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rabbit polyclonal antibodies against adiponectin (Proteintech)

Name: rabbit polyclonal antibodies against adiponectin
Brand: Proteintech
Rating: 95 (49 reviews)

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Proteintech rabbit polyclonal antibodies against adiponectin
Rabbit Polyclonal Antibodies Against Adiponectin, supplied by Proteintech, used in various techniques. Bioz Stars score: 95/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/rabbit polyclonal antibodies against adiponectin/product/Proteintech
Average 95 stars, based on 49 article reviews

rabbit polyclonal antibodies against adiponectin - by Bioz Stars, 2026-03

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Human SGBS adipocytes were pretreated with HT (1 h) (A), OA (48 h) or RSG (24 h) (B) at the concentrations indicated and then either treated with 10 ng/mL TNF-α (black-filled bars), or left untreated (open white bars), for 24 h. Adiponectin levels in the culture medium were determined by ELISA, and expressed as percent of unstimulated control (CTL). Bars represent means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α. ** p <0.01 versus TNF-α.

Journal: PLoS ONE

Article Title: Additive Regulation of Adiponectin Expression by the Mediterranean Diet Olive Oil Components Oleic Acid and Hydroxytyrosol in Human Adipocytes

doi: 10.1371/journal.pone.0128218

Figure Lengend Snippet: Human SGBS adipocytes were pretreated with HT (1 h) (A), OA (48 h) or RSG (24 h) (B) at the concentrations indicated and then either treated with 10 ng/mL TNF-α (black-filled bars), or left untreated (open white bars), for 24 h. Adiponectin levels in the culture medium were determined by ELISA, and expressed as percent of unstimulated control (CTL). Bars represent means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α. ** p <0.01 versus TNF-α.

Article Snippet: 3T3-L1 adipocytes grown in 24-well plates on coverslips (Thermanox, ProSciTech, Thuringowa, Queensland, Australia) were pretreated with HT or OA before TNF-α stimulation for 24 h. The specimens were fixed with cold acetone and then incubated overnight with a rabbit polyclonal antibody against adiponectin (Millipore, Billerica, MA, USA).

Techniques: Enzyme-linked Immunosorbent Assay, Control

SGBS cells were pretreated with either HT, OA or cotreated with HT + OA before 10 ng/mL TNF-α stimulation for 24 h. (A) Adiponectin in the culture medium was determined by ELISA, and expressed as percent of unstimulated control (CTL). (B) Adiponectin intracellular protein levels were determined by Western analysis using antibodies against adiponectin. Western analysis under reducing and denaturing condition here reveals the 30 kDa adiponectin monomer. Adiponectin expression was normalized to β-actin, and expressed as percent of unstimulated control (CTL). Data are means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α alone. † p <0.05 versus each compound + TNF-α.

Journal: PLoS ONE

Article Title: Additive Regulation of Adiponectin Expression by the Mediterranean Diet Olive Oil Components Oleic Acid and Hydroxytyrosol in Human Adipocytes

doi: 10.1371/journal.pone.0128218

Figure Lengend Snippet: SGBS cells were pretreated with either HT, OA or cotreated with HT + OA before 10 ng/mL TNF-α stimulation for 24 h. (A) Adiponectin in the culture medium was determined by ELISA, and expressed as percent of unstimulated control (CTL). (B) Adiponectin intracellular protein levels were determined by Western analysis using antibodies against adiponectin. Western analysis under reducing and denaturing condition here reveals the 30 kDa adiponectin monomer. Adiponectin expression was normalized to β-actin, and expressed as percent of unstimulated control (CTL). Data are means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α alone. † p <0.05 versus each compound + TNF-α.

Techniques: Enzyme-linked Immunosorbent Assay, Control, Western Blot, Expressing

SGBS cells were pretreated with either HT, OA or cotreated with HT + OA before 10 ng/mL TNF-α stimulation for 24 h. Adiponectin mRNA levels were determined by qPCR and normalized to 18S RNA. Data are expressed as fold induction over unstimulated control (CTL). Data are means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α alone. † p <0.05 versus each compound + TNF-α.

Journal: PLoS ONE

Article Title: Additive Regulation of Adiponectin Expression by the Mediterranean Diet Olive Oil Components Oleic Acid and Hydroxytyrosol in Human Adipocytes

doi: 10.1371/journal.pone.0128218

Figure Lengend Snippet: SGBS cells were pretreated with either HT, OA or cotreated with HT + OA before 10 ng/mL TNF-α stimulation for 24 h. Adiponectin mRNA levels were determined by qPCR and normalized to 18S RNA. Data are expressed as fold induction over unstimulated control (CTL). Data are means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α alone. † p <0.05 versus each compound + TNF-α.

Techniques: Control

(A) SGBS cells were treated with 1 μmol/L HT, 10 μmol/L OA, or 1 μmol/L RSG in the absence or presence of the PPARγ antagonist GW9662 at 10 μmol/L (GW), and then stimulated with 10 ng/mL TNF-α for 24 h. Adiponectin levels in the culture medium were determined by ELISA, and expressed as percent of unstimulated control (CTL). Data are means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α alone. † p <0.05 versus the compound-treated group without GW9662. (B) and (C) SGBS cells were treated with 1 μmol/L HT or 10 μmol/L OA before 10 ng/mL TNF-α stimulation for 24 h. (B) Whole-cell lysates were assayed by Western blotting using antibodies against PPARγ1, PPARγ2, and against β-actin, this last used as a loading control. Total PPARγ1 and PPARγ2 band intensities were normalized to β-actin, and are expressed as percent of unstimulated control (CTL). (C) Nuclear proteins were analyzed for PPARγ DNA-binding activity by ELISA as described in Methods. Data are expressed as percent of unstimulated control (CTL). (D) SGBS cells were treated with 1–10 μmol/L HT, or 10 μmol/L OA, or co-treated with OA + HT before 10 ng/mL TNF-α stimulation for 24 h. PPARγ mRNA levels were determined by qPCR and normalized to 18S RNA. Data are expressed as fold induction over unstimulated control (CTL). Bars represent means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α. † p <0.05 versus each compound + TNF-α.

Journal: PLoS ONE

Article Title: Additive Regulation of Adiponectin Expression by the Mediterranean Diet Olive Oil Components Oleic Acid and Hydroxytyrosol in Human Adipocytes

doi: 10.1371/journal.pone.0128218

Figure Lengend Snippet: (A) SGBS cells were treated with 1 μmol/L HT, 10 μmol/L OA, or 1 μmol/L RSG in the absence or presence of the PPARγ antagonist GW9662 at 10 μmol/L (GW), and then stimulated with 10 ng/mL TNF-α for 24 h. Adiponectin levels in the culture medium were determined by ELISA, and expressed as percent of unstimulated control (CTL). Data are means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α alone. † p <0.05 versus the compound-treated group without GW9662. (B) and (C) SGBS cells were treated with 1 μmol/L HT or 10 μmol/L OA before 10 ng/mL TNF-α stimulation for 24 h. (B) Whole-cell lysates were assayed by Western blotting using antibodies against PPARγ1, PPARγ2, and against β-actin, this last used as a loading control. Total PPARγ1 and PPARγ2 band intensities were normalized to β-actin, and are expressed as percent of unstimulated control (CTL). (C) Nuclear proteins were analyzed for PPARγ DNA-binding activity by ELISA as described in Methods. Data are expressed as percent of unstimulated control (CTL). (D) SGBS cells were treated with 1–10 μmol/L HT, or 10 μmol/L OA, or co-treated with OA + HT before 10 ng/mL TNF-α stimulation for 24 h. PPARγ mRNA levels were determined by qPCR and normalized to 18S RNA. Data are expressed as fold induction over unstimulated control (CTL). Bars represent means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α. † p <0.05 versus each compound + TNF-α.

Techniques: Enzyme-linked Immunosorbent Assay, Control, Western Blot, Binding Assay, Activity Assay

SGBS cells were pretreated for 1 h with 10 μmol/L of the JNK inhibitor SP600125 (SP), the ERK1/2 inhibitor PD98059 (PD), or the p38 inhibitor SB203580 (SB), and then stimulated with 10 ng/mL TNF-α for 24 h. Culture media were analyzed for adiponectin by ELISA (A), and whole-cell lysates were assayed by Western blotting using antibodies against adiponectin (B) or PPARγ (C). Adiponectin and PPARγ expression were normalized to β-actin, and expressed as percent of unstimulated control (CTL). Bars represent means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α.

Journal: PLoS ONE

Article Title: Additive Regulation of Adiponectin Expression by the Mediterranean Diet Olive Oil Components Oleic Acid and Hydroxytyrosol in Human Adipocytes

doi: 10.1371/journal.pone.0128218

Figure Lengend Snippet: SGBS cells were pretreated for 1 h with 10 μmol/L of the JNK inhibitor SP600125 (SP), the ERK1/2 inhibitor PD98059 (PD), or the p38 inhibitor SB203580 (SB), and then stimulated with 10 ng/mL TNF-α for 24 h. Culture media were analyzed for adiponectin by ELISA (A), and whole-cell lysates were assayed by Western blotting using antibodies against adiponectin (B) or PPARγ (C). Adiponectin and PPARγ expression were normalized to β-actin, and expressed as percent of unstimulated control (CTL). Bars represent means ± SD (n = 3). # p <0.05 versus CTL. * p <0.05 versus TNF-α.

Techniques: Enzyme-linked Immunosorbent Assay, Western Blot, Expressing, Control

SGBS cells were treated with scrambled negative control siRNA (siControl), JNK1 siRNA (siJNK1), JNK2 siRNA (siJNK2), or JNK1 plus JNK2 siRNA, for 72 h. The mRNA expression levels of JNK1 and JNK2 were measured by qPCR, normalized to 18S RNA, and expressed as fold induction over scrambled negative control siRNA (A). JNK1 and JNK2 intracellular protein levels were assayed by Western blotting, normalized to β-actin, and expressed as percent of scrambled negative control siRNA (B). Bars represent means ± SD. # p <0.05 versus siControl. After 72 h of transfection, cells were stimulated with 10 ng/mL TNF-α for further 24 h. Adiponectin mRNA were determined by qPCR (C), while adiponectin intracellular and secreted protein levels were determined by Western analysis (D) and ELISA (E), respectively. Bars represent means ± SD. # p <0.05 versus siControl without TNF-α. * p <0.05 versus siControl with TNF-α.

Journal: PLoS ONE

Article Title: Additive Regulation of Adiponectin Expression by the Mediterranean Diet Olive Oil Components Oleic Acid and Hydroxytyrosol in Human Adipocytes

doi: 10.1371/journal.pone.0128218

Figure Lengend Snippet: SGBS cells were treated with scrambled negative control siRNA (siControl), JNK1 siRNA (siJNK1), JNK2 siRNA (siJNK2), or JNK1 plus JNK2 siRNA, for 72 h. The mRNA expression levels of JNK1 and JNK2 were measured by qPCR, normalized to 18S RNA, and expressed as fold induction over scrambled negative control siRNA (A). JNK1 and JNK2 intracellular protein levels were assayed by Western blotting, normalized to β-actin, and expressed as percent of scrambled negative control siRNA (B). Bars represent means ± SD. # p <0.05 versus siControl. After 72 h of transfection, cells were stimulated with 10 ng/mL TNF-α for further 24 h. Adiponectin mRNA were determined by qPCR (C), while adiponectin intracellular and secreted protein levels were determined by Western analysis (D) and ELISA (E), respectively. Bars represent means ± SD. # p <0.05 versus siControl without TNF-α. * p <0.05 versus siControl with TNF-α.

Techniques: Negative Control, Expressing, Western Blot, Transfection, Enzyme-linked Immunosorbent Assay

Pre-treatment with HT and OA before TNF-α stimulation prevents JNK activation and restores PPARγ expression and activity and, as a consequence, adiponectin levels. A coherent interpretation of the findings is as follows: upon binding to the cognate receptor, TNF-α induces reactive oxygen species (ROS) production and triggers an inflammatory signaling cascade involving, among others, the activation of JNK, which mediates the degradation of PPARγ (a transcription factor implicated in adiponectin gene expression through a PPAR-responsive element (PPRE) in its promoter). As a result, adiponectin expression is downregulated. Arrow indicates stimulation. Line indicates inhibition. MKK: MAP kinase kinase; pJNK: phosphorylated JNK.

Journal: PLoS ONE

Article Title: Additive Regulation of Adiponectin Expression by the Mediterranean Diet Olive Oil Components Oleic Acid and Hydroxytyrosol in Human Adipocytes

doi: 10.1371/journal.pone.0128218

Figure Lengend Snippet: Pre-treatment with HT and OA before TNF-α stimulation prevents JNK activation and restores PPARγ expression and activity and, as a consequence, adiponectin levels. A coherent interpretation of the findings is as follows: upon binding to the cognate receptor, TNF-α induces reactive oxygen species (ROS) production and triggers an inflammatory signaling cascade involving, among others, the activation of JNK, which mediates the degradation of PPARγ (a transcription factor implicated in adiponectin gene expression through a PPAR-responsive element (PPRE) in its promoter). As a result, adiponectin expression is downregulated. Arrow indicates stimulation. Line indicates inhibition. MKK: MAP kinase kinase; pJNK: phosphorylated JNK.

Techniques: Activation Assay, Expressing, Activity Assay, Binding Assay, Gene Expression, Inhibition

Expression of the Rab22a Q64L mutant inhibits ATP7A trafficking. HeLa cells transiently transfected with myc-tagged, constitutively active Rab22a Q64L were treated with CuCl 2 , fixed, and colabeled for ATP7A (green) and anti-myc to detect the Rab22a mutant (a), EEA1 (b), or golgin-97 (c) (all red). Cells expressing Rab22a Q64L (d) were treated with copper, followed by washout, and colabeled for ATP7A (green) and myc tag (red). Nuclei are labeled with DAPI (blue). Scale bar, 10 μm.

Journal: Molecular Biology of the Cell

Article Title: Trafficking of the Menkes copper transporter ATP7A is regulated by clathrin-, AP-2–, AP-1–, and Rab22-dependent steps

doi: 10.1091/mbc.E12-08-0625

Figure Lengend Snippet: Expression of the Rab22a Q64L mutant inhibits ATP7A trafficking. HeLa cells transiently transfected with myc-tagged, constitutively active Rab22a Q64L were treated with CuCl 2 , fixed, and colabeled for ATP7A (green) and anti-myc to detect the Rab22a mutant (a), EEA1 (b), or golgin-97 (c) (all red). Cells expressing Rab22a Q64L (d) were treated with copper, followed by washout, and colabeled for ATP7A (green) and myc tag (red). Nuclei are labeled with DAPI (blue). Scale bar, 10 μm.

Article Snippet: Polyclonal antibodies against EEA1 (C45B10) and clathrin heavy chain (P1663) were from Cell Signaling Technology; GM130 has been described ( Nelson et al. , 1998 ); ATP7A ( Steveson et al. , 2003 ) was a kind gift from Betty Eipper (University of Connecticut Health Center, Farmington, CT).

Techniques: Expressing, Mutagenesis, Transfection, Labeling

(A) Homogenates of mouse heart, white adipose tissue from various depots (gonadal, retroperitoneal, omental, mesenteric and inguinal) and brown adipose tissue (BAT) were subjected to Western blot analysis with specific antibodies against DLK or GAPDH. (B) and (D) 3T3-L1 cells induced to differentiate for 2, 4, 6, 8 and 10 days were lysed and subjected to immunoblotting analysis with antibodies to DLK, adiponectin, fatty acid synthase (FAS), PPARγ, ERK, phospho-ERK, p38, phospho-p38, JNK, phospho-JNK and tubulin as the loading control. The antibody raised against PPARγ reveals the presence of both PPARγ isoforms, PPARγ1 and PPARγ2. (C) 3T3-L1 cells induced to differentiate for the indicated times were lysed for immunoprecipitation analysis with anti-DLK antibody and subjected to an immunocomplex kinase assay using myelin basic protein (MBP) as a substrate. Diff: Days of differentiation . WB: Western Blot .

Journal: PLoS ONE

Article Title: The Mixed-Lineage Kinase DLK Is a Key Regulator of 3T3-L1 Adipocyte Differentiation

doi: 10.1371/journal.pone.0004743

Figure Lengend Snippet: (A) Homogenates of mouse heart, white adipose tissue from various depots (gonadal, retroperitoneal, omental, mesenteric and inguinal) and brown adipose tissue (BAT) were subjected to Western blot analysis with specific antibodies against DLK or GAPDH. (B) and (D) 3T3-L1 cells induced to differentiate for 2, 4, 6, 8 and 10 days were lysed and subjected to immunoblotting analysis with antibodies to DLK, adiponectin, fatty acid synthase (FAS), PPARγ, ERK, phospho-ERK, p38, phospho-p38, JNK, phospho-JNK and tubulin as the loading control. The antibody raised against PPARγ reveals the presence of both PPARγ isoforms, PPARγ1 and PPARγ2. (C) 3T3-L1 cells induced to differentiate for the indicated times were lysed for immunoprecipitation analysis with anti-DLK antibody and subjected to an immunocomplex kinase assay using myelin basic protein (MBP) as a substrate. Diff: Days of differentiation . WB: Western Blot .

Article Snippet: The rabbit polyclonal antibody raised against adiponectin was obtained from Calbiochem (Mississaga, Ontario, Canada).

Techniques: Western Blot, Control, Immunoprecipitation, Kinase Assay

3T3-L1 cells infected with an empty lentivirus, a lentivirus expressing human DLK shRNA (hDLK) or a lentivirus expressing mouse DLK shRNA (mDLK) were induced to differentiate for the indicated times. After differentiation, cells were subjected to Western blot analysis with specific antibodies against DLK, C/EBPβ, C/EBPδ, C/EBPα, PPARγ, adiponectin, fatty acid synthase (FAS), phospho-JNK, JNK and Akt as the loading control.

Journal: PLoS ONE

Article Title: The Mixed-Lineage Kinase DLK Is a Key Regulator of 3T3-L1 Adipocyte Differentiation

doi: 10.1371/journal.pone.0004743

Figure Lengend Snippet: 3T3-L1 cells infected with an empty lentivirus, a lentivirus expressing human DLK shRNA (hDLK) or a lentivirus expressing mouse DLK shRNA (mDLK) were induced to differentiate for the indicated times. After differentiation, cells were subjected to Western blot analysis with specific antibodies against DLK, C/EBPβ, C/EBPδ, C/EBPα, PPARγ, adiponectin, fatty acid synthase (FAS), phospho-JNK, JNK and Akt as the loading control.

Article Snippet: The rabbit polyclonal antibody raised against adiponectin was obtained from Calbiochem (Mississaga, Ontario, Canada).

Techniques: Infection, Expressing, shRNA, Western Blot, Control

3T3-L1 cells infected with an empty lentivirus (EV), a lentivirus expressing human DLK shRNA (hDLK) or a lentivirus expressing mouse DLK shRNA (mDLK) were induced to differentiate, and at the indicated times, total RNA was extracted. C/EBPβ, C/EBPα, PPARγ, adiponectin and FAS mRNA levels were analyzed by quantitative RT-PCR with specific primers. The expression level of each gene was normalized to the level of the 36B4 housekeeping gene. Results are expressed as fold induction of mRNA levels relative to cells harvested on day 0 and they are representative of at least three independent experiments.

Journal: PLoS ONE

Article Title: The Mixed-Lineage Kinase DLK Is a Key Regulator of 3T3-L1 Adipocyte Differentiation

doi: 10.1371/journal.pone.0004743

Figure Lengend Snippet: 3T3-L1 cells infected with an empty lentivirus (EV), a lentivirus expressing human DLK shRNA (hDLK) or a lentivirus expressing mouse DLK shRNA (mDLK) were induced to differentiate, and at the indicated times, total RNA was extracted. C/EBPβ, C/EBPα, PPARγ, adiponectin and FAS mRNA levels were analyzed by quantitative RT-PCR with specific primers. The expression level of each gene was normalized to the level of the 36B4 housekeeping gene. Results are expressed as fold induction of mRNA levels relative to cells harvested on day 0 and they are representative of at least three independent experiments.

Article Snippet: The rabbit polyclonal antibody raised against adiponectin was obtained from Calbiochem (Mississaga, Ontario, Canada).

Techniques: Infection, Expressing, shRNA, Quantitative RT-PCR

(A) 3T3-L1 cells infected with an empty lentiviral vector (EV) or with a lentivirus expressing human (hDLK) or mouse (mDLK) DLK shRNA were induced to differentiate for 6 days in the presence of 1 µM rosiglitazone. After differentiation, cells were stained for lipids with ORO and photographed. Lipids extracted from ORO-stained cells were quantified by spectrophotometry at 520 nm. The data represent the mean±SEM of three independent experiments, relative to EV-infected cells. (B) 3T3-L1 cells infected with an empty lentiviral vector (EV) or with a lentivirus expressing human (hDLK) or mouse (mDLK) DLK shRNA were induced to differentiate for 2, 4 or 6 days in the presence of 1 µM rosiglitazone or DMSO (vehicule). After differentiation, cells were subjected to Western blot analysis with antibodies directed against DLK, C/EBPβ, C/EBPα, PPARγ, adiponectin and FAS. As a control for protein loading, immunoblots were probed in parallel with an antibody specific for tubulin.

Journal: PLoS ONE

Article Title: The Mixed-Lineage Kinase DLK Is a Key Regulator of 3T3-L1 Adipocyte Differentiation

doi: 10.1371/journal.pone.0004743

Figure Lengend Snippet: (A) 3T3-L1 cells infected with an empty lentiviral vector (EV) or with a lentivirus expressing human (hDLK) or mouse (mDLK) DLK shRNA were induced to differentiate for 6 days in the presence of 1 µM rosiglitazone. After differentiation, cells were stained for lipids with ORO and photographed. Lipids extracted from ORO-stained cells were quantified by spectrophotometry at 520 nm. The data represent the mean±SEM of three independent experiments, relative to EV-infected cells. (B) 3T3-L1 cells infected with an empty lentiviral vector (EV) or with a lentivirus expressing human (hDLK) or mouse (mDLK) DLK shRNA were induced to differentiate for 2, 4 or 6 days in the presence of 1 µM rosiglitazone or DMSO (vehicule). After differentiation, cells were subjected to Western blot analysis with antibodies directed against DLK, C/EBPβ, C/EBPα, PPARγ, adiponectin and FAS. As a control for protein loading, immunoblots were probed in parallel with an antibody specific for tubulin.

Article Snippet: The rabbit polyclonal antibody raised against adiponectin was obtained from Calbiochem (Mississaga, Ontario, Canada).

Techniques: Infection, Plasmid Preparation, Expressing, shRNA, Staining, Spectrophotometry, Western Blot, Control

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