|
Elabscience Biotechnology
kits for mmp2 Kits For Mmp2, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/Rat+MMP-2+(Matrix+Metalloproteinase+2)+ELISA+Kit/pm41789623-96-4-17 Average 94 stars, based on 1 article reviews
kits for mmp2 - by Bioz Stars,
2026-11
94/100 stars
|
Buy from Supplier |
|
Elabscience Biotechnology
immunosorbent assay elisa ![]() Immunosorbent Assay Elisa, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/Human+MMP-2+(Matrix+Metalloproteinase+2)+ELISA+Kit/pmc12153419-107-23-26 Average 93 stars, based on 1 article reviews
immunosorbent assay elisa - by Bioz Stars,
2026-11
93/100 stars
|
Buy from Supplier |
|
Proteintech
mmp2 antibody ![]() Mmp2 Antibody, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/MMP2+Polyclonal+antibody/pmc12291489-60-41-61 Average 96 stars, based on 1 article reviews
mmp2 antibody - by Bioz Stars,
2026-11
96/100 stars
|
Buy from Supplier |
|
Proteintech
mmp2 ![]() Mmp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/MMP2+Antibody/pmc12712735-77-15-26 Average 96 stars, based on 1 article reviews
mmp2 - by Bioz Stars,
2026-11
96/100 stars
|
Buy from Supplier |
|
Proteintech
mmp 7 ![]() Mmp 7, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/MMP7+Antibody/pm35551975-86-8-24 Average 95 stars, based on 1 article reviews
mmp 7 - by Bioz Stars,
2026-11
95/100 stars
|
Buy from Supplier |
|
Proteintech
anti mmp9 ![]() Anti Mmp9, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/MMP9+(N-terminal)+Polyclonal+antibody/pmc13015019-220-43-63 Average 96 stars, based on 1 article reviews
anti mmp9 - by Bioz Stars,
2026-11
96/100 stars
|
Buy from Supplier |
|
Proteintech
mmp1 ![]() Mmp1, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/MMP1+Antibody/pm37403876-245-20-24 Average 96 stars, based on 1 article reviews
mmp1 - by Bioz Stars,
2026-11
96/100 stars
|
Buy from Supplier |
|
Cusabio
mmp 9 ![]() Mmp 9, supplied by Cusabio, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/Rat+matrix+metalloproteinase+2%2FGelatinase+A%2CMMP-2+ELISA+kit/pmc09805095-23-9-33 Average 93 stars, based on 1 article reviews
mmp 9 - by Bioz Stars,
2026-11
93/100 stars
|
Buy from Supplier |
|
Elabscience Biotechnology
mmp2 ![]() Mmp2, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/Mouse+MMP-2+(Matrix+Metalloproteinase+2)+ELISA+Kit/pmc13052030-123-7-9 Average 94 stars, based on 1 article reviews
mmp2 - by Bioz Stars,
2026-11
94/100 stars
|
Buy from Supplier |
|
RayBiotech inc
matrix metalloproteinase 9 ![]() Matrix Metalloproteinase 9, supplied by RayBiotech inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/Matrix+Metalloproteinase-9+Rabbit+Recombinant/pm37369969-88-0-22 Average 91 stars, based on 1 article reviews
matrix metalloproteinase 9 - by Bioz Stars,
2026-11
91/100 stars
|
Buy from Supplier |
|
Boster Bio
mmp9 ![]() Mmp9, supplied by Boster Bio, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/Anti-MMP-9+Antibody/pm41645531-133-43-44 Average 94 stars, based on 1 article reviews
mmp9 - by Bioz Stars,
2026-11
94/100 stars
|
Buy from Supplier |
|
MedChemExpress
mmp 2 ![]() Mmp 2, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/matrix+metalloproteinases-2/MMP-2%2C+Human/pmc11726454-309-0-2 Average 93 stars, based on 1 article reviews
mmp 2 - by Bioz Stars,
2026-11
93/100 stars
|
Buy from Supplier |
Image Search Results
Journal: Lasers in Surgery and Medicine
Article Title: Effects of Nonablative Er‐ YAG Laser on Human Endometrial Stromal Cells (hESCs): A Pilot Study
doi: 10.1002/lsm.70020
Figure Lengend Snippet: The boxplots of the MMP‐2 levels in the cultured media of human endometrial stromal cells (hESCs). Confluent hESC cultures were treated with E 2 (10 −8 M) (group E 2 ), E 2 (10 −8 M)+ ethanol (0.1%) (group E 2 + S), E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 ), Er‐YAG laser + E 2 (10 −8 M) (group E 2 + L), Er‐YAG laser+ E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 + L) for 12, 24, 48, and 72 h. Only hESCs (incubated in serum‐free DMEM/F12) and hESCs + Er‐YAG laser (hESCs + L) groups were incubated for 12 and 72 h. MMP‐2 levels were quantified by ELISA in culture media and normalized to total cell protein ( n = 3, median (Q1–Q3). DMEM, Dulbecco modified Eagle medium; E 2 , estradiol; ELISA, enzyme‐linked immunosorbent assay; Er‐YAG, nonablative Erbium YAG; ESC, endometrial stromal cell; MMP‐2, matrix metalloproteinase‐2; P 4 , progesterone.
Article Snippet: To evaluate the remodeling effect of Er‐YAG laser on endometrial tissue, matrix metalloproteinase‐2 (MMP‐2) levels in conditioned media were measured by an enzyme‐linked
Techniques: Cell Culture, Incubation, Enzyme-linked Immunosorbent Assay, Modification
Journal: Lasers in Surgery and Medicine
Article Title: Effects of Nonablative Er‐ YAG Laser on Human Endometrial Stromal Cells (hESCs): A Pilot Study
doi: 10.1002/lsm.70020
Figure Lengend Snippet: The boxplots of the TNF‐α and IL‐6 levels in the cultured media of human endometrial stromal cells (hESCs). Confluent hESC cultures were treated with E 2 (10 −8 M) (group E 2 ), E 2 (10 −8 M) + ethanol (0.1%) (group E 2 + S), E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 ), Er‐YAG laser + E 2 (10 −8 M) (group E 2 + L), Er‐YAG laser+ E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 + L) for 12, 24, 48, and 72 h. Only hESCs (incubated in serum‐free DMEM/F12) and hESCs + Er‐YAG laser (hESCs + L) groups were incubated for 12 and 72 h. (A) represents subsequent time points for TNF‐α analysis, and (B) represents subsequent time points for IL‐6 analysis. TNF‐α and IL‐6 levels were quantified by ELISA in culture media and normalized to total cell protein ( n = 3, median (Q1–Q3). DMEM, Dulbecco modified Eagle medium; E 2 , estradiol; ELISA, enzyme‐linked immunosorbent assay; Er‐YAG, nonablative Erbium YAG; ESC, endometrial stromal cell; IL‐6: interleukin‐6; MMP‐2, matrix metalloproteinase‐2; P 4 , progesterone; TNF‐α, tumor necrosis factor‐alpha.
Article Snippet: To evaluate the remodeling effect of Er‐YAG laser on endometrial tissue, matrix metalloproteinase‐2 (MMP‐2) levels in conditioned media were measured by an enzyme‐linked
Techniques: Cell Culture, Incubation, Enzyme-linked Immunosorbent Assay, Modification
Journal: Lasers in Surgery and Medicine
Article Title: Effects of Nonablative Er‐ YAG Laser on Human Endometrial Stromal Cells (hESCs): A Pilot Study
doi: 10.1002/lsm.70020
Figure Lengend Snippet: The boxplots of the VEGF‐A levels in the cultured media of human endometrial stromal cells (hESCs). Confluent hESC cultures were treated with E 2 (10 −8 M) (group E 2 ), E 2 (10 −8 M)+ ethanol (0.1%) (group E 2 + S), E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 ), Er‐YAG laser + E 2 (10 −8 M) (group E 2 + L), Er‐YAG laser+ E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 + L) for 12, 24, 48, and 72 h. Only hESCs (incubated in serum‐free DMEM/F12) and hESCs + Er‐YAG laser (hESCs + L) groups were incubated for 12 and 72 h. VEGF‐A levels were quantified by ELISA in culture media and normalized to total cell protein ( n = 3, median (Q1–Q3). DMEM, Dulbecco modified Eagle medium; E 2 , estradiol; ELISA, enzyme‐linked immunosorbent assay; Er‐YAG, nonablative Erbium YAG; ESC, endometrial stromal cell; P 4 , progesterone; VEGF‐A, vascular endothelial growth factor‐A.
Article Snippet: To evaluate the remodeling effect of Er‐YAG laser on endometrial tissue, matrix metalloproteinase‐2 (MMP‐2) levels in conditioned media were measured by an enzyme‐linked
Techniques: Cell Culture, Incubation, Enzyme-linked Immunosorbent Assay, Modification
Journal: Lasers in Surgery and Medicine
Article Title: Effects of Nonablative Er‐ YAG Laser on Human Endometrial Stromal Cells (hESCs): A Pilot Study
doi: 10.1002/lsm.70020
Figure Lengend Snippet: The boxplots of the IGFBP‐1 secretions in the cultured media of human endometrial stromal cells (hESCs). Confluent hESC cultures were treated with E 2 (10 −8 M) (group E 2 ), E 2 (10 −8 M) + ethanol (0.1%) (group E 2 + S), E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 ), Er‐YAG laser+ E 2 (10 −8 M) (group E 2 + L), Er‐YAG laser + E 2 (10 −8 M) + P 4 (10 −7 M) (group E 2 + P 4 + L) for 12, 24, 48, and 72 h. Only hESCs (incubated in serum‐free DMEM/F12) and hESCs + Er‐YAG laser (hESCs + L) groups were incubated for 12 and 72 h. IGFBP‐1 levels were quantified by ELISA in culture media and normalized to total cell protein ( n = 3, median (Q1–Q3). DMEM, Dulbecco modified Eagle medium; E 2 , estradiol; ELISA, enzyme‐linked immunosorbent assay; Er‐YAG, nonablative Erbium YAG; ESC, endometrial stromal cell; IGFBP‐1, insulin‐like growth factor‐binding protein‐1; P 4 , progesterone.
Article Snippet: To evaluate the remodeling effect of Er‐YAG laser on endometrial tissue, matrix metalloproteinase‐2 (MMP‐2) levels in conditioned media were measured by an enzyme‐linked
Techniques: Cell Culture, Incubation, Enzyme-linked Immunosorbent Assay, Modification, Binding Assay
Journal: Clinical and Translational Medicine
Article Title: Hypoxia‐induced secretory autophagy in cancer‐associated fibroblasts promotes ECM remodelling through serglycin secretion in oral squamous cell carcinoma
doi: 10.1002/ctm2.70556
Figure Lengend Snippet: CAFs secrete SRGN via autophagy to promote OSCC cell invasion and migration by facilitating ECM remodelling through interaction with MMP2/9. (A, B) WB analysis of SRGN protein expression levels and quantification in WT CAFs and SRGN KO CAFs. (C) qPCR analysis of SRGN gene expression in WT CAFs and SRGN KO CAFs. (D) UV image of the agarose gel. (E) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with OSCC cells. Invasion ability was assessed by transwell assays. (F) Invasion cell numbers were quantified using ImageJ software. (* p < .05; ** p < .01; *** p < .001). (G) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with SCC9 cells. Migration ability was assessed by scratch assays. (H) Prediction of SRGN‐binding proteins using the STRING database. (I) HEK293T cells were transfected with SRGN‐Flag and incubated for 48 h. Cell lysates were incubated with anti‐Flag beads, and immunoblotting (IB) was performed using anti‐Flag, anti‐MMP11, anti‐MMP9, and anti‐MMP2 antibodies. (J) WB analysis of changes in MMP9, MMP11, MMP2, and SRGN protein expression levels in WT CAFs and SRGN KO CAFs. (K) Gelatin degradation assays were performed to evaluate gelatin degradation after 24 h of co‐culture of CAL27 cells with the supernatants from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs. Scale bar = 20 µm.
Article Snippet: Primary antibodies used in this assay included: β‐actin (1:4000, 20536‐1, Proteintech), MMP9 (1:1000, bs‐4593R, Bioss),
Techniques: Migration, Expressing, Gene Expression, Agarose Gel Electrophoresis, Cell Culture, Software, Binding Assay, Transfection, Incubation, Western Blot, Co-Culture Assay
Journal: Clinical and Translational Medicine
Article Title: Hypoxia‐induced secretory autophagy in cancer‐associated fibroblasts promotes ECM remodelling through serglycin secretion in oral squamous cell carcinoma
doi: 10.1002/ctm2.70556
Figure Lengend Snippet: CAF‐derived SRGN promotes tumour invasion and ECM degradation via autophagy secretion. (A) In vivo xenograft models were established in nude mice and divided into four groups: (a) CAL27, (b) CAL27 + WT CAFs, (c) CAL27 + WT CAFs (3‐MA), and (d) CAL27 + SRGN KO CAFs. (B) Tumour volume and tumour weight were monitored ( n = 7). (C, D) H&E staining and IHC analysis of COL1, E‐cadherin, MMP2 and MMP9 were performed in orthotopic xenograft tumour tissues. The expression levels of COL1, E‐cadherin, MMP2 and MMP9 were quantitatively analyzed using Fiji software. Scale bar = 100 µm. (* p < .05; ** p < .01; *** p < .001).
Article Snippet: Primary antibodies used in this assay included: β‐actin (1:4000, 20536‐1, Proteintech), MMP9 (1:1000, bs‐4593R, Bioss),
Techniques: Derivative Assay, In Vivo, Staining, Expressing, Software
Journal: Clinical and Translational Medicine
Article Title: Hypoxia‐induced secretory autophagy in cancer‐associated fibroblasts promotes ECM remodelling through serglycin secretion in oral squamous cell carcinoma
doi: 10.1002/ctm2.70556
Figure Lengend Snippet: Mechanism diagram of hypoxic CAFs‐derived SRGN secretion and tumour progression promotion. Under normal conditions, SRGN is translocated into the ER and subsequently transported via the Golgi apparatus for secretion into the extracellular space. Under hypoxic conditions, elevated autophagy levels in CAFs facilitate the release of SRGN into the ECM through secretory autophagy‐mediated plasma membrane fusion. Within the ECM, SRGN interacts with MMP2 and MMP9, enhancing ECM remodelling and ultimately promoting the invasive capacity of OSCC cells.
Article Snippet: Primary antibodies used in this assay included: β‐actin (1:4000, 20536‐1, Proteintech), MMP9 (1:1000, bs‐4593R, Bioss),
Techniques: Derivative Assay, Clinical Proteomics, Membrane
Journal: ACS nano
Article Title: Echinacoside-Zinc Nanomaterial Inhibits Skin Glycation by Suppressing the Transcriptional Activation of the Receptor for Advanced Glycation End-Products.
doi: 10.1021/acsnano.3c04726
Figure Lengend Snippet: Figure 2. PPZn exerted anti-antiglycan in glycated model mouse skin. (A−C) Representative images of immunohistochemical (IHC) staining (A−a), HE staining (B−a), and Masson staining (C−a) of mouse skin tissue after the indicated treatment. The statistical results of the IHC staining index (A−b), epidermal thickness (B−b), and collagen density (C−b) are shown on the right. Scale bar, 50 μm. (D) qRT- PCR detection of RAGE mRNA levels in skin tissues of mice after the indicated treatment. (E) Western blot representative images and quantitative analysis of RAGE, COL1A2, MMP1, AGEs, and β-actin protein levels in skin tissues of mice after the indicated treatment. (F) Representative images of TUNEL staining of mouse skin tissue after the indicated treatment. Scale bar, 50 μm. (G−I) Relative Hyp content (G), SOD activity (H), and MDA concentration (I) in skin tissues of mice after the indicated treatment. All values are presented as the mean ± SD; P-values determined by two-sided Student’s t test. *P < 0.05, **P < 0.01, compared with the model.
Article Snippet: After being blocked, samples were then incubated with primary antibodies against MDM2 (Proteintech, 1:200), RAGE (Santa, 1:50), STAT2 (Zenbio, 1:100),
Techniques: Immunohistochemical staining, Immunohistochemistry, Staining, Quantitative RT-PCR, Western Blot, TUNEL Assay, Activity Assay, Concentration Assay
Journal: ACS nano
Article Title: Echinacoside-Zinc Nanomaterial Inhibits Skin Glycation by Suppressing the Transcriptional Activation of the Receptor for Advanced Glycation End-Products.
doi: 10.1021/acsnano.3c04726
Figure Lengend Snippet: Figure 3. PPZn exerted antiglycation effects in HaCaT cells. (A) Western blot representative images and quantitative analysis of RAGE, COL1A2, MMP1, AGEs, and β-actin protein levels in HaCaT cells after the indicated treatment. (B) Cell cycle was determined by flow cytometry in HaCaT cells after the indicated treatment. (C) Representative images of TUNEL staining of HaCaT cells after the indicated treatment. Scale bar, 50 μm. (D, E) Relative MDA concentration (D) and SOD activity (E) in HaCaT cells after the indicated treatment. All values are presented as the mean ± SD; P-values determined by two-sided Student’s t test. *P < 0.05, **P < 0.01, compared with the model.
Article Snippet: After being blocked, samples were then incubated with primary antibodies against MDM2 (Proteintech, 1:200), RAGE (Santa, 1:50), STAT2 (Zenbio, 1:100),
Techniques: Western Blot, Flow Cytometry, TUNEL Assay, Staining, Concentration Assay, Activity Assay
Journal: Cell Proliferation
Article Title: Soluble Sema4D From γδ T Cells Exerts Osteoblast Inhibition via Plexin‐B/ mTOR Signalling Contributing to Pathogenesis of Bisphosphonate‐Related Osteonecrosis of the Jaws
doi: 10.1111/cpr.70114
Figure Lengend Snippet: Autocrine MMP3 secretion induced mSema4D cleavage in γδ T cells. (A) KEGG analysis of DEGs in WT ZOL and TCRδ −/− ZOL mice was highly enriched in matrix metalloproteinase (MMP)‐related pathways. (B) The mRNA levels of Mmp3 and Adam17 in the extraction sockets of WT ZOL and TCRδ −/− ZOL mice. n = 4, * p < 0.05, ns indicates no significance. (C) The mRNA levels of Adam17 , Adam10 , Mmp2 , Mmp3 , Mmp9 and Mmp11 after γδ T cells were incubated with 15 μM ZOL for 3 and 6 days. Only the mRNA level of Mmp3 increased significantly and kept a high level after 6 days incubation. n = 6, * p < 0.05, ** p < 0.01. (D) The protein level of MMP3 was much higher than MMP2 and MMP9 in the γδ T cell supernatant measured by ELISA. n = 4, ** p < 0.01, ns indicates no significance. (E) The proportions of γδ T cells after treatment with GM6001 and TAPI‐2. GM6001 and TAPI‐2 are MMP inhibitors. T10 and T20 indicate 10 and 20 nM TAPI‐2, respectively; G50 and G100 indicate 50 and 100 nM GM6001, respectively. n = 6, ns indicates no significance. (F) The expression of Sema4D on γδ T cells after treatment with GM6001 and TAPI‐2. (G) Analysis of Sema4D expression in γδ T cells after treatment with GM6001 or TAPI‐2 on day 2 and 4. n = 6, * p < 0.05, ** p < 0.01. (H) The level of sSema4D in the supernatant of γδ T cells after treatment with GM6001 or TAPI‐2. n = 3, * p < 0.05, ** p < 0.01. (I) The level of sSema4D in the supernatant of γδ T cells after incubating with MMP2, MMP3 and MMP9 in synergy with GM6001. n = 4, * p < 0.05, ** p < 0.01. Data are mean ± SD.
Article Snippet: The kits of sSema4D (ELK5378, ELK Biotechnology),
Techniques: Extraction, Incubation, Enzyme-linked Immunosorbent Assay, Expressing
Journal: Nature Microbiology
Article Title: Gut–liver translocation of pathogen Klebsiella pneumoniae promotes hepatocellular carcinoma in mice
doi: 10.1038/s41564-024-01890-9
Figure Lengend Snippet: a , Design of 5 Gram-negative bacteria gavage in germ-free mice without DEN (PBS group n = 6; BT group n = 6; PM group n = 6; EC group n = 6; EH group n = 6; KP group n = 6) and related results ( b , c ). b , Gut permeability assays using 500 kDa FITC-dextran (top), live bacteria translocated into liver cultured in blood agar plates (middle) and Cy3-conjugated EUB338 probe FISH assay of liver tissues (bottom). n = 6 biologically independent samples. c , Quantitative analysis of TEM, Alcian blue staining, E-cad, CLDN3, CLDN1 IHC staining, and Cy3-conjugated EUB338 probe FISH of colon tissues. n = 10 biologically independent samples. d , THP-1-induced macrophage using phorbol ester (top row) and MMP-2/-9 activity in K. pneumoniae and THP-induced macrophage co-culture conditional medium using gelatin hydrolysis assay and gelatin zymography (bottom row). n = 3 independent experiments with similar results. Ctrl: BHI and macrophage co-culture conditional medium; EC: E. coli and macrophage co-culture conditional medium; KP: K. pneumoniae and macrophage co-culture conditional medium. e , Design of colon macrophage depletion using Clodrosome and its effect on K. pneumoniae -mediated gut barrier dysfunction in germ-free mice without DEN treatment (PBS group n = 6; KP group n = 6; KPC group n = 6) and related results ( f – h ). f , In vivo imaging of body and liver after Cy5.5- d -Lys-labelled K. pneumoniae gavage (top), and live bacterial culture of liver tissues on blood agar plates and quantification (bottom). n = 6 biologically independent samples. g , Gut permeability assays using 500 kDa FITC-dextran (top left) ( n = 6 biologically independent samples) and MMP-2/-9 activity in mouse faecal supernatant detected using gelatin hydrolysis assay (top middle), gelatin zymography (top right) ( n = 3 independent experiments with similar results) and dynamic activity assay (bottom) ( n = 6 biologically independent samples). h , Quantitative analysis of TEM, Alcian blue staining, E-cad and CLDN1 IHC staining, bacteria number per slide using Cy3-conjugated EUB338 probe (PBS group) and K. pneumoniae probe (KP and KPC groups) FISH of colon tissues. n = 10 biologically independent samples. In b , c (excluding tight junction disappear rate) and f – h (excluding liver with live bacteria and tight junction disappear rate) data are presented as mean ± s.e.m. Each data point in bar plots represents one mouse. Liver with living bacteria and tight junction disappearance rate were analysed using Fisher’s exact test. MMP activity was analysed using two-way ANOVA. Unless otherwise stated, statistical significance was calculated using one-way ANOVA. Adjustments were made for multiple comparisons.
Article Snippet:
Techniques: Bacteria, Permeability, Cell Culture, Staining, Immunohistochemistry, Activity Assay, Co-Culture Assay, Hydrolysis Assay, Zymography, In Vivo Imaging
Journal: Nature Microbiology
Article Title: Gut–liver translocation of pathogen Klebsiella pneumoniae promotes hepatocellular carcinoma in mice
doi: 10.1038/s41564-024-01890-9
Figure Lengend Snippet: a , Design of K. pneumoniae gavage for promoting precancerous lesions in germ-free mice without DEN treatment (GF/PBS group n = 10; GF/EC group n = 8; GF/KP group n = 10) and related results ( b – h ). b , In vivo imaging of body and liver after Cy5.5- d -Lys-labelled K. pneumoniae gavage (left), live bacteria culture of liver tissues on blood agar plate (top right) and Cy3-conjugated EUB338 probe (GF/PBS group), E. coli probe (GF/EC group) or K. pneumoniae probe (GF/KP group) FISH detection in liver tissues (bottom right). c , Gut permeability assays using 500 kDa FITC-dextran (left) ( n = 10 (GF/PBS), 8 (GF/EC), 10 (GF/KP)) and quantitative analysis of TEM (middle) ( n = 6 biologically independent samples) and E-cad IHC staining (right) ( n = 6 biologically independent samples). d , MMP-2/-9 activity in mouse faecal supernatant using gelatin hydrolysis assay (bottom left), gelatin zymography (top left) and dynamic activity assay (right). n = 3 biologically independent samples. e , Masson’s trichrome staining (top left) and COLIV IHC staining (top right) of colon tissues and COLIV protein level by western blot (bottom). n = 6 biologically independent samples. f , Representative images of liver gross morphology (top left) (dashed yellow circles indicate nodules), H&E staining of mice liver sections (bottom left), and nodule number and incidence of dysplasia (right). n = 10 (GF/PBS), 8 (GF/EC), 10 (GF/KP). g , IHC staining for PCNA and Ki-67 (left) ( n = 6 biologically independent samples), and western blot assay of PCNA (right) ( n = 3 biologically independent samples). h , Desmin (left) and α-SMA (middle) IHC staining, and Sirius red staining (right) of liver sections. n = 6 biologically independent samples. i , Design of K. pneumoniae gavage on precancerous lesions in SPF mice without DEN treatment (PBS group n = 6; EC group n = 6; KP group n = 6) and relevant results ( j – n ). j , Gut permeability assays using 500 kDa FITC-dextran. n = 6 biologically independent samples. k , Live bacterial culture of liver tissues on blood agar plate (top), and Cy3-conjugated EUB338 probe (PBS group), E. coli probe (EC group) or K. pneumoniae probe (KP group) FISH detection in liver tissues (bottom). n = 6 biologically independent samples. l , TEM (left) and quantitative analysis (right) of colon tissues. n = 6 biologically independent samples. m , Representative images of liver gross morphology (top) (dashed yellow circles indicate nodules), H&E staining of mice liver sections (middle), and nodule number and incidence of dysplasia (bottom). n = 6 biologically independent samples. n , Representative images of IHC staining for PCNA and Sirius red staining of liver sections (left) with quantitative analysis (right). n = 6 biologically independent samples. o , Design of K. pneumoniae gavage on HCC in SPF mice with DEN treatment (DPBS group n = 7; DEC group n = 6; DKP group n = 7) and related results ( p ). p , Representative images of liver gross morphology (left) (dashed yellow circles indicate tumour) and H&E staining of mice liver sections (middle) with tumour incidence and tumour number quantitative analysis (right). n = 7 (DPBS), 6 (DEC), 7 (DKP). In c (excluding tight junction disappear rate), d , e – h (excluding incidence of dysplasia), j,k , m (excluding incidence of dysplasia), n and p (excluding tumour incidence), data are presented as mean ± s.e.m. Each data point in bar plots represents one mouse. Tight junction disappearance rate, incidence of dysplasia and tumour incidence were analysed using Fisher’s exact test. MMP activity was analysed using two-way ANOVA. Unless otherwise stated, statistical significance was calculated using one-way ANOVA. Adjustments were made for multiple comparisons.
Article Snippet:
Techniques: In Vivo Imaging, Bacteria, Permeability, Immunohistochemistry, Activity Assay, Hydrolysis Assay, Zymography, Staining, Western Blot