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Product listing: Phospho-IRS-1 (Ser302) Antibody, UniProt ID P35568 #2384 to SGLT2 Antibody, UniProt ID P31639 #14210

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

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

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and NADH to lactate and NAD+. When the oxygen supply is too low for mitochondrial ATP production, this reaction recycles NADH generated in glycolysis to NAD+, which reenters glycolysis. The major form of LDH found in muscle cells is the A (LDHA) isozyme. The LDHA promoter contains HIF-1α binding sites (1). LDHA expression is induced under hypoxic conditions (2). During intensive and prolonged muscle exercise, lactate accumulates in muscle cells when the supply of oxygen does not meet demand. When oxygen levels return to normal, LDH converts lactate to pyruvate to generate ATP in the mitochondrial electron transport chain.

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: LKB1 (STK11) is a serine/threonine kinase and tumor suppressor that helps control cell structure, apoptosis and energy homeostasis through regulation of numerous downstream kinases (1,2). A cytosolic protein complex comprised of LKB1, putative kinase STRAD, and the MO25 scaffold protein, activates both AMP-activated protein kinase (AMPK) and several AMPK-related kinases (3). AMPK plays a predominant role as the master regulator of cellular energy homeostasis, controlling downstream effectors that regulate cell growth and apoptosis in response to cellular ATP concentrations (4). LKB1 appears to be phosphorylated in cells at several sites, including human LKB1 at Ser31/325/428 and Thr189/336/363 (5).Mutation in the corresponding LKB1 gene causes Peutz-Jeghers syndrome (PJS), an autosomal dominant disorder characterized by benign GI tract polyps and dark skin lesions of the mouth, hands, and feet (6). A variety of other LKB1 gene mutations have been associated with the formation of sporadic cancers in several tissues (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: LKB1 (STK11) is a serine/threonine kinase and tumor suppressor that helps control cell structure, apoptosis and energy homeostasis through regulation of numerous downstream kinases (1,2). A cytosolic protein complex comprised of LKB1, putative kinase STRAD, and the MO25 scaffold protein, activates both AMP-activated protein kinase (AMPK) and several AMPK-related kinases (3). AMPK plays a predominant role as the master regulator of cellular energy homeostasis, controlling downstream effectors that regulate cell growth and apoptosis in response to cellular ATP concentrations (4). LKB1 appears to be phosphorylated in cells at several sites, including human LKB1 at Ser31/325/428 and Thr189/336/363 (5).Mutation in the corresponding LKB1 gene causes Peutz-Jeghers syndrome (PJS), an autosomal dominant disorder characterized by benign GI tract polyps and dark skin lesions of the mouth, hands, and feet (6). A variety of other LKB1 gene mutations have been associated with the formation of sporadic cancers in several tissues (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO2 in the presence of NAD+. Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis. The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and the citric acid cycle and lipid metabolism. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is comprised of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: α and β. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the α subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration and early death (2).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: TBC1D1 is a paralog of AS160 (1) and both proteins share about 50% identity (2). TBC1D1 was shown to be a candidate gene for severe obesity (3). It plays a role in Glut4 translocation through its GAP activity (2,4). Studies indicate that TBC1D1 is highly expressed in skeletal muscle (1). Insulin, AICAR, and contraction directly regulate TBC1D1 phosphorylation in this tissue (1). Three AMPK phosphorylation sites (Ser231, Ser660, and Ser700) and one Akt phosphorylation site (Thr590) were identified in skeletal muscle (5). Muscle contraction or AICAR treatment increases phosphorylation on Ser231, Ser660, and Ser700 but not on Thr590; insulin increases phosphorylation on Thr590 only (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: TBC1D1 is a paralog of AS160 (1) and both proteins share about 50% identity (2). TBC1D1 was shown to be a candidate gene for severe obesity (3). It plays a role in Glut4 translocation through its GAP activity (2,4). Studies indicate that TBC1D1 is highly expressed in skeletal muscle (1). Insulin, AICAR, and contraction directly regulate TBC1D1 phosphorylation in this tissue (1). Three AMPK phosphorylation sites (Ser231, Ser660, and Ser700) and one Akt phosphorylation site (Thr590) were identified in skeletal muscle (5). Muscle contraction or AICAR treatment increases phosphorylation on Ser231, Ser660, and Ser700 but not on Thr590; insulin increases phosphorylation on Thr590 only (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Glucose homeostasis is regulated by hormones and cellular energy status. Elevations of blood glucose during feeding stimulate insulin release from pancreatic β-cells through a glucose sensing pathway. Feeding also stimulates release of gut hormones such as glucagon-like peptide-1 (GLP-1), which further induces insulin release, inhibits glucagon release and promotes β-cell viability. CREB-dependent transcription likely plays a role in both glucose sensing and GLP-1 signaling (1). The protein CRTC2 (CREB-regulated transcription coactivator 2)/TORC2 (transducer of regulated CREB activity 2) functions as a CREB co-activator (2,3) and is implicated in mediating the effects of these two pathways (4). In quiescent cells, CRTC2/TORC2 is phosphorylated at Ser171 and becomes sequestered in the cytoplasm via an interaction with 14-3-3 proteins. Glucose and gut hormones lead to the dephosphorylation of CRTC2/TORC2 and its dissociation from 14-3-3 proteins. Dephosphorylated CRTC2/TORC2 enters the nucleus to promote CREB-dependent transcription. CRTC2/TORC2 plays a key role in the regulation of hepatic gluconeogenic gene transcription in response to hormonal and energy signals during fasting (5).CRTC2/TORC2-related proteins CRTC1/TORC1 and CRTC3/TORC3 also act as CREB co-activators (2,3). CRTC1/TORC1, CRTC2/TORC2 and CRTC3/TORC3 associate with the HTLV Tax protein to promote Tax-dependent transcription of HTLV-1 long terminal repeats (6,7). CRTC1/TORC1 is highly phosphorylated at Ser151 in mouse hypothalamic cells under basal conditions (8). When these cells are exposed to cAMP or a calcium activator, CRTC1/TORC1 is dephosphorylated and translocates into the nucleus (8). CRTC1/TORC1 is essential for energy balance and fertility (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Pyruvate kinase is a glycolytic enzyme that catalyses the conversion of phosphoenolpyruvate to pyruvate. In mammals, the M1 isoform (PKM1) is expressed in most adult tissues (1). The M2 isoform (PKM2) is an alternatively spliced variant of M1 that is expressed during embryonic development (1). Research studies found that cancer cells exclusively express PKM2 (1-3). PKM2 is shown to be essential for aerobic glycolysis in tumors, known as the Warburg effect (1). When cancer cells switch from the M2 isoform to the M1 isoform, aerobic glycolysis is reduced and oxidative phosphorylation is increased (1). These cells also show decreased tumorigenicity in mouse xenografts (1). Recent studies showed that PKM2 is not essential for all tumor cells (4). In the tumor model studied, PKM2 was found to be active in the non-proliferative tumor cell population and inactive in the proliferative tumor cell population (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Phospholipase A2 (PLA2) is a superfamily of enzymes that hydrolyze glycero-3-phosphocholines and release fatty acids and lysophospholipids (1). PLA2G1B is a member of this superfamily in the 1B group that is expressed most highly in the pancreatic acinar cells (2). Evidence suggests that PLA2G1B plays a role in the absorption and storage of extra energy as fats are metabolized (1,2). Lysophospholipids generated by PLA2G1B inhibit fatty acid oxidation in the liver and reduce energy expenditure, leading to diet-induced obesity and type 2 diabetes with a high fat diet (1). Therefore, a potential intervention of obesity and diabetes could target PLA2G1B in the digestive tract (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Peroxiredoxin 2 (PRDX2, PRXII, NKEFB) is a ubiquitously expressed thioredoxin peroxidase. The enzyme catalyzes the reduction of hydrogen peroxide and organic hydroperoxides via the thioredoxin system (1). An antioxidant, PRDX2 neutralizes endogenous reactive oxygen species (ROS) and regulates cytokine-induced peroxide levels for normal cell function (2). Research studies have shown that PRDX2 plays important roles in inflammation, cancer, and natural killer (NK) cell activation (3). During cancer progression, PRDX2 is upregulated and protects cancer cells from oxidative stress-induced apoptosis (4, 5). In inflammatory diseases such as infection, myocardial infarction, and ischemia, PRDX2 not only protects (host) cells from oxidative stress-induced death, but is also released into extracellular space to trigger local inflammation and to activate NK cells for innate immune response (6, 7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Peroxiredoxin 6 (Prdx6) belongs to an antioxidant enzyme family of non-seleno peroxidases (prdx). It is a unique member of the Prdx family exhibiting both glutathione peroxidase and phospholipase A2 activities (1,2). Prdx6 regulates phospholipid turnover as well as protects cells against oxidative injury. Prdx6 is expressed in all major organs with a particularly high level in lung where it regulates lung surfactant phospholipid synthesis and turnover (3-5). Studies show Prdx6 is aberrantly expressed in various cancers and promotes cancer cell metastasis and invasion (6,7). Elevated expression of Prdx6 and other prdx family members contributes to drug resistance in cancer cells (8,9). Prdx6 is also expressed in neutrophils, where it regulates the function of these cells and activates NADPH oxidase (Nox2) ( 10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Protein-tyrosine phosphatase 1B (PTP1B) is the original member of the protein tyrosine phosphatase (PTP) family of proteins (1). PTP1B is highly expressed in insulin-responsive tissues and negatively regulates insulin, as well as integrin, through dephosphorylation of phosphotyrosine residues (2-4). PTP1B knockout mice show resistance to dietary weight gain and enhanced insulin sensitivity, suggesting a possible role in treatment of obesity as well as type 2 diabetes (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Mitochondrial pyrroline-5-carboxylate reductase 1 (PYCR1) catalyzes the last step in proline biosynthesis (1). Research studies show that proline is a limiting amino acid to clear cell renal cell carcinoma (ccRCC). PYCR1 expression is induced in kidney cancer cells to compensate for the proline shortage and maintain cancer cell growth. Furthermore, PYCR1 knockdown inhibits ccRCC cell proliferation in the absence of proline, suggesting this enzyme as a potential cancer therapeutic target (2). In addition, breast cancer cells also express high levels of PYCR1 (2,3). Proline is restrictive to invasive ductal breast carcinoma cells, indicating proline vulnerability in the breast cancer formation (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The pyruvate dehydrogenase complex catalyzes the conversion of pyruvate and CoA into acetyl-CoA and CO2 in the presence of NAD+. Acetyl-CoA then goes into the citric acid cycle where it reacts with oxaloacetate to form citrate. Acetyl-CoA is also used for fatty acid and cholesterol biosynthesis. The reaction of oxidative decarboxylation of pyruvate therefore serves as a critical link between glycolysis and the citric acid cycle and lipid metabolism. In mammalian cells, the pyruvate dehydrogenase complex is located in the mitochondrial matrix (1). This complex is comprised of three enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). Pyruvate dehydrogenase (E1) consists of two subunits: α and β. This enzyme catalyzes the removal of CO2 from pyruvate. Mutations in the α subunits of pyruvate dehydrogenase (E1) lead to congenital defects that are usually associated with lactic acidosis, neurodegeneration and early death (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: SREBP cleavage activating protein (SCAP) is a membrane-bound protein essential in regulating sterol regulatory element binding protein (SREBP) processing (1). In cholesterol-starved cells, SREBPs move from the ER to the Golgi apparatus with the help of SCAP, where the precursor SREBPs are cleaved by site-1 (S1P) and site-2 (S2P) proteases (1,2). Released SREBP amino-terminal domains enter the nucleus and bind to sterol response elements located in the promoters of a number of genes responsible for the cholesterol synthesis (1,2). Research studies show that the SCAP/SREBP pathway is critical for diabetic fatty liver development and carbohydrate-induced hypertriglyceridemia in mice (3). In addition, the SCAP/SREBP pathway is required to protect cancer cells from lipotoxicity (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Stearoyl-CoA desaturase 1 (SCD1) is a key lipogenic enzyme found in the endoplasmic reticulum that catalyzes the conversion of palmitoyl–CoA and stearoyl–CoA to palmitoleoyl–CoA (16:1) and oleoyl–CoA (18:1) (1-3). Palmitoleate and oleate are the major components of triglycerides, membrane phospholipids and cholesterol esters (1). SCD1-knockout mice show improved insulin sensitivity and reduced body fat (1). Disruption of SCD1 in mouse brown adipose tissue strengthens insulin signaling and results in increased translocation of Glut4 to plasma membrane and enhanced uptake of glucose (4). Furthermore, SCD1 is essential for the onset of diet-induced body weight gain (1) and insulin resistance in the liver (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Stearoyl-CoA desaturase 1 (SCD1) is a key lipogenic enzyme found in the endoplasmic reticulum that catalyzes the conversion of palmitoyl–CoA and stearoyl–CoA to palmitoleoyl–CoA (16:1) and oleoyl–CoA (18:1) (1-3). Palmitoleate and oleate are the major components of triglycerides, membrane phospholipids and cholesterol esters (1). SCD1-knockout mice show improved insulin sensitivity and reduced body fat (1). Disruption of SCD1 in mouse brown adipose tissue strengthens insulin signaling and results in increased translocation of Glut4 to plasma membrane and enhanced uptake of glucose (4). Furthermore, SCD1 is essential for the onset of diet-induced body weight gain (1) and insulin resistance in the liver (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Succinate dehydrogenase (SDH), also known as Complex II or succinate:quinone oxidoreductase, is a key component of the citric acid cycle and the electron transport chain (1). Specifically, it is involved in the oxidation of succinate (2). SDH consists of four subunits: SDHA, SDHB, SDHC, and SDHD (3). Research studies have shown that defects in SDHA cause complex II deficiency (2). In addition, investigators have observed reduction of SDHA in the striatum of patients with Huntington’s disease (3), and reduction of SDHB, SDHC, and SDHD in paragangliomas and phenochromocytomas (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: Sodium/glucose cotransporter 1 (SGLT1) is an active glucose transporter, which utilizes sodium gradients to transport glucose into cells independent of extracellular glucose concentration. SGLT1 is an essential glucose active transport protein that helps maintain high intracellular glucose levels (1). Expression of SGLT1 is mainly seen in intestinal and kidney epithelial cells, although a recent study also characterized SGLT1 expression in cardiac myocytes (2). Abnormal SGLT1 expression may be associated with cases of type 2 diabetes mellitus and myocardial ischaemia (2). Mutation of the corresponding SGLT1 gene can result in congenital glucose/galactose malabsorption, which can lead to neonatal diarrhea and subsequent death if left untreated (3). A recent study of the role of EGFR in cancer cell survival indicates that EGFR can prevent autophagic cell death independent of EGFR kinase activity because the receptor interacts with and stabilizes SLGT1 to maintain basal intracellular glucose levels (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Na(+)/glucose cotransporter 2 (SGLT2) is one of the two main glucose transporters in the kidney proximal convoluted tubule. It is activated by Protein Kinase A and Protein Kinase C, likely through phosphorylation of Ser624 (1,2). SGLT2 is responsible for the majority of glucose reabsorption in the kidney (3,4), and mutations in SGLT2 are known to cause familial renal glucosuria (5,6). SGLT2 is a therapeutic target for type 2 diabetes. Inhibitors of SGLT2 have been developed in order to treat people with type 2 diabetes (7).