Review

anti adiponectin antibody (BioVendor Instruments)

BioVendor Instruments is a verified supplier

BioVendor Instruments manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

BioVendor Instruments anti adiponectin antibody

(A) Cumulative concentration response curve of methylcholine-induced vasodilation in pre-constricted (with U46619) mesenteric arteries incubated overnight without stimulus (white), 50 µg/mL of oxLDL (red), 30 µg/mL of AN (green), or 30 µg/mL of AN plus 50 µg/mL of oxLDL (blue). (B) Summary graph of the maximum response (Emax) obtained from concentrations curves shown in (A). Vessels were obtained from rats ( n = 6-13). (C) Cumulative concentration response curve of methylcholine-induced vasodilation in pre-constricted (with U46619) mesenteric arteries incubated overnight without stimulus (white) or with 50 µg/mL of oxLDL (red), 30 µg/mL of AN plus 50 µg/mL of oxLDL (blue), 30 µg/mL of AN plus 10 µg/mL of TS20 (purple), or 10 µg/mL of the IgG isotype (black). (D) Summary graph of the maximum response (Emax) obtained from concentrations curves shown in C. Vessels from n = 6-7 rats. Values are shown as the mean±SEM. ＊ p ＜0.05; ＊＊ p ＜0.01; ＊＊＊ p ＜0.001. ns, non-significant.

Anti Adiponectin Antibody, supplied by BioVendor Instruments, used in various techniques. Bioz Stars score: 94/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti+adiponectin+polyclonal+antibody/Adiponectin+(HEK)+Human%2C+Rabbit+Polyclonal+Antibody/pmc12416962-82-22-24
Average 94 stars, based on 2 article reviews

anti adiponectin antibody - by Bioz Stars, 2026-09

94/100 stars

Images

1) Product Images from "A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex"

Article Title: A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex

Journal: Journal of Atherosclerosis and Thrombosis

doi: 10.5551/jat.65377

Figure Legend Snippet: (A) Cumulative concentration response curve of methylcholine-induced vasodilation in pre-constricted (with U46619) mesenteric arteries incubated overnight without stimulus (white), 50 µg/mL of oxLDL (red), 30 µg/mL of AN (green), or 30 µg/mL of AN plus 50 µg/mL of oxLDL (blue). (B) Summary graph of the maximum response (Emax) obtained from concentrations curves shown in (A). Vessels were obtained from rats ( n = 6-13). (C) Cumulative concentration response curve of methylcholine-induced vasodilation in pre-constricted (with U46619) mesenteric arteries incubated overnight without stimulus (white) or with 50 µg/mL of oxLDL (red), 30 µg/mL of AN plus 50 µg/mL of oxLDL (blue), 30 µg/mL of AN plus 10 µg/mL of TS20 (purple), or 10 µg/mL of the IgG isotype (black). (D) Summary graph of the maximum response (Emax) obtained from concentrations curves shown in C. Vessels from n = 6-7 rats. Values are shown as the mean±SEM. ＊ p ＜0.05; ＊＊ p ＜0.01; ＊＊＊ p ＜0.001. ns, non-significant.

Techniques Used: Concentration Assay, Incubation

(A) Schematic representation of recombinant human T-cadherin proteins fused with Myc-His-tag. (B) Coomassie brilliant blue (CBB) staining and western blot analysis of purified T-cadherin proteins. (C) Binding of recombinant AN to immobilized T-cadherin in ELISA was determined by anti-AN antibody. (D) Binding of recombinant AN−oxLDL complex to immobilized LOX-1 in ELISA was determined by anti-AN antibody. s.p., signal peptide; EC, extracellular cadherin.

Figure Legend Snippet: (A) Schematic representation of recombinant human T-cadherin proteins fused with Myc-His-tag. (B) Coomassie brilliant blue (CBB) staining and western blot analysis of purified T-cadherin proteins. (C) Binding of recombinant AN to immobilized T-cadherin in ELISA was determined by anti-AN antibody. (D) Binding of recombinant AN−oxLDL complex to immobilized LOX-1 in ELISA was determined by anti-AN antibody. s.p., signal peptide; EC, extracellular cadherin.

Techniques Used: Enzyme-linked Immunosorbent Assay, Recombinant, Staining, Western Blot, Purification, Binding Assay

Correlation between total-AN and high-molecular weight (HMW)-AN (left), total-AN and T-cadherin bindable adiponectin (Tcad-AN) (middle), HMW-AN and Tcad-AN (right).

Figure Legend Snippet: Correlation between total-AN and high-molecular weight (HMW)-AN (left), total-AN and T-cadherin bindable adiponectin (Tcad-AN) (middle), HMW-AN and Tcad-AN (right).

Techniques Used: Enzyme-linked Immunosorbent Assay, High Molecular Weight

(A) Serum levels of AN, T-cadherin bindable adiponectin (Tcad-AN), oxidized LDL (oxLDL) and LOX-1-ligand containing apoB (LAB) in patients on hemodialysis (HD; n = 35) and control subjects ( n = 35). The error bars represent the mean±SD of the values obtained. (B) Comparison of the proportion of MAC-high between HD and controls. MAC-high and -low groups were divided by the median of the MAC values of 70 subjects.

Figure Legend Snippet: (A) Serum levels of AN, T-cadherin bindable adiponectin (Tcad-AN), oxidized LDL (oxLDL) and LOX-1-ligand containing apoB (LAB) in patients on hemodialysis (HD; n = 35) and control subjects ( n = 35). The error bars represent the mean±SD of the values obtained. (B) Comparison of the proportion of MAC-high between HD and controls. MAC-high and -low groups were divided by the median of the MAC values of 70 subjects.

Techniques Used: Comparison, Control

Figure Legend Snippet: The error bars represent mean±SD.

Techniques Used: Comparison

Binding Assay:

Article Title: Adiponectin forms a complex with atherogenic LDL and inhibits its downstream effects
Article Snippet: Human recombinant full-length adiponectin protein (composed of the LMW, MMW, and HMW isoforms) with a C-terminal FLAG sequence (produced in HEK293 cells, cat. no. RD172023100) and the globular form of adiponectin protein with an N-terminal His-tag sequence (produced in Escherichia coli, cat. no. RD172112100) were purchased from BioVendor (BioVendor, LLC, Asheville, NC). .. The following antibodies were used: anti-adiponectin polyclonal antibody (cat. no. RD181023100; BioVendor), anti-LOX-1 (#1-1) (17), anti-p44/42 MAPK (extracellular signal-regulated kinase [Erk] 1/2) (cat. no. 9102, Cell Signaling, Danvers, MA), antiphospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (cat. no. 9101, Cell Signaling), anti-AMPKα (F6; cat. no. 2793, Cell Signaling), anti-phospho-AMPKα (Thr172) (40H9; cat. no. 2535, Cell Signaling), horseradish peroxidase (HRP)conjugated anti-rabbit IgG antibody (cat. no. NA934, GE Healthcare), donkey anti-chicken IgY (cat. no. AP194P, Millipore, Burlington, MA), sheep anti-apoB polyclonal antibody conjugated with HRP (cat. no. PP086, The Binding Site, Birmingham, UK), and anti-apoB chicken monoclonal antibody (HUC20) (18, 19). ..

Article Title: Adiponectin forms a complex with atherogenic LDL and inhibits its downstream effects
Article Snippet: Human recombinant full-length adiponectin protein (composed of the LMW, MMW, and HMW isoforms) with a C-terminal FLAG sequence (produced in HEK293 cells, cat. no. RD172023100) and the globular form of adiponectin protein with an N-terminal His-tag sequence (produced in Escherichia coli , cat. no. RD172112100) were purchased from BioVendor (BioVendor, LLC, Asheville, NC). .. The following antibodies were used: anti-adiponectin polyclonal antibody (cat. no. RD181023100; BioVendor), anti-LOX-1 (#1-1) , anti-p44/42 MAPK (extracellular signal-regulated kinase [Erk] 1/2) (cat. no. 9102, Cell Signaling, Danvers, MA), anti-phospho-p44/42 MAPK (Erk1/2) (Thr202/Tyr204) (cat. no. 9101, Cell Signaling), anti-AMPKα (F6; cat. no. 2793, Cell Signaling), anti-phospho-AMPKα (Thr172) (40H9; cat. no. 2535, Cell Signaling), horseradish peroxidase (HRP)-conjugated anti-rabbit IgG antibody (cat. no. NA934, GE Healthcare), donkey anti-chicken IgY (cat. no. AP194P, Millipore, Burlington, MA), sheep anti-apoB polyclonal antibody conjugated with HRP (cat. no. PP086, The Binding Site, Birmingham, UK), and anti-apoB chicken monoclonal antibody (HUC20) ( , ). ..

Incubation:

Article Title: Adiponectin forms a complex with atherogenic LDL and inhibits its downstream effects
Article Snippet: Then, the proteins were electrotransferred to polyvinylidene difluoride (PVDF) membrane (iBlot2 Transfer Stacks; cat. no. IB24002, Thermo Fisher Scientific) by using an iBlot2 Dry Blotting System (Thermo Fisher Scientific). .. The membranes were blocked for 1 h in Immunoblock solution (cat. no. CTKN001, KAC, Kyoto, Japan) and were subsequently incubated with anti-adiponectin polyclonal antibody (1:1,000; cat. no. RD181023100, BioVendor) and anti-rabbit HRP-conjugated IgG antibody (1:5,000; cat. no. NA934, GE Healthcare). ..

Image Search Results

Effects of AdipoRon on lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in the liver of CORT broilers. (A) Immunoblot of ACC, CPT-1, PPARα and ADPN protein level in the liver of CORT broiler. (B) The change of ACC, CPT-1, PPARα and ADPN protein expression in the liver of CORT broiler. (C) Immunoblot of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein level in the liver of CORT broiler. (D) The change of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein expression in the liver of CORT broiler. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter differ significantly between groups ( p < 0.05, n = 6, biological replicates per group). ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1; TNF-α, Tumor Necrosis Factor-alpha.

Journal: Frontiers in Veterinary Science

Article Title: Adiponectin receptor agonist reduces broiler hepatic lipid deposition

doi: 10.3389/fvets.2025.1667501

Figure Lengend Snippet: Effects of AdipoRon on lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in the liver of CORT broilers. (A) Immunoblot of ACC, CPT-1, PPARα and ADPN protein level in the liver of CORT broiler. (B) The change of ACC, CPT-1, PPARα and ADPN protein expression in the liver of CORT broiler. (C) Immunoblot of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein level in the liver of CORT broiler. (D) The change of p-AMPKα1, AMPKα1, p-JNK1, JNK1 and TNFα protein expression in the liver of CORT broiler. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter differ significantly between groups ( p < 0.05, n = 6, biological replicates per group). ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1; TNF-α, Tumor Necrosis Factor-alpha.

Article Snippet: The membranes were blocked with a 5% skim milk powder solution at room temperature for 2 h. Subsequently, membranes were incubated with primary antibodies at 4°C for 12 h. After incubation with corresponding secondary antibodies at RT for 1 h. The primary antibodies used in this study included: ADPN (bs-0471R; Bioss, Beijing, China), PPAR α (bs-3614R; Bioss, Beijing, China), TNF-α (bsm-33207 M; Bioss, Beijing, China), p-AMPK (bs-5551R; Bioss, Beijing, China), AMPK (bs-41337R; Bioss, Beijing, China), p-JNK1 (bs-17591R; Bioss, Beijing, China), JNK1 (bs-20760R; Bioss, Beijing, China), and GAPDH (bsm-33033 M; Bioss, Beijing, China) as an internal control.

Techniques: Western Blot, Expressing, Software, Control

Effects of AdipoRon on viability, lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in FE-induced LMH cells. (A) The cell viability. (B) The change of oil red O quantification in LMH cells. (C1–3) Liver oil red O staining in LMH cells. Bar = 20 μm. (D) Immunoblot of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1 PPARα, p-JNK1, JNK1 and TNF-α protein level in LMH cells. (E) The change of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1, PPARα, p-JNK1, JNK1 and TNF-α protein expression in LMH cells. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter (a, b, c) differ significantly between groups ( p < 0.05, n = 6 per group, biological replicates). FE, fat emulsion; AdipoRon, adiponectin receptor agonists; ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; TNF-α, tumor necrosis factor-alpha; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1.

Journal: Frontiers in Veterinary Science

Article Title: Adiponectin receptor agonist reduces broiler hepatic lipid deposition

doi: 10.3389/fvets.2025.1667501

Figure Lengend Snippet: Effects of AdipoRon on viability, lipid accumulation, AMPK/PPARα and JNK1 signaling pathway in FE-induced LMH cells. (A) The cell viability. (B) The change of oil red O quantification in LMH cells. (C1–3) Liver oil red O staining in LMH cells. Bar = 20 μm. (D) Immunoblot of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1 PPARα, p-JNK1, JNK1 and TNF-α protein level in LMH cells. (E) The change of ACC, CPT-1, PPARα, ADPN, p-AMPKα1, AMPKα1, PPARα, p-JNK1, JNK1 and TNF-α protein expression in LMH cells. Grayscale values of each band were analyzed using ImageJ software. Normalization was performed by separately comparing the grayscale values of target protein bands with those of corresponding loading control bands (GAPDH), as well as the grayscale values of phosphorylated protein bands with those of total protein bands. The data represent mean ± SEM. Differences were determined by one-way ANOVA followed by Tukey’s test The bars with different small letter (a, b, c) differ significantly between groups ( p < 0.05, n = 6 per group, biological replicates). FE, fat emulsion; AdipoRon, adiponectin receptor agonists; ACC, Acetyl-CoA carboxylase 1; CPT-1, carnitine palmitoyl transferase-1; PPARα, peroxisome proliferators-activated receptor α; ADPN, adiponectin; TNF-α, tumor necrosis factor-alpha; AMPKα1, adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; p-AMPKα1, phosphorylated adenosine 5′-monophosphate (AMP)-activated protein kinase alpha 1; JNK1, c-Jun N-terminal kinase 1; p-JNK1, phosphorylated c-Jun N-terminal kinase 1.

Techniques: Staining, Western Blot, Expressing, Software, Control, Emulsion

Journal: Journal of Atherosclerosis and Thrombosis

Article Title: A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex

doi: 10.5551/jat.65377

Figure Lengend Snippet: (A) Cumulative concentration response curve of methylcholine-induced vasodilation in pre-constricted (with U46619) mesenteric arteries incubated overnight without stimulus (white), 50 µg/mL of oxLDL (red), 30 µg/mL of AN (green), or 30 µg/mL of AN plus 50 µg/mL of oxLDL (blue). (B) Summary graph of the maximum response (Emax) obtained from concentrations curves shown in (A). Vessels were obtained from rats ( n = 6-13). (C) Cumulative concentration response curve of methylcholine-induced vasodilation in pre-constricted (with U46619) mesenteric arteries incubated overnight without stimulus (white) or with 50 µg/mL of oxLDL (red), 30 µg/mL of AN plus 50 µg/mL of oxLDL (blue), 30 µg/mL of AN plus 10 µg/mL of TS20 (purple), or 10 µg/mL of the IgG isotype (black). (D) Summary graph of the maximum response (Emax) obtained from concentrations curves shown in C. Vessels from n = 6-7 rats. Values are shown as the mean±SEM. ＊ p ＜0.05; ＊＊ p ＜0.01; ＊＊＊ p ＜0.001. ns, non-significant.

Article Snippet: The wells were washed three more times with PBS, and the plates were incubated for 1 h at 25°C with 1.0 μg/mL anti-adiponectin antibody (BioVendor, RD181023100) in 1% (w/v) casein-Na blocking solution.

Techniques: Concentration Assay, Incubation

Journal: Journal of Atherosclerosis and Thrombosis

Article Title: A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex

doi: 10.5551/jat.65377

Figure Lengend Snippet: (A) Schematic representation of recombinant human T-cadherin proteins fused with Myc-His-tag. (B) Coomassie brilliant blue (CBB) staining and western blot analysis of purified T-cadherin proteins. (C) Binding of recombinant AN to immobilized T-cadherin in ELISA was determined by anti-AN antibody. (D) Binding of recombinant AN−oxLDL complex to immobilized LOX-1 in ELISA was determined by anti-AN antibody. s.p., signal peptide; EC, extracellular cadherin.

Techniques: Enzyme-linked Immunosorbent Assay, Recombinant, Staining, Western Blot, Purification, Binding Assay

Journal: Journal of Atherosclerosis and Thrombosis

Article Title: A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex

doi: 10.5551/jat.65377

Figure Lengend Snippet: Correlation between total-AN and high-molecular weight (HMW)-AN (left), total-AN and T-cadherin bindable adiponectin (Tcad-AN) (middle), HMW-AN and Tcad-AN (right).

Techniques: Enzyme-linked Immunosorbent Assay, High Molecular Weight

Journal: Journal of Atherosclerosis and Thrombosis

Article Title: A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex

doi: 10.5551/jat.65377

Figure Lengend Snippet: (A) Serum levels of AN, T-cadherin bindable adiponectin (Tcad-AN), oxidized LDL (oxLDL) and LOX-1-ligand containing apoB (LAB) in patients on hemodialysis (HD; n = 35) and control subjects ( n = 35). The error bars represent the mean±SD of the values obtained. (B) Comparison of the proportion of MAC-high between HD and controls. MAC-high and -low groups were divided by the median of the MAC values of 70 subjects.

Techniques: Comparison, Control

Journal: Journal of Atherosclerosis and Thrombosis

Article Title: A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex

doi: 10.5551/jat.65377

Figure Lengend Snippet: The error bars represent mean±SD.

Techniques: Comparison

Review

anti adiponectin antibody (BioVendor Instruments)

Structured Review

Images

1) Product Images from "A Novel ELISA System for Measuring Modified LDL-Adiponectin Complex"

Related Articles

Binding Assay:

Incubation:

Similar Products

Image Search Results