collagenase type ii solution Search Results


96
Proteintech mmp2
A , B Gene set enrichment analysis (GSEA) of the TCGA HCC cohort identified significant enrichment of EMT and IL-6/JAK/STAT3 signaling pathways in tumors with high OXCT1 expression. C Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, <t>MMP2</t> and E-cadherin in HCCLM3-OXCT1 or CON cells and in ( D ) Huh7-shOXCT1 or shCON cells. E Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-Cadherin in HCCLM3 cells treated with vehicle (DMSO) or 10 μM Stattic (STAT3 Inhibitor) for 24 h. F Wound healing assay measured the migratory abilities of the HCCLM3 cells, respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. G Transwell migration and invasion assays of the HCCLM3 cells respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.
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
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96
Proteintech mouse anti mmp2
A , B Gene set enrichment analysis (GSEA) of the TCGA HCC cohort identified significant enrichment of EMT and IL-6/JAK/STAT3 signaling pathways in tumors with high OXCT1 expression. C Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, <t>MMP2</t> and E-cadherin in HCCLM3-OXCT1 or CON cells and in ( D ) Huh7-shOXCT1 or shCON cells. E Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-Cadherin in HCCLM3 cells treated with vehicle (DMSO) or 10 μM Stattic (STAT3 Inhibitor) for 24 h. F Wound healing assay measured the migratory abilities of the HCCLM3 cells, respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. G Transwell migration and invasion assays of the HCCLM3 cells respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.
Mouse Anti 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
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Average 96 stars, based on 1 article reviews
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93
Santa Cruz Biotechnology class ii complexes
A , B Gene set enrichment analysis (GSEA) of the TCGA HCC cohort identified significant enrichment of EMT and IL-6/JAK/STAT3 signaling pathways in tumors with high OXCT1 expression. C Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, <t>MMP2</t> and E-cadherin in HCCLM3-OXCT1 or CON cells and in ( D ) Huh7-shOXCT1 or shCON cells. E Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-Cadherin in HCCLM3 cells treated with vehicle (DMSO) or 10 μM Stattic (STAT3 Inhibitor) for 24 h. F Wound healing assay measured the migratory abilities of the HCCLM3 cells, respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. G Transwell migration and invasion assays of the HCCLM3 cells respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.
Class Ii Complexes, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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95
Boster Bio human plasma mmp 2
A , B Gene set enrichment analysis (GSEA) of the TCGA HCC cohort identified significant enrichment of EMT and IL-6/JAK/STAT3 signaling pathways in tumors with high OXCT1 expression. C Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, <t>MMP2</t> and E-cadherin in HCCLM3-OXCT1 or CON cells and in ( D ) Huh7-shOXCT1 or shCON cells. E Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-Cadherin in HCCLM3 cells treated with vehicle (DMSO) or 10 μM Stattic (STAT3 Inhibitor) for 24 h. F Wound healing assay measured the migratory abilities of the HCCLM3 cells, respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. G Transwell migration and invasion assays of the HCCLM3 cells respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.
Human Plasma Mmp 2, supplied by Boster Bio, 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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86
Rockland Immunochemicals mmp2
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
Mmp2, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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93
Proteintech matrix metalloproteinase 2
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
Matrix Metalloproteinase 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
matrix metalloproteinase 2 - by Bioz Stars, 2026-08
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96
Valiant Co Ltd collagenase type ii enzyme
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
Collagenase Type Ii Enzyme, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
FUJIFILM collagenase type ii
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
Collagenase Type Ii, supplied by FUJIFILM, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Merck KGaA 0.1% collagenase d solution from clostridium histolyticum
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
0.1% Collagenase D Solution From Clostridium Histolyticum, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Lorne Laboratories collagenase type ii
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
Collagenase Type Ii, supplied by Lorne Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
US Biological Life Sciences antibody for collagen type ii c7510-21c
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
Antibody For Collagen Type Ii C7510 21c, supplied by US Biological Life Sciences, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
STEMCELL Technologies Inc collagenase type ii solution
Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) <t>MMP2</t> and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.
Collagenase Type Ii Solution, supplied by STEMCELL Technologies Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


A , B Gene set enrichment analysis (GSEA) of the TCGA HCC cohort identified significant enrichment of EMT and IL-6/JAK/STAT3 signaling pathways in tumors with high OXCT1 expression. C Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-cadherin in HCCLM3-OXCT1 or CON cells and in ( D ) Huh7-shOXCT1 or shCON cells. E Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-Cadherin in HCCLM3 cells treated with vehicle (DMSO) or 10 μM Stattic (STAT3 Inhibitor) for 24 h. F Wound healing assay measured the migratory abilities of the HCCLM3 cells, respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. G Transwell migration and invasion assays of the HCCLM3 cells respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.

Journal: Cell Death & Disease

Article Title: β-catenin mutation reprograms ketone body metabolism to drive hepatocellular carcinoma metastasis and resistance to ketogenic therapy via transcriptional activation of OXCT1

doi: 10.1038/s41419-026-08457-y

Figure Lengend Snippet: A , B Gene set enrichment analysis (GSEA) of the TCGA HCC cohort identified significant enrichment of EMT and IL-6/JAK/STAT3 signaling pathways in tumors with high OXCT1 expression. C Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-cadherin in HCCLM3-OXCT1 or CON cells and in ( D ) Huh7-shOXCT1 or shCON cells. E Western blot analyzed protein levels of OXCT1, STAT3, p-STAT3, Snail, Vimentin, MMP2 and E-Cadherin in HCCLM3 cells treated with vehicle (DMSO) or 10 μM Stattic (STAT3 Inhibitor) for 24 h. F Wound healing assay measured the migratory abilities of the HCCLM3 cells, respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. G Transwell migration and invasion assays of the HCCLM3 cells respectively, treated with vehicle (DMSO) or 10 μM Stattic for 24 h. Quantified data are shown on the right. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.

Article Snippet: Primary antibodies against the following proteins were used: β-actin (#20536-1-AP, Proteintech, China), OXCT1 (#12175-1-AP, Proteintech, China), β-catenin (#8480, Cell Signaling Technology, USA), PPARα (#66826-1-Ig, Proteintech, China), HMGCS2 (#ab137043, Abcam, USA), BDH1 (#15417-1-AP, Proteintech, China), LEF1 (#14972-1-AP, Proteintech, China), MMP2 (#10373-2-AP, Proteintech, China), Snai1 (13099-1-AP, Proteintech, China), Vimentin(#60330-1-Ig, Proteintech, China), E-cadherin (HY- P81271 , MCE, China), STAT3 (#9139, Cell Signaling Technology, USA), p-STAT3 (#9145, Cell Signaling Technology, USA).

Techniques: Protein-Protein interactions, Expressing, Western Blot, Wound Healing Assay, Migration

HCCLM3 cells stably overexpressing β-cateninS33Y (β-catenin) were further infected with shOXCT1 lentivirus to generate cells with concurrent OXCT1 knockdown (β-catenin+shOXCT1). Control (CON), β-catenin, and β-catenin+shOXCT1 cells were used. A Western blot analyzed protein levels of OXCT1 and β-catenin in the CON, β-catenin and β-catenin+shoxct1 groups. B Wound healing assay was performed to measure the migratory abilities of the indicated cell groups. C Transwell migration and invasion assays measured the migratory and invasive abilities of the indicated cell groups. D Western blot analyzed protein levels of STAT3, p-STAT3, MMP2, Snail, Vimentin and E-cadherin in the indicated cell groups. E In tail vein metastasis models, mice ( n = 4 per group) were injected with 2 × 10⁶ cells from each group. Representative livers show metastatic burden (left panel: overview; right panel: magnified views of metastatic lesions). F Western blot analyzed protein levels of STAT3, p-STAT3, MMP2, Vimentin, Snail, E-cadherin, OXCT1, and β-catenin in liver metastatic tissues from each group. G Representative images of liver metastasis with HE staining of the CON, β-catenin, and β-catenin+shoxct1 groups. H Representative images of liver metastasis with Ki67 staining of the CON, β-catenin, and β-catenin+shoxct1 groups. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.

Journal: Cell Death & Disease

Article Title: β-catenin mutation reprograms ketone body metabolism to drive hepatocellular carcinoma metastasis and resistance to ketogenic therapy via transcriptional activation of OXCT1

doi: 10.1038/s41419-026-08457-y

Figure Lengend Snippet: HCCLM3 cells stably overexpressing β-cateninS33Y (β-catenin) were further infected with shOXCT1 lentivirus to generate cells with concurrent OXCT1 knockdown (β-catenin+shOXCT1). Control (CON), β-catenin, and β-catenin+shOXCT1 cells were used. A Western blot analyzed protein levels of OXCT1 and β-catenin in the CON, β-catenin and β-catenin+shoxct1 groups. B Wound healing assay was performed to measure the migratory abilities of the indicated cell groups. C Transwell migration and invasion assays measured the migratory and invasive abilities of the indicated cell groups. D Western blot analyzed protein levels of STAT3, p-STAT3, MMP2, Snail, Vimentin and E-cadherin in the indicated cell groups. E In tail vein metastasis models, mice ( n = 4 per group) were injected with 2 × 10⁶ cells from each group. Representative livers show metastatic burden (left panel: overview; right panel: magnified views of metastatic lesions). F Western blot analyzed protein levels of STAT3, p-STAT3, MMP2, Vimentin, Snail, E-cadherin, OXCT1, and β-catenin in liver metastatic tissues from each group. G Representative images of liver metastasis with HE staining of the CON, β-catenin, and β-catenin+shoxct1 groups. H Representative images of liver metastasis with Ki67 staining of the CON, β-catenin, and β-catenin+shoxct1 groups. Data are presented as the mean ± SD. *, p < 0.05; **, p < 0.01; ***, p < 0.001, ns, not significant.

Article Snippet: Primary antibodies against the following proteins were used: β-actin (#20536-1-AP, Proteintech, China), OXCT1 (#12175-1-AP, Proteintech, China), β-catenin (#8480, Cell Signaling Technology, USA), PPARα (#66826-1-Ig, Proteintech, China), HMGCS2 (#ab137043, Abcam, USA), BDH1 (#15417-1-AP, Proteintech, China), LEF1 (#14972-1-AP, Proteintech, China), MMP2 (#10373-2-AP, Proteintech, China), Snai1 (13099-1-AP, Proteintech, China), Vimentin(#60330-1-Ig, Proteintech, China), E-cadherin (HY- P81271 , MCE, China), STAT3 (#9139, Cell Signaling Technology, USA), p-STAT3 (#9145, Cell Signaling Technology, USA).

Techniques: Stable Transfection, Infection, Knockdown, Control, Western Blot, Wound Healing Assay, Migration, Injection, Staining

Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) MMP2 and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.

Journal: Experimental and Therapeutic Medicine

Article Title: IL-32γ promotes integrin αvβ6 expression through the activation of NF-κB in HSCs

doi: 10.3892/etm.2017.4956

Figure Lengend Snippet: Effect of different concentrations (0, 5, 10 and 20 ng/ml) of IL-32γ on LX-2 activation phenotypes. (A) Growth curves of LX-2 demonstrated that upregulation of IL-32γ promoted proliferation of LX-2. (B) Reverse transcription-quantitative polymerase chain reaction assessing mRNA levels of α-SMA, (C) collagen I, (D) TIMP1, (E) MMP2 and (F) MMP9, representing the activation level of LX-2. (G) Western blot analysis was used to measure collagen I, MMP9, MMP2, α-SMA, TIMP1 and GAPDH expression in whole-cell extracts. Data are presented as the mean ± standard deviation of three experiments. *P<0.01 and **P<0.05 vs. 0 ng/ml IL-32γ. IL-32γ, interleukin-32γ; α-SMA, α-smooth muscle actin; TIMP1, tissue inhibitor of metalloproteinase 1; MMP, matrix metalloproteinases; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; RT-qPCR, reverse transcription-quantitative polymerase chain reaction.

Article Snippet: Primary antibodies were as follows: Anti-integrin αVβ6 (cat. no. ab97588; Abcam, Cambridge, MA, USA), anti-GAPDH (cat. no. KGAA002-2; Nanjing KeyGen Biotech Co., Ltd.), anti-α-SMA (cat. no. G6669; Sigma-Aldrich; Merck KGaA), collagen type I antibody (cat. no. 600-402-103; Rockland, Limerick, PA, USA), TIMP1 (cat. no. 8946), MMP2 (cat. no. 87809), MMP9 (cat. no. 13667), NF-κB: p65 (cat. no. 8242), p50 (cat. no. 3035) (all Cell Signaling Technology, Inc., Danvers, MA, USA) and IL-32γ (cat. no. 513501; Biolegend, Inc.).

Techniques: Activation Assay, Real-time Polymerase Chain Reaction, Western Blot, Expressing, Standard Deviation, Quantitative RT-PCR