human recombinant fabp4 Search Results


93
R&D Systems recombinant human fabp4
( A ) Representative immunoblots ( n = 2) and quantification of <t>FABP4</t> protein relative to β-tubulin loading control in perirenal adipose tissue of WT, Adipo-KO, Endo-KO, and Total-KO mice. WT, Total-KO: n = 5/group; Adipo-KO, Endo-KO: n = 6/group. ( B ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in perirenal adipose tissue of WT and Myeloid-KO mice. n = 5/group. ( C ) Representative FABP4 immunostaining in perigonadal adipose tissue from WT, Adipo-KO, Endo-KO, and Total-KO mice. Magnification, 400 × . ( D ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in isolated perigonadal adipocytes of WT, Adipo-KO, Endo-KO, and Total-KO mice. WT, Adipo-KO, Endo-KO: n = 5/group; Total-KO: n = 1. * P < 0.05, ** P < 0.01, *** P < 0.001 by 1-way ANOVA, followed by Tukey’s multiple-comparison test ( A and D ), or by t test ( B ). ND, no signal detected.
Recombinant Human Fabp4, supplied by R&D Systems, 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/result/recombinant human fabp4/product/R&D Systems
Average 93 stars, based on 1 article reviews
recombinant human fabp4 - by Bioz Stars, 2026-03
93/100 stars
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90
Cloud-Clone corp recombinant human fabp4
The primer sequence of target genes
Recombinant Human Fabp4, supplied by Cloud-Clone corp, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/recombinant human fabp4/product/Cloud-Clone corp
Average 90 stars, based on 1 article reviews
recombinant human fabp4 - by Bioz Stars, 2026-03
90/100 stars
  Buy from Supplier

Image Search Results


( A ) Representative immunoblots ( n = 2) and quantification of FABP4 protein relative to β-tubulin loading control in perirenal adipose tissue of WT, Adipo-KO, Endo-KO, and Total-KO mice. WT, Total-KO: n = 5/group; Adipo-KO, Endo-KO: n = 6/group. ( B ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in perirenal adipose tissue of WT and Myeloid-KO mice. n = 5/group. ( C ) Representative FABP4 immunostaining in perigonadal adipose tissue from WT, Adipo-KO, Endo-KO, and Total-KO mice. Magnification, 400 × . ( D ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in isolated perigonadal adipocytes of WT, Adipo-KO, Endo-KO, and Total-KO mice. WT, Adipo-KO, Endo-KO: n = 5/group; Total-KO: n = 1. * P < 0.05, ** P < 0.01, *** P < 0.001 by 1-way ANOVA, followed by Tukey’s multiple-comparison test ( A and D ), or by t test ( B ). ND, no signal detected.

Journal: JCI Insight

Article Title: Endothelial-derived FABP4 constitutes the majority of basal circulating hormone and regulates lipolysis-driven insulin secretion

doi: 10.1172/jci.insight.164642

Figure Lengend Snippet: ( A ) Representative immunoblots ( n = 2) and quantification of FABP4 protein relative to β-tubulin loading control in perirenal adipose tissue of WT, Adipo-KO, Endo-KO, and Total-KO mice. WT, Total-KO: n = 5/group; Adipo-KO, Endo-KO: n = 6/group. ( B ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in perirenal adipose tissue of WT and Myeloid-KO mice. n = 5/group. ( C ) Representative FABP4 immunostaining in perigonadal adipose tissue from WT, Adipo-KO, Endo-KO, and Total-KO mice. Magnification, 400 × . ( D ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in isolated perigonadal adipocytes of WT, Adipo-KO, Endo-KO, and Total-KO mice. WT, Adipo-KO, Endo-KO: n = 5/group; Total-KO: n = 1. * P < 0.05, ** P < 0.01, *** P < 0.001 by 1-way ANOVA, followed by Tukey’s multiple-comparison test ( A and D ), or by t test ( B ). ND, no signal detected.

Article Snippet: For in-house FABP4 ELISA, we used anti-FABP4 antibodies produced for the Hotamışlıgil lab by the Dana Farber Antibody Core, as described previously ( ) (clone 351.4.2E12.H1.F12 for capture, HRP-tagged clone 351.4.5E1.H3 for detection), and recombinant human FABP4 as a standard (R&D Systems).

Techniques: Western Blot, Control, Immunostaining, Isolation, Comparison

( A ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in CD31-isolated endothelial cells from liver, spleen, heart, and lungs of WT, Adipo-KO, and Endo-KO mice. n = 2/group. ( B ) Representative FABP4 immunostaining in livers of WT, Adipo-KO, Endo-KO, and Myeloid-KO mice; magnification, 200×. ND, no signal detected.

Journal: JCI Insight

Article Title: Endothelial-derived FABP4 constitutes the majority of basal circulating hormone and regulates lipolysis-driven insulin secretion

doi: 10.1172/jci.insight.164642

Figure Lengend Snippet: ( A ) Immunoblots and quantification of FABP4 protein relative to β-tubulin loading control in CD31-isolated endothelial cells from liver, spleen, heart, and lungs of WT, Adipo-KO, and Endo-KO mice. n = 2/group. ( B ) Representative FABP4 immunostaining in livers of WT, Adipo-KO, Endo-KO, and Myeloid-KO mice; magnification, 200×. ND, no signal detected.

Article Snippet: For in-house FABP4 ELISA, we used anti-FABP4 antibodies produced for the Hotamışlıgil lab by the Dana Farber Antibody Core, as described previously ( ) (clone 351.4.2E12.H1.F12 for capture, HRP-tagged clone 351.4.5E1.H3 for detection), and recombinant human FABP4 as a standard (R&D Systems).

Techniques: Western Blot, Control, Isolation, Immunostaining

( A ) Plasma FABP4 levels in lean WT ( n = 43), Adipo-KO ( n = 29), Endo-KO ( n = 29), and Total-KO ( n = 23) male mice. Data are pooled from 5 experiments. Average age of mice is 13 weeks old. Immunoblots of perirenal and mesenteric adipose FABP4 protein expression, for comparison with plasma levels. ( B ) Plasma FABP4 levels in WT versus Myeloid-KO mice. Data are pooled from 2 experiments, n = 8/group/experiment. ( C ) Plasma FABP5 levels in WT, Adipo-KO, Endo-KO, and Total-KO mice. n = 8/group. All samples were collected from male mice after 6-hour daytime food withdrawal. * P < 0.05, **** P < 0.0001 by unpaired t test ( B ) or by 1-way ANOVA, followed by Tukey’s multiple-comparison test ( A and C ).

Journal: JCI Insight

Article Title: Endothelial-derived FABP4 constitutes the majority of basal circulating hormone and regulates lipolysis-driven insulin secretion

doi: 10.1172/jci.insight.164642

Figure Lengend Snippet: ( A ) Plasma FABP4 levels in lean WT ( n = 43), Adipo-KO ( n = 29), Endo-KO ( n = 29), and Total-KO ( n = 23) male mice. Data are pooled from 5 experiments. Average age of mice is 13 weeks old. Immunoblots of perirenal and mesenteric adipose FABP4 protein expression, for comparison with plasma levels. ( B ) Plasma FABP4 levels in WT versus Myeloid-KO mice. Data are pooled from 2 experiments, n = 8/group/experiment. ( C ) Plasma FABP5 levels in WT, Adipo-KO, Endo-KO, and Total-KO mice. n = 8/group. All samples were collected from male mice after 6-hour daytime food withdrawal. * P < 0.05, **** P < 0.0001 by unpaired t test ( B ) or by 1-way ANOVA, followed by Tukey’s multiple-comparison test ( A and C ).

Article Snippet: For in-house FABP4 ELISA, we used anti-FABP4 antibodies produced for the Hotamışlıgil lab by the Dana Farber Antibody Core, as described previously ( ) (clone 351.4.2E12.H1.F12 for capture, HRP-tagged clone 351.4.5E1.H3 for detection), and recombinant human FABP4 as a standard (R&D Systems).

Techniques: Clinical Proteomics, Western Blot, Expressing, Comparison

( A – E ) Plasma FABP4 levels, baseline-corrected plasma FABP4, AUC of baseline-corrected plasma FABP4, nonesterified fatty acid (NEFA), and glycerol responses to 10 mg/kg isoproterenol-induced lipolysis in ~13-week-old WT ( n = 54), Adipo-KO ( n = 40), Endo-KO ( n = 34), and Total-KO ( n = 8 for FABP4, n = 15 for NEFA, glycerol) mice. Data for A – E are pooled from 6 experiments. ( F – H ) NEFA, glycerol, and FABP4 responses to FSK-induced lipolysis in perigonadal adipose explants from WT, Adipo-KO, and Endo-KO mice; n = 4/group. Data are normalized to amount of adipose tissue per culture well. ( I ) Plasma FABP4 responses to 10 mg/kg isoproterenol-induced lipolysis in WT and Myeloid-KO mice; n = 8/group. ( J ) WT versus Adipo Endo-KO mice with deletion of FABP4 in both adipocytes and endothelial cells; n = 6/group. All experiments were in male mice. **** P < 0.0001, *** P < 0.001, ** P <0.01, * P < 0.05 versus WT; °°°° P < 0.0001, °°° P < 0.001, °° P < 0.01, ° P < 0.05 versus Endo-KO; • P < 0.05 versus Adipo-KO, by mixed-effects analysis followed by Tukey’s multiple-comparison test ( A , B , D , and E ), or 2-way ANOVA followed by Tukey’s ( F , G , and H ) or Sidak’s ( I and J ) multiple-comparison test. **** P < 0.0001, ** P <0.01 by 1-way ANOVA followed by Tukey’s multiple-comparison test ( C ). ND, no signal detected.

Journal: JCI Insight

Article Title: Endothelial-derived FABP4 constitutes the majority of basal circulating hormone and regulates lipolysis-driven insulin secretion

doi: 10.1172/jci.insight.164642

Figure Lengend Snippet: ( A – E ) Plasma FABP4 levels, baseline-corrected plasma FABP4, AUC of baseline-corrected plasma FABP4, nonesterified fatty acid (NEFA), and glycerol responses to 10 mg/kg isoproterenol-induced lipolysis in ~13-week-old WT ( n = 54), Adipo-KO ( n = 40), Endo-KO ( n = 34), and Total-KO ( n = 8 for FABP4, n = 15 for NEFA, glycerol) mice. Data for A – E are pooled from 6 experiments. ( F – H ) NEFA, glycerol, and FABP4 responses to FSK-induced lipolysis in perigonadal adipose explants from WT, Adipo-KO, and Endo-KO mice; n = 4/group. Data are normalized to amount of adipose tissue per culture well. ( I ) Plasma FABP4 responses to 10 mg/kg isoproterenol-induced lipolysis in WT and Myeloid-KO mice; n = 8/group. ( J ) WT versus Adipo Endo-KO mice with deletion of FABP4 in both adipocytes and endothelial cells; n = 6/group. All experiments were in male mice. **** P < 0.0001, *** P < 0.001, ** P <0.01, * P < 0.05 versus WT; °°°° P < 0.0001, °°° P < 0.001, °° P < 0.01, ° P < 0.05 versus Endo-KO; • P < 0.05 versus Adipo-KO, by mixed-effects analysis followed by Tukey’s multiple-comparison test ( A , B , D , and E ), or 2-way ANOVA followed by Tukey’s ( F , G , and H ) or Sidak’s ( I and J ) multiple-comparison test. **** P < 0.0001, ** P <0.01 by 1-way ANOVA followed by Tukey’s multiple-comparison test ( C ). ND, no signal detected.

Article Snippet: For in-house FABP4 ELISA, we used anti-FABP4 antibodies produced for the Hotamışlıgil lab by the Dana Farber Antibody Core, as described previously ( ) (clone 351.4.2E12.H1.F12 for capture, HRP-tagged clone 351.4.5E1.H3 for detection), and recombinant human FABP4 as a standard (R&D Systems).

Techniques: Clinical Proteomics, Comparison

( A ) Twelve-hour conditioned media FABP4 levels from CD31-isolated endothelial cells from liver, heart, and lungs of WT, Adipo-KO, and Endo-KO mice, normalized to total cellular protein; n = 3 mice/group. ( B and C ) FABP4 levels in HUVEC lysates and 5-hour conditioned media, normalized to total cellular protein at days 3 through 14 after seeding. Pool of 2 experiments; n = 6/time point. ( D ) Time-course of cumulative FABP4 levels in media of day 7 HUVECs; n = 4/time point. Inset: Media lactate dehydrogenase (LDH) levels during the same time course. °°°° P < 0.0001, °°° P < 0.001 versus 0 hours by 1-way ANOVA followed by Dunnett’s multiple-comparison test. ( E ) Effects of the ER-Golgi pathway inhibitor, brefeldin A (BFA), on FABP4 and endothelin-1 (ET-1) secretion from day 11 HUVECs; n = 3/BFA dose. ( F ) Effects of forskolin (FSK) on FABP4 secretion in HUVECs versus 3T3-L1 adipocytes. n = 3/FSK dose. * P < 0.05 versus HUVEC by 2-way ANOVA followed by Sidak’s multiple-comparison test. ( G ) Effects of FSK on FABP4 and von Willebrand Factor (vWF) secretion from day 11 HUVECs. FABP4, n = 4/FSK dose; vWF, n = 3/FSK dose. ( H ) Total FABP4 measured by ELISA in HUVEC cell lysates (CL), conditioned media (CM), and exosomes (Exos) isolated from CM; n = 3. ( I ) Western blots of FABP4, exosome markers CD-63 and ALiX, and double-membrane protein β-actin in HUVEC cell lysates, conditioned media, and exosomes. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by 1-way ANOVA followed by Sidak’s ( A ), Tukey’s ( B , C , and H ), or Dunnett’s ( E and G ) multiple-comparison test.

Journal: JCI Insight

Article Title: Endothelial-derived FABP4 constitutes the majority of basal circulating hormone and regulates lipolysis-driven insulin secretion

doi: 10.1172/jci.insight.164642

Figure Lengend Snippet: ( A ) Twelve-hour conditioned media FABP4 levels from CD31-isolated endothelial cells from liver, heart, and lungs of WT, Adipo-KO, and Endo-KO mice, normalized to total cellular protein; n = 3 mice/group. ( B and C ) FABP4 levels in HUVEC lysates and 5-hour conditioned media, normalized to total cellular protein at days 3 through 14 after seeding. Pool of 2 experiments; n = 6/time point. ( D ) Time-course of cumulative FABP4 levels in media of day 7 HUVECs; n = 4/time point. Inset: Media lactate dehydrogenase (LDH) levels during the same time course. °°°° P < 0.0001, °°° P < 0.001 versus 0 hours by 1-way ANOVA followed by Dunnett’s multiple-comparison test. ( E ) Effects of the ER-Golgi pathway inhibitor, brefeldin A (BFA), on FABP4 and endothelin-1 (ET-1) secretion from day 11 HUVECs; n = 3/BFA dose. ( F ) Effects of forskolin (FSK) on FABP4 secretion in HUVECs versus 3T3-L1 adipocytes. n = 3/FSK dose. * P < 0.05 versus HUVEC by 2-way ANOVA followed by Sidak’s multiple-comparison test. ( G ) Effects of FSK on FABP4 and von Willebrand Factor (vWF) secretion from day 11 HUVECs. FABP4, n = 4/FSK dose; vWF, n = 3/FSK dose. ( H ) Total FABP4 measured by ELISA in HUVEC cell lysates (CL), conditioned media (CM), and exosomes (Exos) isolated from CM; n = 3. ( I ) Western blots of FABP4, exosome markers CD-63 and ALiX, and double-membrane protein β-actin in HUVEC cell lysates, conditioned media, and exosomes. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001 by 1-way ANOVA followed by Sidak’s ( A ), Tukey’s ( B , C , and H ), or Dunnett’s ( E and G ) multiple-comparison test.

Article Snippet: For in-house FABP4 ELISA, we used anti-FABP4 antibodies produced for the Hotamışlıgil lab by the Dana Farber Antibody Core, as described previously ( ) (clone 351.4.2E12.H1.F12 for capture, HRP-tagged clone 351.4.5E1.H3 for detection), and recombinant human FABP4 as a standard (R&D Systems).

Techniques: Isolation, Comparison, Enzyme-linked Immunosorbent Assay, Western Blot, Membrane

( A ) Plasma insulin responses to 10 mg/kg isoproterenol-induced lipolysis in WT ( n = 52), Adipo-KO ( n = 40), Endo-KO ( n = 34), and Total-KO ( n = 15) mice. Data are pooled from 6 experiments. ( B ) Plasma insulin responses to 10 mg/kg isoproterenol-induced lipolysis in WT versus Myeloid-KO mice; n = 8/group. ( C and D ) Blood glucose levels in response to 10 mg/kg isoproterenol-induced lipolysis in WT versus Endo-KO mice ( n = 10/group) and in WT ( n = 7) versus Adipo-KO ( n = 10) mice. ( E and F ) Plasma FAPB4 and insulin responses in WT and Fabp4 –/– mice injected with PBS or 7 μg of FABP4 prior to induction of lipolysis with 10 mg/kg isoproterenol; n = 8/group. All experiments were in male mice. **** P < 0.0001, *** P < 0.001, ** P < 0.01, * P < 0.05 versus WT; °°°° P < 0.0001, °°° P < 0.001, ° P < 0.05 versus Adipo-KO, by mixed-effects analysis, followed by Tukey’s ( A and F ) or Sidak’s ( C and E ) multiple-comparison test, or 2-way ANOVA followed by Tukey’s multiple-comparison test ( B and D ). ND, no signal detected.

Journal: JCI Insight

Article Title: Endothelial-derived FABP4 constitutes the majority of basal circulating hormone and regulates lipolysis-driven insulin secretion

doi: 10.1172/jci.insight.164642

Figure Lengend Snippet: ( A ) Plasma insulin responses to 10 mg/kg isoproterenol-induced lipolysis in WT ( n = 52), Adipo-KO ( n = 40), Endo-KO ( n = 34), and Total-KO ( n = 15) mice. Data are pooled from 6 experiments. ( B ) Plasma insulin responses to 10 mg/kg isoproterenol-induced lipolysis in WT versus Myeloid-KO mice; n = 8/group. ( C and D ) Blood glucose levels in response to 10 mg/kg isoproterenol-induced lipolysis in WT versus Endo-KO mice ( n = 10/group) and in WT ( n = 7) versus Adipo-KO ( n = 10) mice. ( E and F ) Plasma FAPB4 and insulin responses in WT and Fabp4 –/– mice injected with PBS or 7 μg of FABP4 prior to induction of lipolysis with 10 mg/kg isoproterenol; n = 8/group. All experiments were in male mice. **** P < 0.0001, *** P < 0.001, ** P < 0.01, * P < 0.05 versus WT; °°°° P < 0.0001, °°° P < 0.001, ° P < 0.05 versus Adipo-KO, by mixed-effects analysis, followed by Tukey’s ( A and F ) or Sidak’s ( C and E ) multiple-comparison test, or 2-way ANOVA followed by Tukey’s multiple-comparison test ( B and D ). ND, no signal detected.

Article Snippet: For in-house FABP4 ELISA, we used anti-FABP4 antibodies produced for the Hotamışlıgil lab by the Dana Farber Antibody Core, as described previously ( ) (clone 351.4.2E12.H1.F12 for capture, HRP-tagged clone 351.4.5E1.H3 for detection), and recombinant human FABP4 as a standard (R&D Systems).

Techniques: Clinical Proteomics, Injection, Comparison

( A ) Upper panel: Representative FABP4 immunostaining of pancreas of WT, Adipo-KO, Endo-KO, and Myeloid-KO mice. Islets are encircled by black dotted lines. Magnification, 400×. Lower panel: 2× enlargement of boxed area in upper panel. ( B ) Representative insulin immunostaining of pancreas from WT, Adipo-KO, Endo-KO, and Total-KO mice; magnification, 80×. ( C ) Quantification of insulin-positive area. Pool of 2 experiments. WT: n = 5; Adipo-KO, Endo-KO, Total-KO: n = 6/group. ( D ) Insulin secretion from isolated islets of WT, Adipo-KO, Endo-KO, and Total-KO mice in response to low glucose (LG, 2.8 mM), high glucose (HG, 16.7 mM), HG + forskolin (FSK, 10 μM), and HG + KCl (30 mM). Insulin secretion is normalized to cellular DNA. LG, HG: n = 4/group. HG + FSK or KCl: n = 3/group. ( E ) Fold-increase in insulin secretion induced by HG + FSK (10 μM) over HG from 7D. * P < 0.05, ** P < 0.01, *** P < 0.001 by 1-way ANOVA followed by Tukey’s ( C and E ) or Dunnett’s ( D ) multiple-comparison test. HG Endo-KO is P < 0.05 by t test ( D ).

Journal: JCI Insight

Article Title: Endothelial-derived FABP4 constitutes the majority of basal circulating hormone and regulates lipolysis-driven insulin secretion

doi: 10.1172/jci.insight.164642

Figure Lengend Snippet: ( A ) Upper panel: Representative FABP4 immunostaining of pancreas of WT, Adipo-KO, Endo-KO, and Myeloid-KO mice. Islets are encircled by black dotted lines. Magnification, 400×. Lower panel: 2× enlargement of boxed area in upper panel. ( B ) Representative insulin immunostaining of pancreas from WT, Adipo-KO, Endo-KO, and Total-KO mice; magnification, 80×. ( C ) Quantification of insulin-positive area. Pool of 2 experiments. WT: n = 5; Adipo-KO, Endo-KO, Total-KO: n = 6/group. ( D ) Insulin secretion from isolated islets of WT, Adipo-KO, Endo-KO, and Total-KO mice in response to low glucose (LG, 2.8 mM), high glucose (HG, 16.7 mM), HG + forskolin (FSK, 10 μM), and HG + KCl (30 mM). Insulin secretion is normalized to cellular DNA. LG, HG: n = 4/group. HG + FSK or KCl: n = 3/group. ( E ) Fold-increase in insulin secretion induced by HG + FSK (10 μM) over HG from 7D. * P < 0.05, ** P < 0.01, *** P < 0.001 by 1-way ANOVA followed by Tukey’s ( C and E ) or Dunnett’s ( D ) multiple-comparison test. HG Endo-KO is P < 0.05 by t test ( D ).

Article Snippet: For in-house FABP4 ELISA, we used anti-FABP4 antibodies produced for the Hotamışlıgil lab by the Dana Farber Antibody Core, as described previously ( ) (clone 351.4.2E12.H1.F12 for capture, HRP-tagged clone 351.4.5E1.H3 for detection), and recombinant human FABP4 as a standard (R&D Systems).

Techniques: Immunostaining, Isolation, Comparison

The primer sequence of target genes

Journal: American Journal of Cancer Research

Article Title: 25-HC promotes hepatocellular carcinoma metastasis through up-regulation of TLR4 dependent FABP4

doi:

Figure Lengend Snippet: The primer sequence of target genes

Article Snippet: Recombinant human FABP4 was bought from Cloud-Clone Corp. (Houston, TX, USA) and dissolved in PBS.

Techniques: Sequencing

Sequences of siRNA

Journal: American Journal of Cancer Research

Article Title: 25-HC promotes hepatocellular carcinoma metastasis through up-regulation of TLR4 dependent FABP4

doi:

Figure Lengend Snippet: Sequences of siRNA

Article Snippet: Recombinant human FABP4 was bought from Cloud-Clone Corp. (Houston, TX, USA) and dissolved in PBS.

Techniques:

25-HC increases FABP4 expression which could directly enhance HepG2 cells migration. A. HepG2 cells were treated with the indicated concentrations of 25-HC for 24 hours before mRNA or protein was extracted to determine the expression of FABP4 by RT-qPCR or Western blotting, respectively. B. HepG2 cells were treated with the indicated concentrations of FABP4 (0, 20, 40 and 100 ng/mL) for 24 hours before mRNA or protein was extracted. The mRNA expressions of MMP2 and MMP9 were examined by RT-qPCR and the protein expressions of MMP1, MMP2, MMP3, MMP9 were detected by Western blotting, respectively. C. Migration assay of HepG2 cells after stimulation of FABP4 for 36 hours was performed. Results were obtained from 3 independent experiments and are expressed as the means ± SEM. Statistical significance was determined by one-way ANOVA followed by Dunnett’s test. ns, not significant, *P<0.05, **P<0.01, ***P<0.001.

Journal: American Journal of Cancer Research

Article Title: 25-HC promotes hepatocellular carcinoma metastasis through up-regulation of TLR4 dependent FABP4

doi:

Figure Lengend Snippet: 25-HC increases FABP4 expression which could directly enhance HepG2 cells migration. A. HepG2 cells were treated with the indicated concentrations of 25-HC for 24 hours before mRNA or protein was extracted to determine the expression of FABP4 by RT-qPCR or Western blotting, respectively. B. HepG2 cells were treated with the indicated concentrations of FABP4 (0, 20, 40 and 100 ng/mL) for 24 hours before mRNA or protein was extracted. The mRNA expressions of MMP2 and MMP9 were examined by RT-qPCR and the protein expressions of MMP1, MMP2, MMP3, MMP9 were detected by Western blotting, respectively. C. Migration assay of HepG2 cells after stimulation of FABP4 for 36 hours was performed. Results were obtained from 3 independent experiments and are expressed as the means ± SEM. Statistical significance was determined by one-way ANOVA followed by Dunnett’s test. ns, not significant, *P<0.05, **P<0.01, ***P<0.001.

Article Snippet: Recombinant human FABP4 was bought from Cloud-Clone Corp. (Houston, TX, USA) and dissolved in PBS.

Techniques: Expressing, Migration, Quantitative RT-PCR, Western Blot

Inhibition of FABP4 decreases the promotive effects of 25-HC on HepG2 cells migration. A. HepG2 cells were transfected with siNC or siFABP4 and CCK-8 assay was performed. Results are shown as the cells absorbance at 450 nm. HepG2 cells were transfected with siNC or siFABP4 for 24 hours before cells were treated with 25-HC at 10 μM. 36 hours later, migratory ability of HepG2 cells was determined by Transwell assay. Or 24 hours later, cells were collected for mRNA or protein extraction to determine the expressions of MMPs by RT-qPCR or Western blotting, respectively. B. HepG2 cells were stimulated with 10 μM 25-HC with or without 30 μM BMS-309403. 36 hours later, migration assay was performed. Or 24 hours later, cells were collected for mRNA or protein extraction to determine the expressions of MMPs by RT-qPCR or Western blotting, respectively. C. HepG2 cells were transfected with siNC or siTLR4 for 24 hours before 25-HC treatment. 24 hours later, the mRNA and protein expression of FABP4 was assessed by RT-qPCR and Western blotting, respectively. Results were obtained from 3 independent experiments and are expressed as the means ± SEM. Statistical significance was determined by Student’s t-test. *P<0.05, **P<0.01, ***P<0.001.

Journal: American Journal of Cancer Research

Article Title: 25-HC promotes hepatocellular carcinoma metastasis through up-regulation of TLR4 dependent FABP4

doi:

Figure Lengend Snippet: Inhibition of FABP4 decreases the promotive effects of 25-HC on HepG2 cells migration. A. HepG2 cells were transfected with siNC or siFABP4 and CCK-8 assay was performed. Results are shown as the cells absorbance at 450 nm. HepG2 cells were transfected with siNC or siFABP4 for 24 hours before cells were treated with 25-HC at 10 μM. 36 hours later, migratory ability of HepG2 cells was determined by Transwell assay. Or 24 hours later, cells were collected for mRNA or protein extraction to determine the expressions of MMPs by RT-qPCR or Western blotting, respectively. B. HepG2 cells were stimulated with 10 μM 25-HC with or without 30 μM BMS-309403. 36 hours later, migration assay was performed. Or 24 hours later, cells were collected for mRNA or protein extraction to determine the expressions of MMPs by RT-qPCR or Western blotting, respectively. C. HepG2 cells were transfected with siNC or siTLR4 for 24 hours before 25-HC treatment. 24 hours later, the mRNA and protein expression of FABP4 was assessed by RT-qPCR and Western blotting, respectively. Results were obtained from 3 independent experiments and are expressed as the means ± SEM. Statistical significance was determined by Student’s t-test. *P<0.05, **P<0.01, ***P<0.001.

Article Snippet: Recombinant human FABP4 was bought from Cloud-Clone Corp. (Houston, TX, USA) and dissolved in PBS.

Techniques: Inhibition, Migration, Transfection, CCK-8 Assay, Transwell Assay, Protein Extraction, Quantitative RT-PCR, Western Blot, Expressing

Inhibition of FABP4 decreases the 25-HC-induced HepG2 cells intrahepatic and abdominal metastasis. BALB/C nude mice were intrahepatic inoculation of 5 × 106 HepG2 cells followed by intraperitoneally injection with PBS or 25-HC (10 mg/kg) or 25-HC with BMS-309403 (45 mg/kg). At the end of the experiment, mice were sacrificed, (A) livers were removed and imaged. (B) The number of abdominal metastasis was counted, and body weight was recorded. Results were obtained from 3 independent experiments and are expressed as the means ± SEM. Statistical significance was determined by Student’s t-test, **P<0.01. ns: no significant.

Journal: American Journal of Cancer Research

Article Title: 25-HC promotes hepatocellular carcinoma metastasis through up-regulation of TLR4 dependent FABP4

doi:

Figure Lengend Snippet: Inhibition of FABP4 decreases the 25-HC-induced HepG2 cells intrahepatic and abdominal metastasis. BALB/C nude mice were intrahepatic inoculation of 5 × 106 HepG2 cells followed by intraperitoneally injection with PBS or 25-HC (10 mg/kg) or 25-HC with BMS-309403 (45 mg/kg). At the end of the experiment, mice were sacrificed, (A) livers were removed and imaged. (B) The number of abdominal metastasis was counted, and body weight was recorded. Results were obtained from 3 independent experiments and are expressed as the means ± SEM. Statistical significance was determined by Student’s t-test, **P<0.01. ns: no significant.

Article Snippet: Recombinant human FABP4 was bought from Cloud-Clone Corp. (Houston, TX, USA) and dissolved in PBS.

Techniques: Inhibition, Injection

FABP4 was up-regulated in HCC tissues. (A) The mRNA expression of FABP4 in hepatocellular carcinoma and normal tissues (GEPIA). T, tumor tissues, N, normal tissues. (B) DNA copy number of FABP4 in hepatocellular carcinoma from The Cancer Genome Atlas (TCGA). (C) The expression of FABP4 in hepatocellular carcinoma cell lines (EMBL-EBI). (D) FABP4 transcription in subgroups of patients with hepatocellular carcinoma, stratified based on gender, age, weight, race, tumor grade and cancer stages (UALCAN). (E) Correlation between FABP4 expression and the prognosis of patients with hepatocellular carcinoma (OncoLnc). Data are expressed as the means ± SEM. Statistical significance was determined by Student’s t-test (A and B) or one-way ANOVA followed by Dunnett’s test (D). *P<0.05, **P<0.01, ***P<0.001.

Journal: American Journal of Cancer Research

Article Title: 25-HC promotes hepatocellular carcinoma metastasis through up-regulation of TLR4 dependent FABP4

doi:

Figure Lengend Snippet: FABP4 was up-regulated in HCC tissues. (A) The mRNA expression of FABP4 in hepatocellular carcinoma and normal tissues (GEPIA). T, tumor tissues, N, normal tissues. (B) DNA copy number of FABP4 in hepatocellular carcinoma from The Cancer Genome Atlas (TCGA). (C) The expression of FABP4 in hepatocellular carcinoma cell lines (EMBL-EBI). (D) FABP4 transcription in subgroups of patients with hepatocellular carcinoma, stratified based on gender, age, weight, race, tumor grade and cancer stages (UALCAN). (E) Correlation between FABP4 expression and the prognosis of patients with hepatocellular carcinoma (OncoLnc). Data are expressed as the means ± SEM. Statistical significance was determined by Student’s t-test (A and B) or one-way ANOVA followed by Dunnett’s test (D). *P<0.05, **P<0.01, ***P<0.001.

Article Snippet: Recombinant human FABP4 was bought from Cloud-Clone Corp. (Houston, TX, USA) and dissolved in PBS.

Techniques: Expressing