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recombinant mouse leptin  (R&D Systems)


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    Structured Review

    R&D Systems recombinant mouse leptin
    Recombinant Mouse Leptin, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 162 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/recombinant mouse leptin/product/R&D Systems
    Average 95 stars, based on 162 article reviews
    recombinant mouse leptin - by Bioz Stars, 2026-06
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    Molecular docking models of Astragaloside IV (AS-IV) binding to the core targets. Representative binding poses of AS-IV (shown in stick representation) within the predicted binding pockets of the key target proteins. The calculated binding free energy (kcal/mol) for each complex is indicated. (A) Il22ra2 (−10.2 kcal/mol), (B) Ptgs2 (−9.5 kcal/mol), (C) Wnt1 (−9.3 kcal/mol), <t>(D)</t> <t>Igfbp2</t> (−8.4 kcal/mol), (E) GZMB (−8.2 kcal/mol), (F) <t>Lep</t> (−7.8 kcal/mol), (G) Gfap (−7.8 kcal/mol), (H) Wnt10a (−7.7 kcal/mol). These results demonstrate stable binding interactions between the therapeutic compound AS-IV and all eight core targets identified from the PPI network and WGCNA, with Il22ra2 and Ptgs2 showing the strongest binding affinity.
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    Molecular docking models of Astragaloside IV (AS-IV) binding to the core targets. Representative binding poses of AS-IV (shown in stick representation) within the predicted binding pockets of the key target proteins. The calculated binding free energy (kcal/mol) for each complex is indicated. (A) Il22ra2 (−10.2 kcal/mol), (B) Ptgs2 (−9.5 kcal/mol), (C) Wnt1 (−9.3 kcal/mol), <t>(D)</t> <t>Igfbp2</t> (−8.4 kcal/mol), (E) GZMB (−8.2 kcal/mol), (F) <t>Lep</t> (−7.8 kcal/mol), (G) Gfap (−7.8 kcal/mol), (H) Wnt10a (−7.7 kcal/mol). These results demonstrate stable binding interactions between the therapeutic compound AS-IV and all eight core targets identified from the PPI network and WGCNA, with Il22ra2 and Ptgs2 showing the strongest binding affinity.
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    Molecular docking models of Astragaloside IV (AS-IV) binding to the core targets. Representative binding poses of AS-IV (shown in stick representation) within the predicted binding pockets of the key target proteins. The calculated binding free energy (kcal/mol) for each complex is indicated. (A) Il22ra2 (−10.2 kcal/mol), (B) Ptgs2 (−9.5 kcal/mol), (C) Wnt1 (−9.3 kcal/mol), <t>(D)</t> <t>Igfbp2</t> (−8.4 kcal/mol), (E) GZMB (−8.2 kcal/mol), (F) <t>Lep</t> (−7.8 kcal/mol), (G) Gfap (−7.8 kcal/mol), (H) Wnt10a (−7.7 kcal/mol). These results demonstrate stable binding interactions between the therapeutic compound AS-IV and all eight core targets identified from the PPI network and WGCNA, with Il22ra2 and Ptgs2 showing the strongest binding affinity.
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    Molecular docking models of Astragaloside IV (AS-IV) binding to the core targets. Representative binding poses of AS-IV (shown in stick representation) within the predicted binding pockets of the key target proteins. The calculated binding free energy (kcal/mol) for each complex is indicated. (A) Il22ra2 (−10.2 kcal/mol), (B) Ptgs2 (−9.5 kcal/mol), (C) Wnt1 (−9.3 kcal/mol), <t>(D)</t> <t>Igfbp2</t> (−8.4 kcal/mol), (E) GZMB (−8.2 kcal/mol), (F) <t>Lep</t> (−7.8 kcal/mol), (G) Gfap (−7.8 kcal/mol), (H) Wnt10a (−7.7 kcal/mol). These results demonstrate stable binding interactions between the therapeutic compound AS-IV and all eight core targets identified from the PPI network and WGCNA, with Il22ra2 and Ptgs2 showing the strongest binding affinity.
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    Quantification of fatty acid uptake in the RV. ( A ) BODIPY staining of FA in the RV showed no difference <t>between</t> <t>db/db</t> and WT mice. Representative images of BODIPY stained RV sections. ( B ) Quantification of the cardiomyocyte fatty acid transporter, CD36 was lower in the db/db RV compared to the WT. ( C ) CD36 quantification by western blot showed no difference in the db/db RV. Representative western blots. ( D ) Membrane localization of CD36 showed downregulation in db/db RV. ( E ) Gene expression of FATP6 was upregulated in the db/db RV. ( F ) Protein expression by western blot showed higher FATP6 expression in the db/db RV. Representative western blots of FATP6 and caveolin. ( G ) Protein localization of FATP6 at the membrane was higher in the db/db RV compared to WT. ( H ) Quantification of enzymes involved in fatty acid oxidation. Acyl CoA dehydrogenases long chain and medium chain (ACADl, ACADm, ACS1) and acyl CoA synthetases 1 (ACS1). ACADl was lower in the db/db RV, mACADm and ACS1 were unchanged in the db/db RV. * p < 0.05 by Student’s t-test. n = 4/group. Scale bar: 50 µm
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    Quantification of fatty acid uptake in the RV. ( A ) BODIPY staining of FA in the RV showed no difference <t>between</t> <t>db/db</t> and WT mice. Representative images of BODIPY stained RV sections. ( B ) Quantification of the cardiomyocyte fatty acid transporter, CD36 was lower in the db/db RV compared to the WT. ( C ) CD36 quantification by western blot showed no difference in the db/db RV. Representative western blots. ( D ) Membrane localization of CD36 showed downregulation in db/db RV. ( E ) Gene expression of FATP6 was upregulated in the db/db RV. ( F ) Protein expression by western blot showed higher FATP6 expression in the db/db RV. Representative western blots of FATP6 and caveolin. ( G ) Protein localization of FATP6 at the membrane was higher in the db/db RV compared to WT. ( H ) Quantification of enzymes involved in fatty acid oxidation. Acyl CoA dehydrogenases long chain and medium chain (ACADl, ACADm, ACS1) and acyl CoA synthetases 1 (ACS1). ACADl was lower in the db/db RV, mACADm and ACS1 were unchanged in the db/db RV. * p < 0.05 by Student’s t-test. n = 4/group. Scale bar: 50 µm
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    Quantification of fatty acid uptake in the RV. ( A ) BODIPY staining of FA in the RV showed no difference <t>between</t> <t>db/db</t> and WT mice. Representative images of BODIPY stained RV sections. ( B ) Quantification of the cardiomyocyte fatty acid transporter, CD36 was lower in the db/db RV compared to the WT. ( C ) CD36 quantification by western blot showed no difference in the db/db RV. Representative western blots. ( D ) Membrane localization of CD36 showed downregulation in db/db RV. ( E ) Gene expression of FATP6 was upregulated in the db/db RV. ( F ) Protein expression by western blot showed higher FATP6 expression in the db/db RV. Representative western blots of FATP6 and caveolin. ( G ) Protein localization of FATP6 at the membrane was higher in the db/db RV compared to WT. ( H ) Quantification of enzymes involved in fatty acid oxidation. Acyl CoA dehydrogenases long chain and medium chain (ACADl, ACADm, ACS1) and acyl CoA synthetases 1 (ACS1). ACADl was lower in the db/db RV, mACADm and ACS1 were unchanged in the db/db RV. * p < 0.05 by Student’s t-test. n = 4/group. Scale bar: 50 µm
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    Image Search Results


    Molecular docking models of Astragaloside IV (AS-IV) binding to the core targets. Representative binding poses of AS-IV (shown in stick representation) within the predicted binding pockets of the key target proteins. The calculated binding free energy (kcal/mol) for each complex is indicated. (A) Il22ra2 (−10.2 kcal/mol), (B) Ptgs2 (−9.5 kcal/mol), (C) Wnt1 (−9.3 kcal/mol), (D) Igfbp2 (−8.4 kcal/mol), (E) GZMB (−8.2 kcal/mol), (F) Lep (−7.8 kcal/mol), (G) Gfap (−7.8 kcal/mol), (H) Wnt10a (−7.7 kcal/mol). These results demonstrate stable binding interactions between the therapeutic compound AS-IV and all eight core targets identified from the PPI network and WGCNA, with Il22ra2 and Ptgs2 showing the strongest binding affinity.

    Journal: Frontiers in Nutrition

    Article Title: Astragaloside IV modulates oxidative stress and osteoimmune–Wnt signaling in ovariectomized rats: an integrated study of RNA sequencing, molecular docking, and experimental validation

    doi: 10.3389/fnut.2026.1785452

    Figure Lengend Snippet: Molecular docking models of Astragaloside IV (AS-IV) binding to the core targets. Representative binding poses of AS-IV (shown in stick representation) within the predicted binding pockets of the key target proteins. The calculated binding free energy (kcal/mol) for each complex is indicated. (A) Il22ra2 (−10.2 kcal/mol), (B) Ptgs2 (−9.5 kcal/mol), (C) Wnt1 (−9.3 kcal/mol), (D) Igfbp2 (−8.4 kcal/mol), (E) GZMB (−8.2 kcal/mol), (F) Lep (−7.8 kcal/mol), (G) Gfap (−7.8 kcal/mol), (H) Wnt10a (−7.7 kcal/mol). These results demonstrate stable binding interactions between the therapeutic compound AS-IV and all eight core targets identified from the PPI network and WGCNA, with Il22ra2 and Ptgs2 showing the strongest binding affinity.

    Article Snippet: Primary antibodies diluted in antibody diluent were applied and incubated at 4 °C overnight; the primary antibodies were as follows: PTGS2 (ABclonal, A3560, rabbit, 1:200), IGFBP2 (Proteintech, 66,644-1-IG, mouse, 1:200), WNT1 (ABclonal, A2475, rabbit, 1:200), LEP (bioss, bs-0409R, rabbit, 1:200), GFAP (Proteintech, 60,190-1-IG, mouse, 1:1000), β -catenin (huilanbio, ABB3523, rabbit, 1:200), and NF-κB p65 (Cell Signaling Technology, 8,242, rabbit, 1:200), with EDTA-based retrieval used for all targets.

    Techniques: Binding Assay

    Multiplex immunofluorescence imaging and semi-quantification of target proteins in femoral trabecular bone. Representative multiplex immunofluorescence images showing DAPI (nuclei), target protein staining, and merged overlays in the femoral trabecular region from Sham, OVX, and OVX-AS-IV-M treated rats. Panels show staining for (A) NF-κB p65, (B) Wnt1, (C) Gfap, (D) β-catenin, (E) Igfbp2, (F) Lep, and (G) Ptgs2. Scale bar, 50 μm. The corresponding semi-quantification of mean fluorescence intensity (MFI) for each marker is presented to the right of each image panel, normalized to the Sham group (set to 1). Data are presented as mean ± SD with individual data points overlaid. Statistical comparisons were performed using one-way ANOVA followed by Dunnett’s multiple-comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Journal: Frontiers in Nutrition

    Article Title: Astragaloside IV modulates oxidative stress and osteoimmune–Wnt signaling in ovariectomized rats: an integrated study of RNA sequencing, molecular docking, and experimental validation

    doi: 10.3389/fnut.2026.1785452

    Figure Lengend Snippet: Multiplex immunofluorescence imaging and semi-quantification of target proteins in femoral trabecular bone. Representative multiplex immunofluorescence images showing DAPI (nuclei), target protein staining, and merged overlays in the femoral trabecular region from Sham, OVX, and OVX-AS-IV-M treated rats. Panels show staining for (A) NF-κB p65, (B) Wnt1, (C) Gfap, (D) β-catenin, (E) Igfbp2, (F) Lep, and (G) Ptgs2. Scale bar, 50 μm. The corresponding semi-quantification of mean fluorescence intensity (MFI) for each marker is presented to the right of each image panel, normalized to the Sham group (set to 1). Data are presented as mean ± SD with individual data points overlaid. Statistical comparisons were performed using one-way ANOVA followed by Dunnett’s multiple-comparisons test. * p < 0.05, ** p < 0.01, *** p < 0.001.

    Article Snippet: Primary antibodies diluted in antibody diluent were applied and incubated at 4 °C overnight; the primary antibodies were as follows: PTGS2 (ABclonal, A3560, rabbit, 1:200), IGFBP2 (Proteintech, 66,644-1-IG, mouse, 1:200), WNT1 (ABclonal, A2475, rabbit, 1:200), LEP (bioss, bs-0409R, rabbit, 1:200), GFAP (Proteintech, 60,190-1-IG, mouse, 1:1000), β -catenin (huilanbio, ABB3523, rabbit, 1:200), and NF-κB p65 (Cell Signaling Technology, 8,242, rabbit, 1:200), with EDTA-based retrieval used for all targets.

    Techniques: Multiplex Assay, Immunofluorescence, Imaging, Staining, Fluorescence, Marker

    Quantification of fatty acid uptake in the RV. ( A ) BODIPY staining of FA in the RV showed no difference between db/db and WT mice. Representative images of BODIPY stained RV sections. ( B ) Quantification of the cardiomyocyte fatty acid transporter, CD36 was lower in the db/db RV compared to the WT. ( C ) CD36 quantification by western blot showed no difference in the db/db RV. Representative western blots. ( D ) Membrane localization of CD36 showed downregulation in db/db RV. ( E ) Gene expression of FATP6 was upregulated in the db/db RV. ( F ) Protein expression by western blot showed higher FATP6 expression in the db/db RV. Representative western blots of FATP6 and caveolin. ( G ) Protein localization of FATP6 at the membrane was higher in the db/db RV compared to WT. ( H ) Quantification of enzymes involved in fatty acid oxidation. Acyl CoA dehydrogenases long chain and medium chain (ACADl, ACADm, ACS1) and acyl CoA synthetases 1 (ACS1). ACADl was lower in the db/db RV, mACADm and ACS1 were unchanged in the db/db RV. * p < 0.05 by Student’s t-test. n = 4/group. Scale bar: 50 µm

    Journal: Cardiovascular diabetology. Endocrinology reports

    Article Title: Diabetes-induced right ventricular remodeling precedes left ventricular remodeling and occurs via a distinct fatty acid uptake pathway

    doi: 10.1186/s40842-026-00287-3

    Figure Lengend Snippet: Quantification of fatty acid uptake in the RV. ( A ) BODIPY staining of FA in the RV showed no difference between db/db and WT mice. Representative images of BODIPY stained RV sections. ( B ) Quantification of the cardiomyocyte fatty acid transporter, CD36 was lower in the db/db RV compared to the WT. ( C ) CD36 quantification by western blot showed no difference in the db/db RV. Representative western blots. ( D ) Membrane localization of CD36 showed downregulation in db/db RV. ( E ) Gene expression of FATP6 was upregulated in the db/db RV. ( F ) Protein expression by western blot showed higher FATP6 expression in the db/db RV. Representative western blots of FATP6 and caveolin. ( G ) Protein localization of FATP6 at the membrane was higher in the db/db RV compared to WT. ( H ) Quantification of enzymes involved in fatty acid oxidation. Acyl CoA dehydrogenases long chain and medium chain (ACADl, ACADm, ACS1) and acyl CoA synthetases 1 (ACS1). ACADl was lower in the db/db RV, mACADm and ACS1 were unchanged in the db/db RV. * p < 0.05 by Student’s t-test. n = 4/group. Scale bar: 50 µm

    Article Snippet: Male and female 6–8 week old leptin receptor mutant (db/db) that are homozygous for a spontaneous mutation in the leptin receptor [ ] and heterozygote lean littermates (wild type, WT) were ordered from Jackson Laboratories (#00697).

    Techniques: Staining, Western Blot, Membrane, Gene Expression, Expressing

    RV remodeling in 8–10 week old db/db mice. ( A ) RV weight normalized to tibia length (TL) was higher compared to WT. ( B ) RV anterior wall (RVAW) thickness was higher in diastole in the db/db mice compared to the WT and trended towards significance during systole. ( C ) RV myocyte cross-sectional area (CSA) remained the same in the db/db RV, n = 20. Representative images of lectin staining. ( D ) Quantification of fibrosis by picrosirius red staining showed higher collagen in the db/db RV compared to WT. Representative images of PSR staining. ( F ) Quantification of lipid accumulation by oil red O staining showed higher lipid accumulation in the db/db RV compared to the WT. Representative images of oil red O staining. * p < 0.05 by Student’s t-test. For oil red O and picrosirius red staining, n = 3 with at least three views quantified per image. Scale bar: 50 µm

    Journal: Cardiovascular diabetology. Endocrinology reports

    Article Title: Diabetes-induced right ventricular remodeling precedes left ventricular remodeling and occurs via a distinct fatty acid uptake pathway

    doi: 10.1186/s40842-026-00287-3

    Figure Lengend Snippet: RV remodeling in 8–10 week old db/db mice. ( A ) RV weight normalized to tibia length (TL) was higher compared to WT. ( B ) RV anterior wall (RVAW) thickness was higher in diastole in the db/db mice compared to the WT and trended towards significance during systole. ( C ) RV myocyte cross-sectional area (CSA) remained the same in the db/db RV, n = 20. Representative images of lectin staining. ( D ) Quantification of fibrosis by picrosirius red staining showed higher collagen in the db/db RV compared to WT. Representative images of PSR staining. ( F ) Quantification of lipid accumulation by oil red O staining showed higher lipid accumulation in the db/db RV compared to the WT. Representative images of oil red O staining. * p < 0.05 by Student’s t-test. For oil red O and picrosirius red staining, n = 3 with at least three views quantified per image. Scale bar: 50 µm

    Article Snippet: Male and female 6–8 week old leptin receptor mutant (db/db) that are homozygous for a spontaneous mutation in the leptin receptor [ ] and heterozygote lean littermates (wild type, WT) were ordered from Jackson Laboratories (#00697).

    Techniques: Staining

    Functional assessment of RV remodeling in T2D mice by echocardiography. ( A ) Representative images from M-mode echocardiography comparing WT and db/db RV. ( B ) RV FAC was lower in the db/db RV alongside ( C ) lower PA-VTI, suggestive of impaired systolic function. ( D ) RV E/e’ was higher in the db/db RV. ( E ) Representative images from M-mode echocardiography comparing Con and T2D RV. ( F ) Lower RV FAC and ( G ) TAPSE in T2D compared to the Con were indicative of impaired RV systolic function. * p < 0.05 by Student’s t-test. n = 5–11 per group

    Journal: Cardiovascular diabetology. Endocrinology reports

    Article Title: Diabetes-induced right ventricular remodeling precedes left ventricular remodeling and occurs via a distinct fatty acid uptake pathway

    doi: 10.1186/s40842-026-00287-3

    Figure Lengend Snippet: Functional assessment of RV remodeling in T2D mice by echocardiography. ( A ) Representative images from M-mode echocardiography comparing WT and db/db RV. ( B ) RV FAC was lower in the db/db RV alongside ( C ) lower PA-VTI, suggestive of impaired systolic function. ( D ) RV E/e’ was higher in the db/db RV. ( E ) Representative images from M-mode echocardiography comparing Con and T2D RV. ( F ) Lower RV FAC and ( G ) TAPSE in T2D compared to the Con were indicative of impaired RV systolic function. * p < 0.05 by Student’s t-test. n = 5–11 per group

    Article Snippet: Male and female 6–8 week old leptin receptor mutant (db/db) that are homozygous for a spontaneous mutation in the leptin receptor [ ] and heterozygote lean littermates (wild type, WT) were ordered from Jackson Laboratories (#00697).

    Techniques: Functional Assay