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Polyclonal Antibody Immunofluorescence Immunocytochemistry Lipid Catabolic Process

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

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

Background: HSL (hormone-sensitive lipase) catalyzes the hydrolysis of triacylglycerol, the rate-limiting step in lipolysis. Lipolytic stimuli activate adenylyl cyclase and thus increase intracellular cAMP levels, which in turn activate protein kinase A (PKA). PKA phosphorylates HSL at Ser563, Ser659, and Ser660, which stimulates HSL activity (1,2). In contrast, AMPK phosphorylates HSL at Ser565, which reduces HSL phosphorylation at Ser563 by PKA and inhibits HSL activity (2,3). Recent work indicates that phosphorylation at Ser600 by p44/42 MAPKs also enhances the enzymatic activity of HSL (4).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: HSL (hormone-sensitive lipase) catalyzes the hydrolysis of triacylglycerol, the rate-limiting step in lipolysis. Lipolytic stimuli activate adenylyl cyclase and thus increase intracellular cAMP levels, which in turn activate protein kinase A (PKA). PKA phosphorylates HSL at Ser563, Ser659, and Ser660, which stimulates HSL activity (1,2). In contrast, AMPK phosphorylates HSL at Ser565, which reduces HSL phosphorylation at Ser563 by PKA and inhibits HSL activity (2,3). Recent work indicates that phosphorylation at Ser600 by p44/42 MAPKs also enhances the enzymatic activity of HSL (4).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: HSL (hormone-sensitive lipase) catalyzes the hydrolysis of triacylglycerol, the rate-limiting step in lipolysis. Lipolytic stimuli activate adenylyl cyclase and thus increase intracellular cAMP levels, which in turn activate protein kinase A (PKA). PKA phosphorylates HSL at Ser563, Ser659, and Ser660, which stimulates HSL activity (1,2). In contrast, AMPK phosphorylates HSL at Ser565, which reduces HSL phosphorylation at Ser563 by PKA and inhibits HSL activity (2,3). Recent work indicates that phosphorylation at Ser600 by p44/42 MAPKs also enhances the enzymatic activity of HSL (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin)

Background: The maintenance of glucose homeostasis is an essential physiological process that is regulated by hormones. An elevation in blood glucose levels during feeding stimulates insulin release from pancreatic β cells through a glucose sensing pathway (1). Insulin is synthesized as a precursor molecule, proinsulin, which is processed prior to secretion. A- and B-peptides are joined together by a disulfide bond to form insulin, while the central portion of the precursor molecule is cleaved and released as the C-peptide. Insulin stimulates glucose uptake from blood into skeletal muscle and adipose tissue. Insulin deficiency leads to type 1 diabetes mellitus (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin)

Background: Glucose homeostasis is regulated by hormones. Elevation of blood glucose levels during feeding stimulates insulin release from pancreatic β-cells through a glucose sensing pathway (1). Proinsulin, the insulin precursor molecule, is processed prior to its secretion. Insulin is composed of A-peptide and B-peptide which are joined by a disulfide bond. The center one-third of the molecule is cleaved and released as C-peptide, which has a longer half-life than insulin (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Triacylglycerol is stored in lipid droplets as a primary energy reserve. Perilipin is localized at the periphery of lipid droplets and serves as a protective coating against lipases (1-3). Evidence suggests that PKA regulates lipolysis by phosphorylating perilipin (1,2,4,5). Phosphorylation of perilipin results in the conformational change that exposes lipid droplets to endogenous lipases, such as hormone-sensitive lipases (2). Hence, perilipin plays a pivotal role in lipid storage (2,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Triacylglycerol is stored in lipid droplets as a primary energy reserve. Perilipin is localized at the periphery of lipid droplets and serves as a protective coating against lipases (1-3). Evidence suggests that PKA regulates lipolysis by phosphorylating perilipin (1,2,4,5). Phosphorylation of perilipin results in the conformational change that exposes lipid droplets to endogenous lipases, such as hormone-sensitive lipases (2). Hence, perilipin plays a pivotal role in lipid storage (2,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Triglycerides form an important energy store in many living organisms. Adipose tissue serves as the primary storage depot for triglycerides in mammals. Lipolytic enzymes mobilize triglycerides during periods of starvation to provide organisms with necessary energy. Hormone-sensitive lipase (HSL), the first identified lipolytic enzyme, hydrolyzes triglycerides in mammalian adipose tissues (1-3). Additional lipolytic enzymes, including adipose triglyceride lipase (ATGL), have also been discovered. The primary function of ATGL is to catalyze the hydrolysis of the first ester bond of lipid molecules. This enzyme may provide diglyceride substrates for HSL hydrolysis. ATGL is abundantly expressed in murine white and brown adipose tissue, and is highly substrate specific (4). ATGL was independently identified as desnutrin (5) and the TG-hydrolace inducible phospholipase-A2-ζ (6).

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

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

Background: Lipin 1 was identified as a nuclear protein required for adipose tissue development (1). The expression of Lipin 1 is induced during adipocyte differentiation (1). The abnormal development of adipose tissues caused by mutations in the lipin 1 gene results in lipodystrophy, a condition associated with low body fat, fatty liver, hypertriglyceridemia, and insulin resistance (1). Lipin 1 plays a role in lipid metabolism in various tissues and cell types including liver, muscle, adipose tissues, and neuronal cell lines (2-4). It has dual functions at the molecular level: Lipin 1 serves as a transcriptional coactivator in liver, and a phosphatidate phosphatase in triglyceride and phospholipid biosynthesis pathways (5). Lipin 1 is regulated by mTOR, illustrating a connection between adipocyte development and nutrient-sensing pathways (6). It also mediates hepatic insulin signaling by TORC2/CRTC2 (7).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Dog, Hamster, Human, Mouse, Pig, Rat

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

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Chicken, D. melanogaster, Dog, Guinea Pig, Hamster, Human, Monkey, Mouse, Pig, Rat

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

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$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).