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Mouse Nitric Oxide Mediated Signal Transduction

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

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

Background: Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated eNOS (D9A5L) Rabbit mAb #32027.
APPLICATIONS
REACTIVITY
Bovine, Human, Mouse, Rat

Application Methods: Western Blotting

Background: Endothelial nitric-oxide synthase (eNOS) is an important enzyme in the cardiovascular system. It catalyzes the production of nitric oxide (NO), a key regulator of blood pressure, vascular remodeling, and angiogenesis (1,2). The activity of eNOS is regulated by phosphorylation at multiple sites. The two most thoroughly studied sites are the activation site Ser1177 and the inhibitory site Thr495 (3). Several protein kinases including Akt/PKB, PKA, and AMPK activate eNOS by phosphorylating Ser1177 in response to various stimuli (4,5). In contrast, bradykinin and H2O2 activate eNOS activity by promoting both Ser1177 phosphorylation and Thr495 dephosphorylation (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in mouse cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated iNOS (D6B6S) Rabbit mAb #13120.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated iNOS (D6B6S) Rabbit mAb #13120.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated iNOS (D6B6S) Rabbit mAb #13120.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Nitric Oxide Synthase (NOS) catalyzes the formation of nitric oxide (NO) and citruline from L-arginine, oxygen and cofactors. Three family members have been characterized: neuronal NOS (nNOS), which is found primarily in neuronal tissue; inducible NOS (iNOS), which is induced by interferon gamma and lipopolysaccharides in the kidney and cardiovascular system; and endothelial NOS (eNOS), which is expressed in blood vessels (1). NO is a messenger molecule with diverse functions throughout the body including the maintenance of vascular integrity, homeostasis, synaptic plasticity, long-term potentiation, learning, and memory (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Angiotensinogen (AGT) is the primary precursor of angiotensins, peptide hormones that play a central role in the renin-angiotensin system (RAS) (1-3). AGT is a secreted protein synthesized primarily by the liver and secreted into circulation. Upon binding to renin, the amino terminal fragment of AGT is cleaved and released as a decapeptide hormone termed angiotensin 1 (Ang I). Ang I is subsequently processed by angiotensin converting enzyme (ACE) to generate angiotensin II (Ang II), which acts on AT1 and AT2 receptors in the central nervous system to increase production of anti-diuretic hormone (ADH), while promoting vasoconstriction in the peripheral circulation (4). Aberrant upregulation of Ang II has been associated with numerous clinical conditions, including hypertension, atherosclerosis, myocardial hypertrophy, and obesity (5-7). Alternative cleavage products of Ang I (e.g., Ang 1-7) can also be generated by ACE2 cleavage, some of which display biological functions that are distinct from Ang II (8). Treatments that target the RAS (e.g., ACE inhibitors) are consequently of significant importance in the treatment of hypertensive and hypertensive-related disorders(5-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: MAFA belongs to the musculoaponeurotic fibrosarcoma (MAF) family of basic leucine-zipper transcription factors (1). In the mouse embryo, MAFA expression is first detected at E13.5, restricted to Nkx6.1-positive insulin-producing islet cells (2). Expression of the MAFA gene is sensitive to physiological glucose levels, and genomic targets regulated by MAFA include β-cell transcription factors (e.g., PDX1) and the insulin gene (2, 3). Ectopic expression of MAFA was shown to induce insulin production by pancreatic α-cells (2), while conditional overexpression of MAFA in vivo promoted transdifferentiation of α-cells into insulin-producing β-cells (4). Targeted deletion of the MAFA gene in mice likewise led to a loss of β-cell identity and function (5). Collectively, these data suggest that MAFA is critical for the development, maintenance, and physiological function of insulin-producing pancreatic β-cells, highlighting its potential utility as a target for translational and clinical research studies in diabetes (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: NeuroD is a member of the basic helix-loop-helix (bHLH) family of transcription factors. These proteins function by forming heterodimers with E-proteins and binding to the canonical E-box sequence CANNTG (1,2). Neuronal activity results in CaMKII-mediated phosphorylation of NeuroD at Ser336, which is necessary for formation and growth of dendrites (3,4). NeuroD is also phosphorylated at Ser274 though the results are context dependent as phosphorylation by Erk stimulates NeuroD activity in pancreatic β-cells while phosphorylation by GSK-3β inhibits NeuroD in neurons (3). NeuroD is crucially important in both the pancreas and developing nervous system, and plays a large role in the development of the inner ear and mammalian retina (3). Mice lacking NeuroD become severely diabetic and die shortly after birth due to defects in β-cell differentiation (2,3,5,6). The lack of NeuroD in the brain results in severe defects in development (5). Human mutations have been linked to a number of types of diabetes including type I diabetes mellitus and maturity-onset diabetes of the young (1,3).

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

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

Background: The pancreatic duodenal homeobox gene-1 (Pdx1) is a transcription factor that contributes to pancreas development, pancreatic β-cell differentiation, and mature β-cell function (1,2). It plays an essential role in the commitment of endoderm to a pancreatic and later β-cell phenotype (2,3). In the mature pancreas, Pdx1 expression is more restricted to the pancreatic β-cells (3), where it promotes the expression of genes important for β-cell functions such as insulin, glucokinase, and Glut2 (4-6). Mutations of the corresponding Pdx1 gene may be associated with diabetes and cases of pancreatic insufficiency (7).

$108
250 PCR reactions
500 µl
SimpleChIP® Mouse PDX1 Promoter Primers contain a mix of forward and reverse PCR primers that are specific to a region of the mouse pancreatic and duodenal homeobox 1 (PDX1) gene. These primers can be used to amplify DNA that has been isolated using chromatin immunoprecipitation (ChIP). Primers have been optimized for use in SYBR® Green quantitative real-time PCR and have been tested in conjunction with SimpleChIP® Enzymatic Chromatin IP Kits #9004 and #9005 and ChIP-validated antibodies from Cell Signaling Technology®.
REACTIVITY
Mouse

Background: The chromatin immunoprecipitation (ChIP) assay is a powerful and versatile technique used for probing protein-DNA interactions within the natural chromatin context of the cell (1,2). This assay can be used to either identify multiple proteins associated with a specific region of the genome or to identify the many regions of the genome bound by a particular protein (3-6). ChIP can be used to determine the specific order of recruitment of various proteins to a gene promoter or to "measure" the relative amount of a particular histone modification across an entire gene locus (3,4). In addition to histone proteins, the ChIP assay can be used to analyze binding of transcription factors and co-factors, DNA replication factors, and DNA repair proteins. When performing the ChIP assay, cells are first fixed with formaldehyde, a reversible protein-DNA cross-linking agent that "preserves" the protein-DNA interactions occurring in the cell (1,2). Cells are lysed and chromatin is harvested and fragmented using either sonication or enzymatic digestion. Fragmented chromatin is then immunoprecipitated with antibodies specific to a particular protein or histone modification. Any DNA sequences that are associated with the protein or histone modification of interest will co-precipitate as part of the cross-linked chromatin complex and the relative amount of that DNA sequence will be enriched by the immunoselection process. After immunoprecipitation, the protein-DNA cross-links are reversed and the DNA is purified. Standard PCR or quantitative real-time PCR are often used to measure the amount of enrichment of a particular DNA sequence by a protein-specific immunoprecipitation (1,2). Alternatively, the ChIP assay can be combined with genomic tiling micro-array (ChIP on chip) techniques, high throughput sequencing (ChIP-Seq), or cloning strategies, all of which allow for genome-wide analysis of protein-DNA interactions and histone modifications (5-8). SimpleChIP® primers have been optimized for amplification of ChIP-isolated DNA using real-time quantitative PCR and provide important positive and negative controls that can be used to confirm a successful ChIP experiment.

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometric analysis of human cells. The unconjugated Phospho-Akt (Ser473) (193H12) Rabbit mAb #4058 reacts with phospho-Akt (Ser473) from human, mouse and rat. CST expects that Phospho-Akt (Ser473) (193H12) Rabbit mAb (Alexa Fluor® 488 Conjugate) will also recognize phospho-Akt (Ser473) in these species.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

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).

$303
100 µl
$715
300 µl
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Rat

Application Methods: 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).

$307
100 µl
$719
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: 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).

$122
20 µl
$307
100 µl
$719
300 µl
APPLICATIONS
REACTIVITY
Human, Mouse, 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).