h fabp Search Results


human h fabp elisa kit  (Hycult Biotech)
92
Hycult Biotech human h fabp elisa kit
Human H Fabp Elisa Kit, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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fabp3  (R&D Systems)
91
R&D Systems fabp3
GRE-transcriptional activity of GR in the absence or presence of FABP1, FABP2, <t>FABP3,</t> FABP4 or FABP5 in response to vehicle control or increasing concentrations of (A) hydrocortisone (B) dexamethasone or (C) prednisolone, was assessed using a reporter gene in COS-7 cells after 24 h treatment (n=3). (D) Expression of the GR in naïve COS-7 cells or following transfection with GR determined by immunoblotting. Transcriptional activity of the endogenous or transfected GR in the presence of FABP4 in response to (E) dexamethasone or (F) prednisolone (n=3). (G) FABP translocation to the nucleus in COS-7 cells transfected with GR and GFP-FABP1 or GFP-FABP4 following 24 h treatment with vehicle or an EC 80 concentration of hydrocortisone, dexamethasone or prednisolone (n=3). Data are mean ± SEM from n independent experiments, as stated. For concentration-response curves, symbols show means and error bars, S.E.M. *** p<0.001, two-way ANOVA with Sidak’s multiple comparison test. For bar graphs, bars show the mean, error bars the S.E.M. and symbols show the independent data points for each experiment. *** p<0.001, two-way ANOVA with Dunnett’s multiple comparisons test.
Fabp3, supplied by R&D Systems, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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western blotting fabp3 proteintech  (Proteintech)
93
Proteintech western blotting fabp3 proteintech
GRE-transcriptional activity of GR in the absence or presence of FABP1, FABP2, <t>FABP3,</t> FABP4 or FABP5 in response to vehicle control or increasing concentrations of (A) hydrocortisone (B) dexamethasone or (C) prednisolone, was assessed using a reporter gene in COS-7 cells after 24 h treatment (n=3). (D) Expression of the GR in naïve COS-7 cells or following transfection with GR determined by immunoblotting. Transcriptional activity of the endogenous or transfected GR in the presence of FABP4 in response to (E) dexamethasone or (F) prednisolone (n=3). (G) FABP translocation to the nucleus in COS-7 cells transfected with GR and GFP-FABP1 or GFP-FABP4 following 24 h treatment with vehicle or an EC 80 concentration of hydrocortisone, dexamethasone or prednisolone (n=3). Data are mean ± SEM from n independent experiments, as stated. For concentration-response curves, symbols show means and error bars, S.E.M. *** p<0.001, two-way ANOVA with Sidak’s multiple comparison test. For bar graphs, bars show the mean, error bars the S.E.M. and symbols show the independent data points for each experiment. *** p<0.001, two-way ANOVA with Dunnett’s multiple comparisons test.
Western Blotting Fabp3 Proteintech, 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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fabp3 nm 010174 mouse tagged orf  (OriGene)
91
OriGene fabp3 nm 010174 mouse tagged orf
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Fabp3 Nm 010174 Mouse Tagged Orf, supplied by OriGene, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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protein 3 fabp 3 polyclonal antibody  (R&D Systems)
90
R&D Systems protein 3 fabp 3 polyclonal antibody
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Protein 3 Fabp 3 Polyclonal Antibody, supplied by R&D Systems, 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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mouse monoclonal antibodies against fabp3  (Hycult Biotech)
90
Hycult Biotech mouse monoclonal antibodies against fabp3
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Mouse Monoclonal Antibodies Against Fabp3, supplied by Hycult Biotech, 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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elisa hk402  (Hycult Biotech)
92
Hycult Biotech elisa hk402
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Elisa Hk402, supplied by Hycult Biotech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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inhibitory mouse anti  (Bio-Rad)
91
Bio-Rad inhibitory mouse anti
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Inhibitory Mouse Anti, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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fatty acid binding protein 3 fabp3 antibody affinity changzhou china  (Boster Bio)
93
Boster Bio fatty acid binding protein 3 fabp3 antibody affinity changzhou china
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Fatty Acid Binding Protein 3 Fabp3 Antibody Affinity Changzhou China, supplied by Boster Bio, 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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fabp3 boster bio anti cardiac fabp fabp3 antibody picobandtm  (Boster Bio)
93
Boster Bio fabp3 boster bio anti cardiac fabp fabp3 antibody picobandtm
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Fabp3 Boster Bio Anti Cardiac Fabp Fabp3 Antibody Picobandtm, supplied by Boster Bio, 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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rat h fabp elisa kit  (Hycult Biotech)
93
Hycult Biotech rat h fabp elisa kit
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Rat H Fabp Elisa Kit, supplied by Hycult Biotech, 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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anti human monoclonal antibody h fabp 67d3  (Hycult Biotech)
90
Hycult Biotech anti human monoclonal antibody h fabp 67d3
( A ) Structure of heart-type fatty acid-binding protein <t>(FABP3,</t> PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.
Anti Human Monoclonal Antibody H Fabp 67d3, supplied by Hycult Biotech, 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


GRE-transcriptional activity of GR in the absence or presence of FABP1, FABP2, FABP3, FABP4 or FABP5 in response to vehicle control or increasing concentrations of (A) hydrocortisone (B) dexamethasone or (C) prednisolone, was assessed using a reporter gene in COS-7 cells after 24 h treatment (n=3). (D) Expression of the GR in naïve COS-7 cells or following transfection with GR determined by immunoblotting. Transcriptional activity of the endogenous or transfected GR in the presence of FABP4 in response to (E) dexamethasone or (F) prednisolone (n=3). (G) FABP translocation to the nucleus in COS-7 cells transfected with GR and GFP-FABP1 or GFP-FABP4 following 24 h treatment with vehicle or an EC 80 concentration of hydrocortisone, dexamethasone or prednisolone (n=3). Data are mean ± SEM from n independent experiments, as stated. For concentration-response curves, symbols show means and error bars, S.E.M. *** p<0.001, two-way ANOVA with Sidak’s multiple comparison test. For bar graphs, bars show the mean, error bars the S.E.M. and symbols show the independent data points for each experiment. *** p<0.001, two-way ANOVA with Dunnett’s multiple comparisons test.

Journal: bioRxiv

Article Title: Fatty acid binding proteins shape the cellular response to activation of the glucocorticoid receptor

doi: 10.1101/2021.07.02.450968

Figure Lengend Snippet: GRE-transcriptional activity of GR in the absence or presence of FABP1, FABP2, FABP3, FABP4 or FABP5 in response to vehicle control or increasing concentrations of (A) hydrocortisone (B) dexamethasone or (C) prednisolone, was assessed using a reporter gene in COS-7 cells after 24 h treatment (n=3). (D) Expression of the GR in naïve COS-7 cells or following transfection with GR determined by immunoblotting. Transcriptional activity of the endogenous or transfected GR in the presence of FABP4 in response to (E) dexamethasone or (F) prednisolone (n=3). (G) FABP translocation to the nucleus in COS-7 cells transfected with GR and GFP-FABP1 or GFP-FABP4 following 24 h treatment with vehicle or an EC 80 concentration of hydrocortisone, dexamethasone or prednisolone (n=3). Data are mean ± SEM from n independent experiments, as stated. For concentration-response curves, symbols show means and error bars, S.E.M. *** p<0.001, two-way ANOVA with Sidak’s multiple comparison test. For bar graphs, bars show the mean, error bars the S.E.M. and symbols show the independent data points for each experiment. *** p<0.001, two-way ANOVA with Dunnett’s multiple comparisons test.

Article Snippet: Immunoblotting used primary antibodies recognising FABP1 (Abcam (AB76812; rabbit, 1:300), FABP2 (gift from Dr Satoshi Kaiura, Dainippon Sumi-tomo Pharma Co. Ltd., Osaka, Japan; mouse; 1:400), FABP3 (R&D Systems MAB1678; rabbit, 1:200), FABP4 (Abcam AB92501; rabbit, 1:1000), FABP5 (Abcam AB37267; rabbit, 1:200), GR (Abcam AB183127; rabbit, 1:400) or β-actin (Cell Signaling Technology 3700S; mouse, 1:5000).

Techniques: Activity Assay, Control, Expressing, Transfection, Western Blot, Translocation Assay, Concentration Assay, Comparison

( A ) Structure of heart-type fatty acid-binding protein (FABP3, PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: ( A ) Structure of heart-type fatty acid-binding protein (FABP3, PDB ID 3WVM ) in complex with palmitate (C16:0). Protein structure is represented as ribbons and colored according to the secondary structure elements as follows: α-helixes shown in orange, β-sheets in cyan, and loops in gray. C16:0 is shown as dark blue sticks, while residues involved in ligand and water cluster binding are shown as light gray balls and sticks. Water molecules (red spheres) and hydrogen bonds (yellow dashed lines) are shown. ( B ) Human FABP3 amino acid sequence. Residues colored in yellow were not assigned from the NMR spectra either for the apo-form or for the holo-form, while residues in cyan were not assigned only for complexes of FABP3 with acylcarnitines (ACs). Crosspeaks for residues colored in gray were not observed in any 2D 1 H- N HSQC spectra. The black arrow points to the position of the TEV cleavage site. ( C ) Assigned 2D 1 H- N HSQC spectra of human apo-FABP3 in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). His-tagged FABP3 (noncleaved) is shown in blue, and cleaved FABP3 is shown in red. Backbone amide resonances are denoted as one letter symbol and residue number according to the sequence in B. Labels for the residues from the His-tag are shown in light blue. Side chain amide resonances were not assigned. Residues are numbered according to UniProt ID P05413.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Binding Assay, Sequencing, Residue

Toxicity of C16:0-carnitine in PANC-1 cells after 4 h of incubation in the presence or in the absence of 60 μM heart-type fatty acid-binding protein (FABP3) in the cell media. Data are shown as the mean ± SEM of 3 independent experiments in at least 6 technical replicates. * indicates a significant difference compared to the cells not subjected to FABP3 treatment at the respective C16:0-carnitine concentration.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Toxicity of C16:0-carnitine in PANC-1 cells after 4 h of incubation in the presence or in the absence of 60 μM heart-type fatty acid-binding protein (FABP3) in the cell media. Data are shown as the mean ± SEM of 3 independent experiments in at least 6 technical replicates. * indicates a significant difference compared to the cells not subjected to FABP3 treatment at the respective C16:0-carnitine concentration.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Incubation, Binding Assay, Concentration Assay

Toxicity of C16:0-carnitine in native and heart-type fatty acid-binding protein (FABP3)-overexpressing PANC-1 cells after 4 h of incubation. Data are shown as the mean ± SEM of 3 independent experiments in at least 6 technical replicates. * indicates a significant difference compared to the native cells at the respective concentration of C16:0-carnitine.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Toxicity of C16:0-carnitine in native and heart-type fatty acid-binding protein (FABP3)-overexpressing PANC-1 cells after 4 h of incubation. Data are shown as the mean ± SEM of 3 independent experiments in at least 6 technical replicates. * indicates a significant difference compared to the native cells at the respective concentration of C16:0-carnitine.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Binding Assay, Incubation, Concentration Assay

Superposition of the 2D 1 H- 15 N HSQC spectra for ( A ) heart-type fatty acid-binding protein (FABP3)-C18:1(n-9) t and ( B ) FABP3-C18:1(n-9) t -carnitine complex in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). The spectrum of apo-FABP3—in blue, spectrum of the FABP3-ligand complex—in red. Residues with chemical shift perturbations (CSPs) larger than the mean plus one standard deviation are assigned and black arrows show the shift of the corresponding crosspeak. * marks the crosspeaks that have disappeared upon binding of the acylcarnitines (ACs).

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Superposition of the 2D 1 H- 15 N HSQC spectra for ( A ) heart-type fatty acid-binding protein (FABP3)-C18:1(n-9) t and ( B ) FABP3-C18:1(n-9) t -carnitine complex in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi). The spectrum of apo-FABP3—in blue, spectrum of the FABP3-ligand complex—in red. Residues with chemical shift perturbations (CSPs) larger than the mean plus one standard deviation are assigned and black arrows show the shift of the corresponding crosspeak. * marks the crosspeaks that have disappeared upon binding of the acylcarnitines (ACs).

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Binding Assay, Standard Deviation

Mapping of the chemical shift perturbations (CSPs) caused by binding of ( A ) C8:0, ( B ) C12:0, ( C ) C14:0, ( D ) C16:0, ( E ) C18:1(n-9) c , ( F ) C20:5(n-3) c , ( G ) C8:0-carnitine, ( H ) C12:0-carnitine, ( I ) C14:0-carnitine, ( J ) C16:0-carnitine, ( K ) C18:1(n-9) c -carnitine, or ( L ) C20:5(n-3) c -carnitine onto the heart-type fatty acid-binding protein (FABP3) structure. The CSPs are color-coded, in which red indicates larger shifts, while blue indicates no changes in the averaged δ H and δ N NMR chemical shifts. Unassigned or disappeared residues are colored in gray. FABP3 structure is taken from PDB ID 3WVM.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Mapping of the chemical shift perturbations (CSPs) caused by binding of ( A ) C8:0, ( B ) C12:0, ( C ) C14:0, ( D ) C16:0, ( E ) C18:1(n-9) c , ( F ) C20:5(n-3) c , ( G ) C8:0-carnitine, ( H ) C12:0-carnitine, ( I ) C14:0-carnitine, ( J ) C16:0-carnitine, ( K ) C18:1(n-9) c -carnitine, or ( L ) C20:5(n-3) c -carnitine onto the heart-type fatty acid-binding protein (FABP3) structure. The CSPs are color-coded, in which red indicates larger shifts, while blue indicates no changes in the averaged δ H and δ N NMR chemical shifts. Unassigned or disappeared residues are colored in gray. FABP3 structure is taken from PDB ID 3WVM.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Binding Assay

ITC results of the heart-type fatty acid-binding protein (FABP3) interaction with fatty acids (FAs) and acylcarnitines (ACs) in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi) at 25 °C.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: ITC results of the heart-type fatty acid-binding protein (FABP3) interaction with fatty acids (FAs) and acylcarnitines (ACs) in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi) at 25 °C.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques:

( A ) Superposition of the ITC titration curves of the heart-type fatty acid-binding protein (FABP3) interaction with C18:1(n-9) c in black and C18:1(n-9) c -carnitine in cyan. Both experiments were performed in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi) at 25 °C. Graphical representation of the thermodynamic binding parameters of the FABP3 interaction with ( B ) C18:1(n-9) c and ( C ) C18:1(n-9) c -carnitine.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: ( A ) Superposition of the ITC titration curves of the heart-type fatty acid-binding protein (FABP3) interaction with C18:1(n-9) c in black and C18:1(n-9) c -carnitine in cyan. Both experiments were performed in 20 mM K 2 HPO 4 /KH 2 PO 4 , 50 mM KCl buffer pH 7.6 (KPi) at 25 °C. Graphical representation of the thermodynamic binding parameters of the FABP3 interaction with ( B ) C18:1(n-9) c and ( C ) C18:1(n-9) c -carnitine.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Titration, Binding Assay

Superposition of the ITC thermograms for heart-type fatty acid-binding protein (FABP3) titrated with ( A ) C18:1(n-9) c and ( B ) C18:1(n-9) c -carnitine at three different temperatures: 16 (cyan), 25 (black), and 37 °C (red).

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Superposition of the ITC thermograms for heart-type fatty acid-binding protein (FABP3) titrated with ( A ) C18:1(n-9) c and ( B ) C18:1(n-9) c -carnitine at three different temperatures: 16 (cyan), 25 (black), and 37 °C (red).

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Binding Assay

Heat capacity change, Δ C p , and temperature dependence of the binding free energy, Δ G . ( A ) Δ C p values for four fatty acids (FAs) and corresponding acylcarnitines (ACs) binding to heart-type fatty acid-binding protein (FABP3). ( B ) Δ G of FA or AC binding to FABP3 within the temperature range from 0 to 100 °C.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Heat capacity change, Δ C p , and temperature dependence of the binding free energy, Δ G . ( A ) Δ C p values for four fatty acids (FAs) and corresponding acylcarnitines (ACs) binding to heart-type fatty acid-binding protein (FABP3). ( B ) Δ G of FA or AC binding to FABP3 within the temperature range from 0 to 100 °C.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Binding Assay

Comparison of the changes in the heat capacity, Δ C p , for the heart-type fatty acid-binding protein (FABP3)—ligand complexes.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Comparison of the changes in the heat capacity, Δ C p , for the heart-type fatty acid-binding protein (FABP3)—ligand complexes.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Comparison

Top. Competitive binding studies of heart-type fatty acid-binding protein (FABP3)-C18:1(n-9) t -carnitine and three fatty acids (FAs) of different chain lengths. ( A ) Reference titration of C18:1(n-9) t -carnitine to apo-FABP3. ( B ) FABP3-C8:0 complex titrated with C18:1(n-9) t -carnitine. ( C ) FABP3-C10:0 complex titrated with C18:1(n-9) t -carnitine. ( D ) FABP3-C18:1(n-9) t -carnitine complex titrated with C10:0. ( E ) FABP3-C18:1(n-9) t -carnitine complex titrated with C12:0. All experiments were performed in 20 mM K 2 HPO 4 /KH 2 PO 4 and 50 mM KCl buffer pH 7.6 (KPi) at 25 °C. Bottom. Schematic representation of ligand binding and competition. Protein is represented as the dark blue sector, acylcarnitines (ACs) as orange, and FAs as cyan circles. Green arrows indicate that the competition event between ligands was successful.

Journal: International Journal of Molecular Sciences

Article Title: Heart-Type Fatty Acid Binding Protein Binds Long-Chain Acylcarnitines and Protects against Lipotoxicity

doi: 10.3390/ijms24065528

Figure Lengend Snippet: Top. Competitive binding studies of heart-type fatty acid-binding protein (FABP3)-C18:1(n-9) t -carnitine and three fatty acids (FAs) of different chain lengths. ( A ) Reference titration of C18:1(n-9) t -carnitine to apo-FABP3. ( B ) FABP3-C8:0 complex titrated with C18:1(n-9) t -carnitine. ( C ) FABP3-C10:0 complex titrated with C18:1(n-9) t -carnitine. ( D ) FABP3-C18:1(n-9) t -carnitine complex titrated with C10:0. ( E ) FABP3-C18:1(n-9) t -carnitine complex titrated with C12:0. All experiments were performed in 20 mM K 2 HPO 4 /KH 2 PO 4 and 50 mM KCl buffer pH 7.6 (KPi) at 25 °C. Bottom. Schematic representation of ligand binding and competition. Protein is represented as the dark blue sector, acylcarnitines (ACs) as orange, and FAs as cyan circles. Green arrows indicate that the competition event between ligands was successful.

Article Snippet: The commercially available FuGENE ® HD transfection reagent (Promega Corporation, Madison, WI, USA) was mixed with the FABP3 (NM_010174) mouse tagged ORF clone plasmid (OriGene Technologies, Inc., Rockville, MD, USA) in a 4:1 ratio for transfection according to the manufacturer’s protocol.

Techniques: Binding Assay, Titration, Ligand Binding Assay