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Human Brown Fat Cell Differentiation

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated C/EBPα (D56F10) XP® Rabbit mAb #8178.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors that are critical for cellular differentiation, terminal function, and inflammatory response (1). Six members of the family have been characterized (C/EBPα, β, δ, γ, ε, and ζ) and are distributed in a variety of tissues (1). Translation from alternative start codons results in two isoforms of C/EBPα (p42 and p30), which are both strong transcriptional activators (2). It has been reported that insulin and insulin-like growth factor-I stimulate the dephosphorylation of C/EBPα, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 seems to be required for adipogenesis (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). The predominant fatty acid binding protein found in adipocytes is FABP4, also called adipocyte fatty acid binding protein or aP2. FABP4 is also expressed in macrophages (3). FABP4 knockout mice fed a high-fat and high-calorie diet become obese but develop neither insulin resistance nor diabetes, suggesting that this protein might be a link between obesity and insulin resistance and diabetes (4). Mice deficient in both FABP4 and ApoE show protection against atherosclerosis when compared with mice deficient only in ApoE (3). Mice carrying a FABP4 genetic variant exhibit both reduced FABP4 expression and a reduced potential for developing type 2 diabetes and coronary heart disease. A related study in humans indicated a similar pattern, suggesting that FABP4 may be a potential therapeutic target in the treatment of these disorders (1).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). The predominant fatty acid binding protein found in adipocytes is FABP4, also called adipocyte fatty acid binding protein or aP2. FABP4 is also expressed in macrophages (3). FABP4 knockout mice fed a high-fat and high-calorie diet become obese but develop neither insulin resistance nor diabetes, suggesting that this protein might be a link between obesity and insulin resistance and diabetes (4). Mice deficient in both FABP4 and ApoE show protection against atherosclerosis when compared with mice deficient only in ApoE (3). Mice carrying a FABP4 genetic variant exhibit both reduced FABP4 expression and a reduced potential for developing type 2 diabetes and coronary heart disease. A related study in humans indicated a similar pattern, suggesting that FABP4 may be a potential therapeutic target in the treatment of these disorders (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Peroxisome proliferator-activated receptor γ (PPARγ) is a member of the ligand-activated nuclear receptor superfamily and functions as a transcriptional activator (1). PPARγ is preferentially expressed in adipocytes as well as in vascular smooth muscle cells and macrophage (2). Besides its role in mediating adipogenesis and lipid metabolism (2), PPARγ also modulates insulin sensitivity, cell proliferation and inflammation (3). PPARγ transcriptional activity is inhibited by MAP kinase phosphorylation of PPARγ at Ser84 (4,5).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors critical for cellular differentiation, terminal functions and inflammatory response (1). Six members of the family have been characterized (C/EBPα, -β, -γ, -δ, -ε and -ζ) and are distributed in a variety of tissues (1). There are two forms of C/EBPβ, the 38 kDa liver activating protein (LAP) and the 20 kDa liver inhibitory protein (LIP) which may be products of alternative translation. The 38 kDa LAP protein is a transcriptional activator while LIP may act as an inhibitor of C/EBPβ transcriptional activity (2). Phosphorylation of C/EBPβ at distinct sites stimulates its transcriptional activity (3-5). Phosphorylation at serine 105 of rat C/EBPβ, a unique site only present in the rat sequence, seems essential for rat C/EBPβ activation (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors critical for cellular differentiation, terminal functions and inflammatory response (1). Six members of the family have been characterized (C/EBPα, -β, -γ, -δ, -ε and -ζ) and are distributed in a variety of tissues (1). There are two forms of C/EBPβ, the 38 kDa liver activating protein (LAP) and the 20 kDa liver inhibitory protein (LIP) which may be products of alternative translation. The 38 kDa LAP protein is a transcriptional activator while LIP may act as an inhibitor of C/EBPβ transcriptional activity (2). Phosphorylation of C/EBPβ at distinct sites stimulates its transcriptional activity (3-5). Phosphorylation at serine 105 of rat C/EBPβ, a unique site only present in the rat sequence, seems essential for rat C/EBPβ activation (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Adiponectin, also termed AdipoQ, Acrp30, apM1 and GBP28, is an adipokine expressed exclusively in brown and white adipocytes (1). It is secreted into the blood and exists in three major forms: a low molecular weight trimer, a medium molecular weight hexamer and a high molecular weight multimer (1). Adiponectin levels are decreased in obese and insulin-resistant mice and humans (2), suggesting that this adipokine is critical to maintain insulin sensitivity. Adiponectin stimulates the phosphorylation of AMPKα at Thr172 and activates AMPK in skeletal muscle (3). It also stimulates glucose uptake in myocytes (3). The block of AMPK activation by a dominant-negative AMPKα2 isoform inhibits the effect of adiponectin on glucose uptake, indicating that adiponectin stimulates glucose uptake and increases insulin sensitivity through its action on AMPK (3). Adiponectin mutants that are not able to form oligomers larger than trimers have no effect on the AMPK pathway (4). Mutations that render adiponectin unable to form high molecular weight multimers are associated with human diabetes (4), indicating the importance of multimerization for adiponectin activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Myoglobin (MB) is an oxygen-binding protein that contains one polypeptide chain and one heme group. It is expressed in vertebrate skeletal and cardiac muscles where it plays an essential role in the storage and transport of oxygen to mitochondria. Reversible oxygen binding occurs by a linkage with the imidazole nitrogen of the 91st histidine residue in the myoglobin chain. Research studies indicate that the blockade of myoglobin in isolated cardiac myocytes mimics hypoxia when electrically stimulated for paced contractions (1). During fetal development, myoglobin is required to support cardiac function (2). Diving mammals are known to have high concentrations of myoglobin in their blood, which may contribute to their ability to endure long periods of oxygen deprivation during deep dives (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: A group of related glucose transporters (Glut1-5 and 7) mediate the facilitated diffusion of glucose in nonepithelial mammalian tissues. Within insulin-responsive tissues such as muscle and fat, Glut1 contributes to basal glucose uptake while Glut4 is responsible for insulin-stimulated glucose transport (1-3). Glut4 is a 12-transmembrane domain protein that facilitates glucose transport in the direction of the glucose gradient. This transporter localizes to intracellular organelles (endosomes) in unstimulated cells and translocates to the cell surface following insulin stimulation (1,2,4). Translocation of Glut4 is dependent on Akt, which may act by phosphorylating AS160, a RabGAP protein involved in membrane trafficking (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Several oxidoreductases of the protein disulfide isomerase (PDI) family essential for disulfide formation and isomerization are localized to the ER (2). Studies have found that the ER-residing protein endoplasmic oxidoreductin-1 (Ero1) provides the oxidizing potential to the ER in Saccharomyces cerevisiae (3). In vitro experiments demonstrated that Ero1 is oxidized by molecular oxygen in a FAD-dependent manner and the oxidized Ero1 in turn serves as an oxidant for PDI (4). Two human homologs of Ero1, Ero1-like (Ero1-Lα and β) have been identified (2,5). Ero1-Lα is an ER membrane-associated N-glycoprotein that promotes oxidative protein folding and has been shown to be expressed in several cell lines and tissues (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The placenta-specific gene 8 (Plac8) encodes a chromatin-binding protein that was first identified from placenta and that is highly expressed in plasmacytoid dendritic cells (1,2). Research studies indicate that Plac8 plays a role in immune function and is essential in the differentiation of brown fat (3,4). During brown fat differentiation, Plac8 interacts with the transcription factor C/EBPβ at its promoter sequence to activate the transcription of C/EBPβ (4). Experimental deletion of Plac8 in mice leads to impaired innate immune function, abnormal brown fat function, cold intolerance, and obesity (3,4). Additional studies examining the spread of colorectal carcinoma suggest a possible role for Plac8 in cancer invasion, possibly through promoting the epithelial-to-mesenchymal transition seen during tumor progression (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: PPARγ coactivator-1α (PGC-1α) was originally identified as a transcriptional coactivator whose expression closely correlated with adaptive thermogenesis following exposure to cold temperatures (1). Named for its association with the nuclear receptor peroxisome-proliferator activated receptor (PPARγ), PGC-1α interacts with a diverse array of transcription factors to regulate numerous aspects of cell physiology (2). PGC-1α helps to regulate cell processes important in adaptive thermogenesis and energy metabolism, including the related functions of glucose uptake, gluconeogenesis, insulin secretion, and mitochondrial biogenesis (3). Long thought to be a potential therapeutic target for the treatment of type II diabetes, obesity, cardiomyopathy, or other metabolic disorders (reviewed in 4), a recent functional survey found no obvious differences in PPARγ activity associated with recognized PGC-1α variants (5).