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Proteintech
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Santa Cruz Biotechnology
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Boster Bio
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Rockland Immunochemicals
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Proteintech
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Merck KGaA
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Lorne Laboratories
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US Biological Life Sciences
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STEMCELL Technologies Inc
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Image Search Results
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),
Techniques: Protein-Protein interactions, Expressing, Western Blot, Wound Healing Assay, Migration
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),
Techniques: Stable Transfection, Infection, Knockdown, Control, Western Blot, Wound Healing Assay, Migration, Injection, Staining
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;
Techniques: Activation Assay, Real-time Polymerase Chain Reaction, Western Blot, Expressing, Standard Deviation, Quantitative RT-PCR