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antibody against human adiponectin  (Boster Bio)


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    Structured Review

    Boster Bio antibody against human adiponectin
    Fig. 1 Detection of serum <t>adiponectin</t> isoforms with monoclonal antibodies (mAbs) against recombinant human adiponectin. a Western blot to screen mAbs detecting different adiponectin isoforms. Human serum was loaded into each lane of the gel and resolved by polyacrylamide gel electrophoresis (PAGE) and then transferred to a membrane. Each lane of the membrane was then separately cut and incubated with each mAb from hybridoma culture supernatant. After the secondary antibody was probed, the cut membrane was combined to form one sheet and developed with ECL solution. Eleven different mAbs from culture supernatant were tested to investigate their recognition patterns of adiponectin isoforms in serum. The mAb KH7–33, in lane 3, was selected as a representative recognizing only the middle molecular weight (MMW) isoform of adiponectin. The mAb KH7–41, in lane 4, was selected as a representative recognizing both the MMW and low molecular weight (LMW) isoforms of adiponectin. The mAb KH4–8, in lane 8, was selected as a representative mAb recognizing both the MMW and HMW isoforms of adiponectin. b Comparison of the mAb recognition patterns of adiponectin isoforms in human, mouse, and rat sera by Western blot. Human, mouse, and rat sera were separated by sodium dodecyl sulfate–PAGE. All three mAbs (KH7–33, KH7–41, and KH4–8) recognized the rat and mouse adiponectin MMW isoform. Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. <t>PB9001)</t> or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011). Mouse and rat serum were obtained via heart puncture of male BALB/c mice and Sprague Dawley rats (8 weeks old), respectively. Human serum was obtained from a male volunteer (55 years old)
    Antibody Against Human Adiponectin, supplied by Boster Bio, 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/product/antibody+against+human+adiponectin/pm30376894-123-12-16?v=Boster+Bio
    Average 90 stars, based on 1 article reviews
    antibody against human adiponectin - by Bioz Stars, 2026-08
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    Images

    1) Product Images from "Potential therapeutic antibodies targeting specific adiponectin isoforms in rheumatoid arthritis."

    Article Title: Potential therapeutic antibodies targeting specific adiponectin isoforms in rheumatoid arthritis.

    Journal: Arthritis research & therapy

    doi: 10.1186/s13075-018-1736-3

    Fig. 1 Detection of serum adiponectin isoforms with monoclonal antibodies (mAbs) against recombinant human adiponectin. a Western blot to screen mAbs detecting different adiponectin isoforms. Human serum was loaded into each lane of the gel and resolved by polyacrylamide gel electrophoresis (PAGE) and then transferred to a membrane. Each lane of the membrane was then separately cut and incubated with each mAb from hybridoma culture supernatant. After the secondary antibody was probed, the cut membrane was combined to form one sheet and developed with ECL solution. Eleven different mAbs from culture supernatant were tested to investigate their recognition patterns of adiponectin isoforms in serum. The mAb KH7–33, in lane 3, was selected as a representative recognizing only the middle molecular weight (MMW) isoform of adiponectin. The mAb KH7–41, in lane 4, was selected as a representative recognizing both the MMW and low molecular weight (LMW) isoforms of adiponectin. The mAb KH4–8, in lane 8, was selected as a representative mAb recognizing both the MMW and HMW isoforms of adiponectin. b Comparison of the mAb recognition patterns of adiponectin isoforms in human, mouse, and rat sera by Western blot. Human, mouse, and rat sera were separated by sodium dodecyl sulfate–PAGE. All three mAbs (KH7–33, KH7–41, and KH4–8) recognized the rat and mouse adiponectin MMW isoform. Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011). Mouse and rat serum were obtained via heart puncture of male BALB/c mice and Sprague Dawley rats (8 weeks old), respectively. Human serum was obtained from a male volunteer (55 years old)
    Figure Legend Snippet: Fig. 1 Detection of serum adiponectin isoforms with monoclonal antibodies (mAbs) against recombinant human adiponectin. a Western blot to screen mAbs detecting different adiponectin isoforms. Human serum was loaded into each lane of the gel and resolved by polyacrylamide gel electrophoresis (PAGE) and then transferred to a membrane. Each lane of the membrane was then separately cut and incubated with each mAb from hybridoma culture supernatant. After the secondary antibody was probed, the cut membrane was combined to form one sheet and developed with ECL solution. Eleven different mAbs from culture supernatant were tested to investigate their recognition patterns of adiponectin isoforms in serum. The mAb KH7–33, in lane 3, was selected as a representative recognizing only the middle molecular weight (MMW) isoform of adiponectin. The mAb KH7–41, in lane 4, was selected as a representative recognizing both the MMW and low molecular weight (LMW) isoforms of adiponectin. The mAb KH4–8, in lane 8, was selected as a representative mAb recognizing both the MMW and HMW isoforms of adiponectin. b Comparison of the mAb recognition patterns of adiponectin isoforms in human, mouse, and rat sera by Western blot. Human, mouse, and rat sera were separated by sodium dodecyl sulfate–PAGE. All three mAbs (KH7–33, KH7–41, and KH4–8) recognized the rat and mouse adiponectin MMW isoform. Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011). Mouse and rat serum were obtained via heart puncture of male BALB/c mice and Sprague Dawley rats (8 weeks old), respectively. Human serum was obtained from a male volunteer (55 years old)

    Techniques Used: Bioprocessing, Recombinant, Western Blot, Polyacrylamide Gel Electrophoresis, Membrane, Incubation, Molecular Weight, Comparison

    Fig. 2 Immunohistological assays in human tissues with monoclonal antibodies (mAbs). To determine the pattern of recognition of adiponectin isoforms in human tissues by mAbs, a normal human adipose tissue was immunostained with mAbs (KH7–41, KH7–33, and KH4–8) (200×, scale bar = 25 μm). mAbs recognized adiponectin in the nucleus of adipocytes (blue arrow) and in vessels and endothelial cells (red arrow). b Human lung, kidney, and pancreas were stained with the KH7–41, KH7–33, and KH4–8 mAbs (100×). Abbreviations: HMW high molecular weight, LMW low molecular weight, MMW middle molecular weight
    Figure Legend Snippet: Fig. 2 Immunohistological assays in human tissues with monoclonal antibodies (mAbs). To determine the pattern of recognition of adiponectin isoforms in human tissues by mAbs, a normal human adipose tissue was immunostained with mAbs (KH7–41, KH7–33, and KH4–8) (200×, scale bar = 25 μm). mAbs recognized adiponectin in the nucleus of adipocytes (blue arrow) and in vessels and endothelial cells (red arrow). b Human lung, kidney, and pancreas were stained with the KH7–41, KH7–33, and KH4–8 mAbs (100×). Abbreviations: HMW high molecular weight, LMW low molecular weight, MMW middle molecular weight

    Techniques Used: Bioprocessing, Staining, High Molecular Weight, Molecular Weight

    Fig. 4 Epitope mapping of monoclonal antibody (mAb) KH4–8 against adiponectin. To identify the epitope-recognizing site of the KH4–8 mAb, PEPperMAP® technology was performed as described in the Methods. Human adiponectin was translated into linear 15–amino acid peptides with a peptide-peptide overlap of 14 amino acids. Human adiponectin peptide microarrays were incubated with mouse mAb KH4–8 at different concentrations followed by staining with secondary goat anti-mouse IgG (H + L) DyLight680 antibody. The light intensity was read by a reader. The amino acid sequence QQNHYD (139–144) was confirmed from among the full 244–amino acid sequence to be the epitope of adiponectin
    Figure Legend Snippet: Fig. 4 Epitope mapping of monoclonal antibody (mAb) KH4–8 against adiponectin. To identify the epitope-recognizing site of the KH4–8 mAb, PEPperMAP® technology was performed as described in the Methods. Human adiponectin was translated into linear 15–amino acid peptides with a peptide-peptide overlap of 14 amino acids. Human adiponectin peptide microarrays were incubated with mouse mAb KH4–8 at different concentrations followed by staining with secondary goat anti-mouse IgG (H + L) DyLight680 antibody. The light intensity was read by a reader. The amino acid sequence QQNHYD (139–144) was confirmed from among the full 244–amino acid sequence to be the epitope of adiponectin

    Techniques Used: Incubation, Staining, Sequencing

    Fig. 7 Anti-adiponectin antibodies reduce the histological signs of inflammation. The upper and lower panels present hematoxylin and eosin (H&E) staining and immunostaining against mouse adiponectin of mouse knee joints (n = 8), respectively. a Normal, b control, saline-treated arthritic, c KH7– 33-treated arthritic, d KH4–8-treated arthritic, and (e) prednisolone-treated arthritic mice. Tissue structure was visualized by using H&E staining (original magnification, 40×). Scale bar = 2 mm. f Arthritic symptoms were evaluated by scoring the degree of inflammation on H&E histological sections of knee joints as described in the Methods. Small blue squares on H&E staining are magnified in the upper right corner (400×). Abbreviations: C cartilage, F femur, M meniscus, S subchondral bone, T tibia. In the lower panel, immunohistochemistry (IHC) reveals adiponectin expression in collagen-induced arthritis mouse joints (200×). The increased adiponectin expression level observed on IHC was not decreased by monoclonal antibody treatment. Adiponectin immunostaining score level was evaluated as described in the Methods. Results are presented as the mean of experiments (± standard error of the mean indicated by error bar) (one-way analysis of variance followed by Dunn’s multiple comparison test). ***P <0.001 versus the normal (NOR) group and #P <0.05, ##P <0.01 versus the control (CON) group. Abbreviation: pre prednisolone
    Figure Legend Snippet: Fig. 7 Anti-adiponectin antibodies reduce the histological signs of inflammation. The upper and lower panels present hematoxylin and eosin (H&E) staining and immunostaining against mouse adiponectin of mouse knee joints (n = 8), respectively. a Normal, b control, saline-treated arthritic, c KH7– 33-treated arthritic, d KH4–8-treated arthritic, and (e) prednisolone-treated arthritic mice. Tissue structure was visualized by using H&E staining (original magnification, 40×). Scale bar = 2 mm. f Arthritic symptoms were evaluated by scoring the degree of inflammation on H&E histological sections of knee joints as described in the Methods. Small blue squares on H&E staining are magnified in the upper right corner (400×). Abbreviations: C cartilage, F femur, M meniscus, S subchondral bone, T tibia. In the lower panel, immunohistochemistry (IHC) reveals adiponectin expression in collagen-induced arthritis mouse joints (200×). The increased adiponectin expression level observed on IHC was not decreased by monoclonal antibody treatment. Adiponectin immunostaining score level was evaluated as described in the Methods. Results are presented as the mean of experiments (± standard error of the mean indicated by error bar) (one-way analysis of variance followed by Dunn’s multiple comparison test). ***P <0.001 versus the normal (NOR) group and #P <0.05, ##P <0.01 versus the control (CON) group. Abbreviation: pre prednisolone

    Techniques Used: Staining, Immunostaining, Control, Saline, Immunohistochemistry, Expressing, Comparison



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    Image Search Results


    Effects of a HIIT session on adiponectin isoforms. A low-molecular weight (LMW) adiponectin; B medium-molecular weight (MMW) adiponectin; C high-molecular weight (HMW) adiponectin; D representative blots with the three adiponectin isoforms. All values are normalized by the total protein loading (Ponceau Red staining), each dot united by a line represents the pre- and post-exercise values of the same participant, while the dots with the error bars at the Pre-post w/Error indicate the mean and SEM of the whole group. * : p < 0.05, indicate significant differences between the pre- and post-exercise values. Full-length blots/gels are presented in Supplementary File 1

    Journal: BMC Sports Science, Medicine and Rehabilitation

    Article Title: Acute effects of high-intensity interval training on adiponectin isoforms in inactive young adults: a quasi-experimental study

    doi: 10.1186/s13102-025-01433-7

    Figure Lengend Snippet: Effects of a HIIT session on adiponectin isoforms. A low-molecular weight (LMW) adiponectin; B medium-molecular weight (MMW) adiponectin; C high-molecular weight (HMW) adiponectin; D representative blots with the three adiponectin isoforms. All values are normalized by the total protein loading (Ponceau Red staining), each dot united by a line represents the pre- and post-exercise values of the same participant, while the dots with the error bars at the Pre-post w/Error indicate the mean and SEM of the whole group. * : p < 0.05, indicate significant differences between the pre- and post-exercise values. Full-length blots/gels are presented in Supplementary File 1

    Article Snippet: Following transfer, membranes were blocked for one hour with 5% bovine serum albumin (BSA) in TBST buffer, washed with TBST, and incubated overnight at 4 °C with a rabbit monoclonal primary antibody against human adiponectin (1:1000 dilution; Cell Signaling ® , catalog number 2789 S).

    Techniques: Molecular Weight, High Molecular Weight, Staining

    Effects of a HIIT session on the ratio of adiponectin isoforms. A ratio between high-molecular (HMW) and low-molecular weight (LMW) adiponectin; B ratio between medium-molecular (MMW) and LMW adiponectin; C ratio between HMW and MMW adiponectin. Each dot united by a line represent the pre- and post-exercise values of the same participant, while the dots with the error bars at the Pre-post w/Error indicate the mean and SEM of the whole group. * : p < 0.05, indicate significant differences between the pre- and post-exercise values

    Journal: BMC Sports Science, Medicine and Rehabilitation

    Article Title: Acute effects of high-intensity interval training on adiponectin isoforms in inactive young adults: a quasi-experimental study

    doi: 10.1186/s13102-025-01433-7

    Figure Lengend Snippet: Effects of a HIIT session on the ratio of adiponectin isoforms. A ratio between high-molecular (HMW) and low-molecular weight (LMW) adiponectin; B ratio between medium-molecular (MMW) and LMW adiponectin; C ratio between HMW and MMW adiponectin. Each dot united by a line represent the pre- and post-exercise values of the same participant, while the dots with the error bars at the Pre-post w/Error indicate the mean and SEM of the whole group. * : p < 0.05, indicate significant differences between the pre- and post-exercise values

    Article Snippet: Following transfer, membranes were blocked for one hour with 5% bovine serum albumin (BSA) in TBST buffer, washed with TBST, and incubated overnight at 4 °C with a rabbit monoclonal primary antibody against human adiponectin (1:1000 dilution; Cell Signaling ® , catalog number 2789 S).

    Techniques: Molecular Weight

    Figure 3. Effects of a maximal exercise session on adiponectin isoforms and its association with metabolic outcomes. (A) Low-molecular weight (LMW) adiponectin before and after the exercise session; (B) medium-molecular weight (MMW) adiponectin before and after the exercise session along with the representative blot with the adiponectin isoforms; (C) association between the changes (∆) of total cholesterol and the percentage of ∆of LMW adiponectin before and after exercise; (D) association between the ∆of the fibroblast growth factor (FGF)21 and the percentage of ∆of LMW adiponectin before and after exercise; (E) association between the ∆of plasma creatinine and the percentage of ∆ of MMW adiponectin before and after exercise; (F) association between the ∆in proteinuria and the percentage of ∆of MMW adiponectin before and after exercise. Original images of (B) can be found in supplementary materials.

    Journal: Biomolecules

    Article Title: Metabolic Response After a Single Maximal Exercise Session in Physically Inactive Young Adults (EASY Study): Relevancy of Adiponectin Isoforms

    doi: 10.3390/biom15030314

    Figure Lengend Snippet: Figure 3. Effects of a maximal exercise session on adiponectin isoforms and its association with metabolic outcomes. (A) Low-molecular weight (LMW) adiponectin before and after the exercise session; (B) medium-molecular weight (MMW) adiponectin before and after the exercise session along with the representative blot with the adiponectin isoforms; (C) association between the changes (∆) of total cholesterol and the percentage of ∆of LMW adiponectin before and after exercise; (D) association between the ∆of the fibroblast growth factor (FGF)21 and the percentage of ∆of LMW adiponectin before and after exercise; (E) association between the ∆of plasma creatinine and the percentage of ∆ of MMW adiponectin before and after exercise; (F) association between the ∆in proteinuria and the percentage of ∆of MMW adiponectin before and after exercise. Original images of (B) can be found in supplementary materials.

    Article Snippet: After washing in TBST, they were incubated overnight at 4 ◦C with a primary antibody against human adiponectin (1:1000 dilution, rabbit monoclonal antibody, Cell Signaling®, catalog number 2789S, Danvers, USA).

    Techniques: Molecular Weight, Clinical Proteomics

    a Glycosylated fibronectin concentrations in BMI subgroups of 20–25 and 30–35 kg/m 2 in the study and the control group. b Effect of smoking on concentrations of glycosylated fibronectin in the control and GDM groups. c Multiple of median (MoM) values for fibronectin and glycosylated fibronectin between control and GDM groups. d Multiple of median (MoM) values for adiponectin and glycosylated adiponectin between control and GDM groups

    Journal: Archives of Gynecology and Obstetrics

    Article Title: Glycosylated fibronectin as a first trimester marker for gestational diabetes

    doi: 10.1007/s00404-020-05670-8

    Figure Lengend Snippet: a Glycosylated fibronectin concentrations in BMI subgroups of 20–25 and 30–35 kg/m 2 in the study and the control group. b Effect of smoking on concentrations of glycosylated fibronectin in the control and GDM groups. c Multiple of median (MoM) values for fibronectin and glycosylated fibronectin between control and GDM groups. d Multiple of median (MoM) values for adiponectin and glycosylated adiponectin between control and GDM groups

    Article Snippet: Standard adiponectin assay was done by coating 96-well plates with mouse monoclonal IgG antibody against human adiponectin (MAB10651, R&D Systems, Abingdon, UK).

    Techniques: Control

    Fig. 1 Detection of serum adiponectin isoforms with monoclonal antibodies (mAbs) against recombinant human adiponectin. a Western blot to screen mAbs detecting different adiponectin isoforms. Human serum was loaded into each lane of the gel and resolved by polyacrylamide gel electrophoresis (PAGE) and then transferred to a membrane. Each lane of the membrane was then separately cut and incubated with each mAb from hybridoma culture supernatant. After the secondary antibody was probed, the cut membrane was combined to form one sheet and developed with ECL solution. Eleven different mAbs from culture supernatant were tested to investigate their recognition patterns of adiponectin isoforms in serum. The mAb KH7–33, in lane 3, was selected as a representative recognizing only the middle molecular weight (MMW) isoform of adiponectin. The mAb KH7–41, in lane 4, was selected as a representative recognizing both the MMW and low molecular weight (LMW) isoforms of adiponectin. The mAb KH4–8, in lane 8, was selected as a representative mAb recognizing both the MMW and HMW isoforms of adiponectin. b Comparison of the mAb recognition patterns of adiponectin isoforms in human, mouse, and rat sera by Western blot. Human, mouse, and rat sera were separated by sodium dodecyl sulfate–PAGE. All three mAbs (KH7–33, KH7–41, and KH4–8) recognized the rat and mouse adiponectin MMW isoform. Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011). Mouse and rat serum were obtained via heart puncture of male BALB/c mice and Sprague Dawley rats (8 weeks old), respectively. Human serum was obtained from a male volunteer (55 years old)

    Journal: Arthritis research & therapy

    Article Title: Potential therapeutic antibodies targeting specific adiponectin isoforms in rheumatoid arthritis.

    doi: 10.1186/s13075-018-1736-3

    Figure Lengend Snippet: Fig. 1 Detection of serum adiponectin isoforms with monoclonal antibodies (mAbs) against recombinant human adiponectin. a Western blot to screen mAbs detecting different adiponectin isoforms. Human serum was loaded into each lane of the gel and resolved by polyacrylamide gel electrophoresis (PAGE) and then transferred to a membrane. Each lane of the membrane was then separately cut and incubated with each mAb from hybridoma culture supernatant. After the secondary antibody was probed, the cut membrane was combined to form one sheet and developed with ECL solution. Eleven different mAbs from culture supernatant were tested to investigate their recognition patterns of adiponectin isoforms in serum. The mAb KH7–33, in lane 3, was selected as a representative recognizing only the middle molecular weight (MMW) isoform of adiponectin. The mAb KH7–41, in lane 4, was selected as a representative recognizing both the MMW and low molecular weight (LMW) isoforms of adiponectin. The mAb KH4–8, in lane 8, was selected as a representative mAb recognizing both the MMW and HMW isoforms of adiponectin. b Comparison of the mAb recognition patterns of adiponectin isoforms in human, mouse, and rat sera by Western blot. Human, mouse, and rat sera were separated by sodium dodecyl sulfate–PAGE. All three mAbs (KH7–33, KH7–41, and KH4–8) recognized the rat and mouse adiponectin MMW isoform. Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011). Mouse and rat serum were obtained via heart puncture of male BALB/c mice and Sprague Dawley rats (8 weeks old), respectively. Human serum was obtained from a male volunteer (55 years old)

    Article Snippet: Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011).

    Techniques: Bioprocessing, Recombinant, Western Blot, Polyacrylamide Gel Electrophoresis, Membrane, Incubation, Molecular Weight, Comparison

    Fig. 2 Immunohistological assays in human tissues with monoclonal antibodies (mAbs). To determine the pattern of recognition of adiponectin isoforms in human tissues by mAbs, a normal human adipose tissue was immunostained with mAbs (KH7–41, KH7–33, and KH4–8) (200×, scale bar = 25 μm). mAbs recognized adiponectin in the nucleus of adipocytes (blue arrow) and in vessels and endothelial cells (red arrow). b Human lung, kidney, and pancreas were stained with the KH7–41, KH7–33, and KH4–8 mAbs (100×). Abbreviations: HMW high molecular weight, LMW low molecular weight, MMW middle molecular weight

    Journal: Arthritis research & therapy

    Article Title: Potential therapeutic antibodies targeting specific adiponectin isoforms in rheumatoid arthritis.

    doi: 10.1186/s13075-018-1736-3

    Figure Lengend Snippet: Fig. 2 Immunohistological assays in human tissues with monoclonal antibodies (mAbs). To determine the pattern of recognition of adiponectin isoforms in human tissues by mAbs, a normal human adipose tissue was immunostained with mAbs (KH7–41, KH7–33, and KH4–8) (200×, scale bar = 25 μm). mAbs recognized adiponectin in the nucleus of adipocytes (blue arrow) and in vessels and endothelial cells (red arrow). b Human lung, kidney, and pancreas were stained with the KH7–41, KH7–33, and KH4–8 mAbs (100×). Abbreviations: HMW high molecular weight, LMW low molecular weight, MMW middle molecular weight

    Article Snippet: Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011).

    Techniques: Bioprocessing, Staining, High Molecular Weight, Molecular Weight

    Fig. 4 Epitope mapping of monoclonal antibody (mAb) KH4–8 against adiponectin. To identify the epitope-recognizing site of the KH4–8 mAb, PEPperMAP® technology was performed as described in the Methods. Human adiponectin was translated into linear 15–amino acid peptides with a peptide-peptide overlap of 14 amino acids. Human adiponectin peptide microarrays were incubated with mouse mAb KH4–8 at different concentrations followed by staining with secondary goat anti-mouse IgG (H + L) DyLight680 antibody. The light intensity was read by a reader. The amino acid sequence QQNHYD (139–144) was confirmed from among the full 244–amino acid sequence to be the epitope of adiponectin

    Journal: Arthritis research & therapy

    Article Title: Potential therapeutic antibodies targeting specific adiponectin isoforms in rheumatoid arthritis.

    doi: 10.1186/s13075-018-1736-3

    Figure Lengend Snippet: Fig. 4 Epitope mapping of monoclonal antibody (mAb) KH4–8 against adiponectin. To identify the epitope-recognizing site of the KH4–8 mAb, PEPperMAP® technology was performed as described in the Methods. Human adiponectin was translated into linear 15–amino acid peptides with a peptide-peptide overlap of 14 amino acids. Human adiponectin peptide microarrays were incubated with mouse mAb KH4–8 at different concentrations followed by staining with secondary goat anti-mouse IgG (H + L) DyLight680 antibody. The light intensity was read by a reader. The amino acid sequence QQNHYD (139–144) was confirmed from among the full 244–amino acid sequence to be the epitope of adiponectin

    Article Snippet: Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011).

    Techniques: Incubation, Staining, Sequencing

    Fig. 7 Anti-adiponectin antibodies reduce the histological signs of inflammation. The upper and lower panels present hematoxylin and eosin (H&E) staining and immunostaining against mouse adiponectin of mouse knee joints (n = 8), respectively. a Normal, b control, saline-treated arthritic, c KH7– 33-treated arthritic, d KH4–8-treated arthritic, and (e) prednisolone-treated arthritic mice. Tissue structure was visualized by using H&E staining (original magnification, 40×). Scale bar = 2 mm. f Arthritic symptoms were evaluated by scoring the degree of inflammation on H&E histological sections of knee joints as described in the Methods. Small blue squares on H&E staining are magnified in the upper right corner (400×). Abbreviations: C cartilage, F femur, M meniscus, S subchondral bone, T tibia. In the lower panel, immunohistochemistry (IHC) reveals adiponectin expression in collagen-induced arthritis mouse joints (200×). The increased adiponectin expression level observed on IHC was not decreased by monoclonal antibody treatment. Adiponectin immunostaining score level was evaluated as described in the Methods. Results are presented as the mean of experiments (± standard error of the mean indicated by error bar) (one-way analysis of variance followed by Dunn’s multiple comparison test). ***P <0.001 versus the normal (NOR) group and #P <0.05, ##P <0.01 versus the control (CON) group. Abbreviation: pre prednisolone

    Journal: Arthritis research & therapy

    Article Title: Potential therapeutic antibodies targeting specific adiponectin isoforms in rheumatoid arthritis.

    doi: 10.1186/s13075-018-1736-3

    Figure Lengend Snippet: Fig. 7 Anti-adiponectin antibodies reduce the histological signs of inflammation. The upper and lower panels present hematoxylin and eosin (H&E) staining and immunostaining against mouse adiponectin of mouse knee joints (n = 8), respectively. a Normal, b control, saline-treated arthritic, c KH7– 33-treated arthritic, d KH4–8-treated arthritic, and (e) prednisolone-treated arthritic mice. Tissue structure was visualized by using H&E staining (original magnification, 40×). Scale bar = 2 mm. f Arthritic symptoms were evaluated by scoring the degree of inflammation on H&E histological sections of knee joints as described in the Methods. Small blue squares on H&E staining are magnified in the upper right corner (400×). Abbreviations: C cartilage, F femur, M meniscus, S subchondral bone, T tibia. In the lower panel, immunohistochemistry (IHC) reveals adiponectin expression in collagen-induced arthritis mouse joints (200×). The increased adiponectin expression level observed on IHC was not decreased by monoclonal antibody treatment. Adiponectin immunostaining score level was evaluated as described in the Methods. Results are presented as the mean of experiments (± standard error of the mean indicated by error bar) (one-way analysis of variance followed by Dunn’s multiple comparison test). ***P <0.001 versus the normal (NOR) group and #P <0.05, ##P <0.01 versus the control (CON) group. Abbreviation: pre prednisolone

    Article Snippet: Lane 1, KH7–41; lane 2, KH7–33; lane 3, KH4–8; lane 4, commercial antibody against human adiponectin (Boster Immunoleader cat. no. PB9001) or mouse/rat adiponectin (Boster Immunoleader cat. no. PB9011).

    Techniques: Staining, Immunostaining, Control, Saline, Immunohistochemistry, Expressing, Comparison

    The expression of adiponectin was located in macrophages of atherosclerotic lesions from patients and cholesterol-fed rabbits by immunohistochemistry. Arterial serial sections from human atherosclerotic lesions (a), rabbits fed regular chow (b), or 2% cholesterol-containing diet for 6 weeks ((c), (d)) were stained for macrophages or adiponectin antibodies. Nuclei were stained by DAPI. L represents the vascular lumen. Bar = 50 μ m.

    Journal: Mediators of Inflammation

    Article Title: Troglitazone and Δ2Troglitazone Enhance Adiponectin Expression in Monocytes/Macrophages through the AMP-Activated Protein Kinase Pathway

    doi: 10.1155/2014/726068

    Figure Lengend Snippet: The expression of adiponectin was located in macrophages of atherosclerotic lesions from patients and cholesterol-fed rabbits by immunohistochemistry. Arterial serial sections from human atherosclerotic lesions (a), rabbits fed regular chow (b), or 2% cholesterol-containing diet for 6 weeks ((c), (d)) were stained for macrophages or adiponectin antibodies. Nuclei were stained by DAPI. L represents the vascular lumen. Bar = 50 μ m.

    Article Snippet: The first section was incubated sequentially for overnight at 4°C with a 1 : 100 dilution of rabbit antibodies against human adiponectin (Epitomics) in phosphate-buffered saline (PBS) containing 10% normal horse serum (Gibco) (PBS-NHS) and for 90 min at room temperature with a 1 : 200 dilution of biotinylated goat anti-rabbit IgG antibodies (Santa Cruz Biotechnology) in PBS-NHS, then bound antibodies were visualized using 3,3′-diaminobenzidine (DAB, Sigma-Aldrich).

    Techniques: Expressing, Immunohistochemistry, Staining

    Troglitazone (TG) and Δ2troglitazone (Δ2TG) enhanced adiponectin mRNA and protein expression in THP-1 cells. ((a)–(d)) The expression of adiponectin mRNA was examined by quantitative RT-PCR. Macrophages were treated with 9 μ M of TG for the indicated time (a) or with the indicated concentration of TG for 18 h (b). In addition, macrophages were treated with 9 μ M of Δ2TG for the indicated time (c) or with the indicated concentration of Δ2TG for 18 h (d). GAPDH was used as the internal control. (e) Macrophages were incubated for 18 h with 9 μ M of TG or Δ2TG and adiponectin protein expression was measured in cell lysates by Western blotting. β -actin was used as the loading control. (f) Macrophages were treated for 18 h with 9 μ M TG or Δ2TG, and then, the distribution of adiponectin was analyzed by immunofluorescent microscopy. The merged images of adiponectin staining and DAPI were shown on the right panel. Adiponectin expression is indicated by green fluorescence (FITC) and nuclei by blue fluorescence (DAPI). The level of adiponectin expression was higher in TG or Δ2TG-treated cells. Scale bar = 50 μ m. * P < 0.05 as compared to the untreated cells.

    Journal: Mediators of Inflammation

    Article Title: Troglitazone and Δ2Troglitazone Enhance Adiponectin Expression in Monocytes/Macrophages through the AMP-Activated Protein Kinase Pathway

    doi: 10.1155/2014/726068

    Figure Lengend Snippet: Troglitazone (TG) and Δ2troglitazone (Δ2TG) enhanced adiponectin mRNA and protein expression in THP-1 cells. ((a)–(d)) The expression of adiponectin mRNA was examined by quantitative RT-PCR. Macrophages were treated with 9 μ M of TG for the indicated time (a) or with the indicated concentration of TG for 18 h (b). In addition, macrophages were treated with 9 μ M of Δ2TG for the indicated time (c) or with the indicated concentration of Δ2TG for 18 h (d). GAPDH was used as the internal control. (e) Macrophages were incubated for 18 h with 9 μ M of TG or Δ2TG and adiponectin protein expression was measured in cell lysates by Western blotting. β -actin was used as the loading control. (f) Macrophages were treated for 18 h with 9 μ M TG or Δ2TG, and then, the distribution of adiponectin was analyzed by immunofluorescent microscopy. The merged images of adiponectin staining and DAPI were shown on the right panel. Adiponectin expression is indicated by green fluorescence (FITC) and nuclei by blue fluorescence (DAPI). The level of adiponectin expression was higher in TG or Δ2TG-treated cells. Scale bar = 50 μ m. * P < 0.05 as compared to the untreated cells.

    Article Snippet: The first section was incubated sequentially for overnight at 4°C with a 1 : 100 dilution of rabbit antibodies against human adiponectin (Epitomics) in phosphate-buffered saline (PBS) containing 10% normal horse serum (Gibco) (PBS-NHS) and for 90 min at room temperature with a 1 : 200 dilution of biotinylated goat anti-rabbit IgG antibodies (Santa Cruz Biotechnology) in PBS-NHS, then bound antibodies were visualized using 3,3′-diaminobenzidine (DAB, Sigma-Aldrich).

    Techniques: Expressing, Quantitative RT-PCR, Concentration Assay, Control, Incubation, Western Blot, Microscopy, Staining, Fluorescence

    PPAR γ antagonist GW9662 abolished the TG-stimulated adiponectin mRNA expression and had no effect on Δ2TG-enhanced adiponectin mRNA expression in THP-1 cells. Macrophages were incubated for 1 h with 5 μ M GW9662 (a PPAR γ inhibitor) and then for 18 h with or without 9 μ M TG (a) or Δ2TG (b) in the continued presence of the inhibitor, and then, adiponectin mRNA expression was measured by quantitative RT-PCR. * P < 0.05 as compared to the untreated cells. † P < 0.05 as compared to the TG or Δ2TG-treated cells, respectively.

    Journal: Mediators of Inflammation

    Article Title: Troglitazone and Δ2Troglitazone Enhance Adiponectin Expression in Monocytes/Macrophages through the AMP-Activated Protein Kinase Pathway

    doi: 10.1155/2014/726068

    Figure Lengend Snippet: PPAR γ antagonist GW9662 abolished the TG-stimulated adiponectin mRNA expression and had no effect on Δ2TG-enhanced adiponectin mRNA expression in THP-1 cells. Macrophages were incubated for 1 h with 5 μ M GW9662 (a PPAR γ inhibitor) and then for 18 h with or without 9 μ M TG (a) or Δ2TG (b) in the continued presence of the inhibitor, and then, adiponectin mRNA expression was measured by quantitative RT-PCR. * P < 0.05 as compared to the untreated cells. † P < 0.05 as compared to the TG or Δ2TG-treated cells, respectively.

    Article Snippet: The first section was incubated sequentially for overnight at 4°C with a 1 : 100 dilution of rabbit antibodies against human adiponectin (Epitomics) in phosphate-buffered saline (PBS) containing 10% normal horse serum (Gibco) (PBS-NHS) and for 90 min at room temperature with a 1 : 200 dilution of biotinylated goat anti-rabbit IgG antibodies (Santa Cruz Biotechnology) in PBS-NHS, then bound antibodies were visualized using 3,3′-diaminobenzidine (DAB, Sigma-Aldrich).

    Techniques: Expressing, Incubation, Quantitative RT-PCR

    TG and Δ2TG enhanced adiponectin mRNA expression was mediated through the AMPK pathway in THP-1 cells. The expression of adiponectin mRNA was examined by quantitative RT-PCR. Macrophages were treated with 150 μ M of AICAR (an AMPK activator) for the indicated time (a) or with the indicated concentration for 18 h (b). Macrophages were treated with compound C (an AMPK inhibitor) for the indicated concentration and then with (c) or without (d) AICAR for 18 h and then adiponectin mRNA expression was measured by real-time PCR. Macrophages were incubated for 1 h with compound C and then for 18 h with or without 9 μ M TG (e) or Δ2TG (f) in the continued presence of the inhibitor, and then, adiponectin mRNA expression was measured by real-time PCR. * P < 0.05 as compared to the untreated cells. † P < 0.05 as compared to the TG or Δ2TG-treated cells.

    Journal: Mediators of Inflammation

    Article Title: Troglitazone and Δ2Troglitazone Enhance Adiponectin Expression in Monocytes/Macrophages through the AMP-Activated Protein Kinase Pathway

    doi: 10.1155/2014/726068

    Figure Lengend Snippet: TG and Δ2TG enhanced adiponectin mRNA expression was mediated through the AMPK pathway in THP-1 cells. The expression of adiponectin mRNA was examined by quantitative RT-PCR. Macrophages were treated with 150 μ M of AICAR (an AMPK activator) for the indicated time (a) or with the indicated concentration for 18 h (b). Macrophages were treated with compound C (an AMPK inhibitor) for the indicated concentration and then with (c) or without (d) AICAR for 18 h and then adiponectin mRNA expression was measured by real-time PCR. Macrophages were incubated for 1 h with compound C and then for 18 h with or without 9 μ M TG (e) or Δ2TG (f) in the continued presence of the inhibitor, and then, adiponectin mRNA expression was measured by real-time PCR. * P < 0.05 as compared to the untreated cells. † P < 0.05 as compared to the TG or Δ2TG-treated cells.

    Article Snippet: The first section was incubated sequentially for overnight at 4°C with a 1 : 100 dilution of rabbit antibodies against human adiponectin (Epitomics) in phosphate-buffered saline (PBS) containing 10% normal horse serum (Gibco) (PBS-NHS) and for 90 min at room temperature with a 1 : 200 dilution of biotinylated goat anti-rabbit IgG antibodies (Santa Cruz Biotechnology) in PBS-NHS, then bound antibodies were visualized using 3,3′-diaminobenzidine (DAB, Sigma-Aldrich).

    Techniques: Expressing, Quantitative RT-PCR, Concentration Assay, Real-time Polymerase Chain Reaction, Incubation