolved in 20-mM Tris buffer containing 2-mM CaCl2 and 1-mM MgCl2 (pH 7.3), at a concentration of 10 μg/100 L and 100 μg/100 μL, respectively. ..



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    Sino Biological proteases recombinant human mmp2
    Proteases Recombinant Human Mmp2, supplied by Sino Biological, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    R&D Systems pro mmp2
    Nisin inhibits T. denticola <t>-induced-MMP2</t> activation in PDL cells. ( a ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to wild-type T. denticola (35405) (50 MOI) for 2 h, washed three times with PBS, followed by treatment with nisin (100 µg/mL) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( b <t>),</t> <t>Pro-MMP2</t> (c), active MMP2 (d) and dentilisin/PrtP (e). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 1a.
    Pro Mmp2, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Nisin inhibits T. denticola <t>-induced-MMP2</t> activation in PDL cells. ( a ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to wild-type T. denticola (35405) (50 MOI) for 2 h, washed three times with PBS, followed by treatment with nisin (100 µg/mL) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( b <t>),</t> <t>Pro-MMP2</t> (c), active MMP2 (d) and dentilisin/PrtP (e). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 1a.
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    R&D Systems recombinant human mmp2 protein
    (A) Protein estimation of neutrophil cell secretome. Protein estimation of cell secretome obtained from HL60 cells, differentiated into neutrophils was carried out using ‘Bradford reagent’ as per protocol described by the manufacturer. Total protein content in secretome of HL60 cells differentiated neutrophil cell control and cells exposed to NS1 antigen and varying concentrations of atorvastatin. (B) <t>MMP-2</t> estimation by ELISA in neutrophils’ secretome (culture medium harvested from NS1-treated neutrophils).
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    Sino Biological recombinant human mmp2
    Engineering and characterization of E. coli Nissle 1917 to express TME-responsive IL-15 (A) A <t>recombinant</t> plasmid (pNeae2) encoding conditionally released IL-15 protein was introduced into E. coli Nissle 1917 (EcN) and expressed on the bacterial outer membrane. (B and C) The expression of HA-tagged IL-15 in EcN-IL-15 was analyzed by flow cytometry and western blot. (D) Western blot analysis of the cleavage of EcN-IL-15 by recombinant proteases. (E–G) The isolated mouse splenocytes were labeled with CFSE and stimulated for 72 h with supernatant from <t>MMP2</t> cleavage of EcN or EcN-IL-15, followed by flow cytometry analysis and CCK8 assay ( n = 3). (H–J) EcN-IL-15 strains delayed tumor progression in vivo ( n = 4). (H) Treatment schedule of EcN-IL-15 in subcutaneous MC38 tumor. (I) MC38 tumor growth curves with different treatments (means ± SD). (J) Kaplan-Meier survival curves. (K) EcN-IL-15 reshapes the TME and boosts anti-tumor immune responses. Quantification of CD3 + T cells, CD4 + T cells, CD8 + T cells, NK cells, DCs, and macrophages in MC38 tumor tissues; n = 4 biological replicates. Data are presented as means ± SEM unless otherwise specified. p values were analyzed by one-way analysis of variance (ANOVA) with Tukey’s multiple comparisons test (G, K), two-way ANOVA with Tukey’s multiple comparisons test (I), or Mantel-Cox log rank test (J). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001; ns, not significant.
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    Image Search Results


    Nisin inhibits T. denticola -induced-MMP2 activation in PDL cells. ( a ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to wild-type T. denticola (35405) (50 MOI) for 2 h, washed three times with PBS, followed by treatment with nisin (100 µg/mL) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( b ), Pro-MMP2 (c), active MMP2 (d) and dentilisin/PrtP (e). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 1a.

    Journal: Scientific Reports

    Article Title: Nisin bacteriocin blocks T. denticola -triggered MMP2 activation and pathogen internalization via TLR2

    doi: 10.1038/s41598-026-43673-8

    Figure Lengend Snippet: Nisin inhibits T. denticola -induced-MMP2 activation in PDL cells. ( a ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to wild-type T. denticola (35405) (50 MOI) for 2 h, washed three times with PBS, followed by treatment with nisin (100 µg/mL) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( b ), Pro-MMP2 (c), active MMP2 (d) and dentilisin/PrtP (e). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 1a.

    Article Snippet: For in vitro MMP2 activation, different concentrations of purified dentilisin/PrtP (20, 40 or 80 ng) , and pro-MMP2 (20 ng) (Cat #902-MP-010; R&D Systems, Minneapolis, MN) diluted in reaction buffer (TCNB, 50 mM Tris, 10 mM CaCl 2 , 150 mM NaCl, 0.05% (w/v) Brij 35, pH 7.5) were mixed and incubated for 30 min at room temperature, then mixed with 4X sample buffer (Cat #1610747, Bio-Rad, Hercules, CA) and loaded onto 10% gelatin-containing SDS-PAGE gels (Cat #ZY00100BOX, Thermo Fisher scientific, Novex TM 10% zymogram plus (Gelatin) protein gels).

    Techniques: Activation Assay, Zymography

    T. denticola purified dentilisin/PrtP directly activates recombinant MMP2 in vitro, and nisin attenuates this activation. ( a ) Representative gelatin zymogram of recombinant Pro-MMP2 (20 ng) incubated with increasing concentrations of purified dentilisin/PrtP (20, 40, or 80 ng) in the presence or absence of nisin (20, 40, or 80 µg). Quantitative analysis of band intensities for total MMP2 ( b ), Pro-MMP2 ( c ), active MMP2 ( d ) and dentilisin/PrtP ( e ). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 2a.

    Journal: Scientific Reports

    Article Title: Nisin bacteriocin blocks T. denticola -triggered MMP2 activation and pathogen internalization via TLR2

    doi: 10.1038/s41598-026-43673-8

    Figure Lengend Snippet: T. denticola purified dentilisin/PrtP directly activates recombinant MMP2 in vitro, and nisin attenuates this activation. ( a ) Representative gelatin zymogram of recombinant Pro-MMP2 (20 ng) incubated with increasing concentrations of purified dentilisin/PrtP (20, 40, or 80 ng) in the presence or absence of nisin (20, 40, or 80 µg). Quantitative analysis of band intensities for total MMP2 ( b ), Pro-MMP2 ( c ), active MMP2 ( d ) and dentilisin/PrtP ( e ). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 2a.

    Article Snippet: For in vitro MMP2 activation, different concentrations of purified dentilisin/PrtP (20, 40 or 80 ng) , and pro-MMP2 (20 ng) (Cat #902-MP-010; R&D Systems, Minneapolis, MN) diluted in reaction buffer (TCNB, 50 mM Tris, 10 mM CaCl 2 , 150 mM NaCl, 0.05% (w/v) Brij 35, pH 7.5) were mixed and incubated for 30 min at room temperature, then mixed with 4X sample buffer (Cat #1610747, Bio-Rad, Hercules, CA) and loaded onto 10% gelatin-containing SDS-PAGE gels (Cat #ZY00100BOX, Thermo Fisher scientific, Novex TM 10% zymogram plus (Gelatin) protein gels).

    Techniques: Purification, Recombinant, In Vitro, Activation Assay, Incubation

    Dentilisin/PrtP-deficient T. denticola does not activate MMP2 and is unaffected by nisin in PDL cells. ( a ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to purified dentilisin/PrtP (50 ng/ml), wild-type T. denticola (WT) (35405) (50 MOI) or mutant T. denticola (MT) (50 MOI) for 2 h and treated with nisin (100 µg/ml) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( b ), Pro-MMP2 ( c ), active MMP2 ( d ) and dentilisin/PrtP ( e ). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 3a.

    Journal: Scientific Reports

    Article Title: Nisin bacteriocin blocks T. denticola -triggered MMP2 activation and pathogen internalization via TLR2

    doi: 10.1038/s41598-026-43673-8

    Figure Lengend Snippet: Dentilisin/PrtP-deficient T. denticola does not activate MMP2 and is unaffected by nisin in PDL cells. ( a ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to purified dentilisin/PrtP (50 ng/ml), wild-type T. denticola (WT) (35405) (50 MOI) or mutant T. denticola (MT) (50 MOI) for 2 h and treated with nisin (100 µg/ml) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( b ), Pro-MMP2 ( c ), active MMP2 ( d ) and dentilisin/PrtP ( e ). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped gel image is presented in Supplementary Information as Fig. 3a.

    Article Snippet: For in vitro MMP2 activation, different concentrations of purified dentilisin/PrtP (20, 40 or 80 ng) , and pro-MMP2 (20 ng) (Cat #902-MP-010; R&D Systems, Minneapolis, MN) diluted in reaction buffer (TCNB, 50 mM Tris, 10 mM CaCl 2 , 150 mM NaCl, 0.05% (w/v) Brij 35, pH 7.5) were mixed and incubated for 30 min at room temperature, then mixed with 4X sample buffer (Cat #1610747, Bio-Rad, Hercules, CA) and loaded onto 10% gelatin-containing SDS-PAGE gels (Cat #ZY00100BOX, Thermo Fisher scientific, Novex TM 10% zymogram plus (Gelatin) protein gels).

    Techniques: Purification, Mutagenesis, Zymography

    T. denticola -triggered activation of MMP2 and nisin effects are mediated via TLR2 in PDL cells. PDL cells were transduced with TLR2 shRNA or scramble shRNA lentiviral particles in serum-free media, then selected in puromycin. ( a ) Immunoblot showing TLR2 protein levels in cells transduced with scramble shRNA or TLR2 shRNA lentiviral particles. ( b ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to wild-type T. denticola (35405) (50 MOI) for 2 h, washed three times with PBS, treated with gentamicin (50 µg/ml) for 1 h, washed three times again with PBS, and then treated with nisin (100 µg/ml) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( c ), Pro-MMP2 ( d ), active MMP2 ( e ) and dentilisin/PrtP ( f ). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped blot and gel images are presented in Supplementary Information as Figs. 4a and b.

    Journal: Scientific Reports

    Article Title: Nisin bacteriocin blocks T. denticola -triggered MMP2 activation and pathogen internalization via TLR2

    doi: 10.1038/s41598-026-43673-8

    Figure Lengend Snippet: T. denticola -triggered activation of MMP2 and nisin effects are mediated via TLR2 in PDL cells. PDL cells were transduced with TLR2 shRNA or scramble shRNA lentiviral particles in serum-free media, then selected in puromycin. ( a ) Immunoblot showing TLR2 protein levels in cells transduced with scramble shRNA or TLR2 shRNA lentiviral particles. ( b ) Representative gelatin zymogram showing MMP2 levels in PDL cells exposed to wild-type T. denticola (35405) (50 MOI) for 2 h, washed three times with PBS, treated with gentamicin (50 µg/ml) for 1 h, washed three times again with PBS, and then treated with nisin (100 µg/ml) for 24 h. Conditioned media were analyzed by gelatin zymography. Quantitative analysis of band intensities for total MMP2 ( c ), Pro-MMP2 ( d ), active MMP2 ( e ) and dentilisin/PrtP ( f ). Data are representative of at least three independent experiments. Intergroup differences were analyzed by the analysis of variance (ANOVA) and Tukey’s post hoc test. * p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001. The uncropped blot and gel images are presented in Supplementary Information as Figs. 4a and b.

    Article Snippet: For in vitro MMP2 activation, different concentrations of purified dentilisin/PrtP (20, 40 or 80 ng) , and pro-MMP2 (20 ng) (Cat #902-MP-010; R&D Systems, Minneapolis, MN) diluted in reaction buffer (TCNB, 50 mM Tris, 10 mM CaCl 2 , 150 mM NaCl, 0.05% (w/v) Brij 35, pH 7.5) were mixed and incubated for 30 min at room temperature, then mixed with 4X sample buffer (Cat #1610747, Bio-Rad, Hercules, CA) and loaded onto 10% gelatin-containing SDS-PAGE gels (Cat #ZY00100BOX, Thermo Fisher scientific, Novex TM 10% zymogram plus (Gelatin) protein gels).

    Techniques: Activation Assay, Transduction, shRNA, Western Blot, Zymography

    (A) Protein estimation of neutrophil cell secretome. Protein estimation of cell secretome obtained from HL60 cells, differentiated into neutrophils was carried out using ‘Bradford reagent’ as per protocol described by the manufacturer. Total protein content in secretome of HL60 cells differentiated neutrophil cell control and cells exposed to NS1 antigen and varying concentrations of atorvastatin. (B) MMP-2 estimation by ELISA in neutrophils’ secretome (culture medium harvested from NS1-treated neutrophils).

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Elucidation of neutrophils-mediated effect of MMP-2 on lung epithelial cells; implications for acute respiratory distress syndrome and severe dengue pathogenesis

    doi: 10.3389/fcimb.2025.1670259

    Figure Lengend Snippet: (A) Protein estimation of neutrophil cell secretome. Protein estimation of cell secretome obtained from HL60 cells, differentiated into neutrophils was carried out using ‘Bradford reagent’ as per protocol described by the manufacturer. Total protein content in secretome of HL60 cells differentiated neutrophil cell control and cells exposed to NS1 antigen and varying concentrations of atorvastatin. (B) MMP-2 estimation by ELISA in neutrophils’ secretome (culture medium harvested from NS1-treated neutrophils).

    Article Snippet: Recombinant human MMP2 protein was procured from R & D Systems.

    Techniques: Control, Enzyme-linked Immunosorbent Assay

    Expression profile of apoptotic genes in epithelial cells treated with varying concentrations of MMP-2. Histogram represents the fold change of gene upon normalization with GAPDH. Histograms represents the fold change genes upon normalization with GAPDH. * p < 0.05, ** p < 0.01, *** p < 0.001, compared with control. (A) Histogram represents the fold change of relative Caspase-3 expression in A549 cells stimulated with different concentrations of MMP-2 (1, 10, and 100 ng/ml), compared with the non-stimulated control. p < 0.01 compared with control. (B) Histogram represents the fold change of relative Bad expression in A549 cells treated with MMP-2 (1, 10, and 100 ng/ml), compared with the control. **p < 0.01 and p < 0.001 compared with control. (C) Histogram represents the fold change of relative BAX expression in A549 cells treated with MMP-2 (10 and 100 ng/ml), compared with control. p < 0.05 compared with control. (D) Histogram represents the fold change of relative Caspase-6 expression in A549 cells exposed to MMP-2 (100 ng/ml), compared with the non-stimulated control. p < 0.001 compared with control. (E) Histogram represents the fold change of relative DAPK-1 expression in A549 cells treated with MMP-2 (1 and 10 ng/ml), compared with the non-stimulated control. p < 0.05 compared with control.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Elucidation of neutrophils-mediated effect of MMP-2 on lung epithelial cells; implications for acute respiratory distress syndrome and severe dengue pathogenesis

    doi: 10.3389/fcimb.2025.1670259

    Figure Lengend Snippet: Expression profile of apoptotic genes in epithelial cells treated with varying concentrations of MMP-2. Histogram represents the fold change of gene upon normalization with GAPDH. Histograms represents the fold change genes upon normalization with GAPDH. * p < 0.05, ** p < 0.01, *** p < 0.001, compared with control. (A) Histogram represents the fold change of relative Caspase-3 expression in A549 cells stimulated with different concentrations of MMP-2 (1, 10, and 100 ng/ml), compared with the non-stimulated control. p < 0.01 compared with control. (B) Histogram represents the fold change of relative Bad expression in A549 cells treated with MMP-2 (1, 10, and 100 ng/ml), compared with the control. **p < 0.01 and p < 0.001 compared with control. (C) Histogram represents the fold change of relative BAX expression in A549 cells treated with MMP-2 (10 and 100 ng/ml), compared with control. p < 0.05 compared with control. (D) Histogram represents the fold change of relative Caspase-6 expression in A549 cells exposed to MMP-2 (100 ng/ml), compared with the non-stimulated control. p < 0.001 compared with control. (E) Histogram represents the fold change of relative DAPK-1 expression in A549 cells treated with MMP-2 (1 and 10 ng/ml), compared with the non-stimulated control. p < 0.05 compared with control.

    Article Snippet: Recombinant human MMP2 protein was procured from R & D Systems.

    Techniques: Expressing, Control

    Experiment with Balb/c mice using NS1 alone and in combination with atorvastatin. (A) Diagrammatic representation of treatment plan for mice for NS1 antigen alone and in combination with atorvastatin. (B) Histogram represents the fold change of relative MMP-2 expression profile in mice blood exposed after the treatment with NS1 and atorvastatin. # p < 0.05, compared with control and ** p < 0.001, compared with NS1-treated group. (C) Immunohistochemistry of the NS1-treated mice alone and in combination with atorvastatin. Upper panel shows the H&E staining and the lower panel shoes the CD31, also known as platelet endothelial cell adhesion molecule 1 (PECAM-1) expressed on leukocytes. The figure used here is one of the representative out of three independent experiments performed at least in duplicate.

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: Elucidation of neutrophils-mediated effect of MMP-2 on lung epithelial cells; implications for acute respiratory distress syndrome and severe dengue pathogenesis

    doi: 10.3389/fcimb.2025.1670259

    Figure Lengend Snippet: Experiment with Balb/c mice using NS1 alone and in combination with atorvastatin. (A) Diagrammatic representation of treatment plan for mice for NS1 antigen alone and in combination with atorvastatin. (B) Histogram represents the fold change of relative MMP-2 expression profile in mice blood exposed after the treatment with NS1 and atorvastatin. # p < 0.05, compared with control and ** p < 0.001, compared with NS1-treated group. (C) Immunohistochemistry of the NS1-treated mice alone and in combination with atorvastatin. Upper panel shows the H&E staining and the lower panel shoes the CD31, also known as platelet endothelial cell adhesion molecule 1 (PECAM-1) expressed on leukocytes. The figure used here is one of the representative out of three independent experiments performed at least in duplicate.

    Article Snippet: Recombinant human MMP2 protein was procured from R & D Systems.

    Techniques: Expressing, Control, Immunohistochemistry, Staining

    Engineering and characterization of E. coli Nissle 1917 to express TME-responsive IL-15 (A) A recombinant plasmid (pNeae2) encoding conditionally released IL-15 protein was introduced into E. coli Nissle 1917 (EcN) and expressed on the bacterial outer membrane. (B and C) The expression of HA-tagged IL-15 in EcN-IL-15 was analyzed by flow cytometry and western blot. (D) Western blot analysis of the cleavage of EcN-IL-15 by recombinant proteases. (E–G) The isolated mouse splenocytes were labeled with CFSE and stimulated for 72 h with supernatant from MMP2 cleavage of EcN or EcN-IL-15, followed by flow cytometry analysis and CCK8 assay ( n = 3). (H–J) EcN-IL-15 strains delayed tumor progression in vivo ( n = 4). (H) Treatment schedule of EcN-IL-15 in subcutaneous MC38 tumor. (I) MC38 tumor growth curves with different treatments (means ± SD). (J) Kaplan-Meier survival curves. (K) EcN-IL-15 reshapes the TME and boosts anti-tumor immune responses. Quantification of CD3 + T cells, CD4 + T cells, CD8 + T cells, NK cells, DCs, and macrophages in MC38 tumor tissues; n = 4 biological replicates. Data are presented as means ± SEM unless otherwise specified. p values were analyzed by one-way analysis of variance (ANOVA) with Tukey’s multiple comparisons test (G, K), two-way ANOVA with Tukey’s multiple comparisons test (I), or Mantel-Cox log rank test (J). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001; ns, not significant.

    Journal: Cell Reports Medicine

    Article Title: Probiotic-mediated tumor microenvironment reprogramming with protease-sensitive interleukin-15 and photothermal therapy

    doi: 10.1016/j.xcrm.2025.102191

    Figure Lengend Snippet: Engineering and characterization of E. coli Nissle 1917 to express TME-responsive IL-15 (A) A recombinant plasmid (pNeae2) encoding conditionally released IL-15 protein was introduced into E. coli Nissle 1917 (EcN) and expressed on the bacterial outer membrane. (B and C) The expression of HA-tagged IL-15 in EcN-IL-15 was analyzed by flow cytometry and western blot. (D) Western blot analysis of the cleavage of EcN-IL-15 by recombinant proteases. (E–G) The isolated mouse splenocytes were labeled with CFSE and stimulated for 72 h with supernatant from MMP2 cleavage of EcN or EcN-IL-15, followed by flow cytometry analysis and CCK8 assay ( n = 3). (H–J) EcN-IL-15 strains delayed tumor progression in vivo ( n = 4). (H) Treatment schedule of EcN-IL-15 in subcutaneous MC38 tumor. (I) MC38 tumor growth curves with different treatments (means ± SD). (J) Kaplan-Meier survival curves. (K) EcN-IL-15 reshapes the TME and boosts anti-tumor immune responses. Quantification of CD3 + T cells, CD4 + T cells, CD8 + T cells, NK cells, DCs, and macrophages in MC38 tumor tissues; n = 4 biological replicates. Data are presented as means ± SEM unless otherwise specified. p values were analyzed by one-way analysis of variance (ANOVA) with Tukey’s multiple comparisons test (G, K), two-way ANOVA with Tukey’s multiple comparisons test (I), or Mantel-Cox log rank test (J). ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001; ns, not significant.

    Article Snippet: Recombinant human MMP2, MMP9, and uPA were purchased from Sino Biological.

    Techniques: Recombinant, Plasmid Preparation, Membrane, Expressing, Flow Cytometry, Western Blot, Isolation, Labeling, CCK-8 Assay, In Vivo