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rabbit polyclonal antibody raised against adiponectin  (Millipore)

 
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    Structured Review

    Millipore rabbit polyclonal antibody raised against adiponectin
    (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, <t>adiponectin,</t> 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 .
    Rabbit Polyclonal Antibody Raised Against Adiponectin, supplied by Millipore, 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/result/rabbit polyclonal antibody raised against adiponectin/product/Millipore
    Average 90 stars, based on 1 article reviews
    rabbit polyclonal antibody raised against adiponectin - by Bioz Stars, 2026-03
    90/100 stars

    Images

    1) Product Images from "The Mixed-Lineage Kinase DLK Is a Key Regulator of 3T3-L1 Adipocyte Differentiation"

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

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0004743

    (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 .
    Figure Legend 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 .

    Techniques Used: 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.
    Figure Legend 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.

    Techniques Used: 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.
    Figure Legend 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.

    Techniques Used: 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.
    Figure Legend 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.

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



    Similar Products

    rabbit polyclonal antibody raised against adiponectin  (Millipore)
    90
    Millipore rabbit polyclonal antibody raised against adiponectin
    (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, <t>adiponectin,</t> 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 .
    Rabbit Polyclonal Antibody Raised Against Adiponectin, supplied by Millipore, 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/result/rabbit polyclonal antibody raised against adiponectin/product/Millipore
    Average 90 stars, based on 1 article reviews
    rabbit polyclonal antibody raised against adiponectin - by Bioz Stars, 2026-03
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (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