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Product listing: eIF4A (C32B4) Rabbit mAb, UniProt ID P38919 #2013 to eNOS (D9A5L) Rabbit mAb, UniProt ID P29474 #32027

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

Application Methods: Western Blotting

Background: A variety of factors contribute to the important biological event of initiation of translation. The eIF4F complex of translation initiation factors binds to the 5' m7 GTP cap to open up the mRNA secondary structure and allow small ribosome subunit binding (1). eIF4A, an eIF4 complex component that acts as an ATP-dependent RNA helicase, unwinds the secondary structure of the 5' mRNA untranslated region to mediate ribosome binding (2,3). In addition, eIF4A has recently been shown to repress Dpp/BMP signalling in a translation-independent manner in Drosophila (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Eukaryotic initiation factor 4B (eIF4B) is thought to assist the eIF4F complex in translation initiation. In plants, eIF4B is known to interact with the poly-(A) binding protein, increasing its poly-(A) binding activity (1). Heat shock and serum starvation cause dephosphorylation of eIF4B at multiple sites with kinetics similar to those of the corresponding inhibition of translation, while phosphorylation of eIF4B following insulin treatment correlates well with an observed increase in translation (2-5). Multiple kinases, including p70 S6 kinase, can phosphorylate eIF4B in vitro, and at least one serum-inducible eIF4B phosphorylation site is sensitive to rapamycin and LY294002 (6). Recently, Ser406 was identified as a novel phosphorylation site regulated by mitogens (7), and the phosphorylation of this site is dependent on MEK and mTOR activity (7). This phosphorylation is shown to be essential for the translational activity of eIF4B (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 eIF4E (C46H6) Rabbit mAb #2067.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 4E (eIF4E) binds to the mRNA cap structure to mediate the initiation of translation (1,2). eIF4E interacts with eIF4G, a scaffold protein that promotes assembly of eIF4E and eIF4A into the eIF4F complex (2). eIF4B is thought to assist the eIF4F complex in translation initiation. Upon activation by mitogenic and/or stress stimuli mediated by Erk and p38 MAPK, Mnk1 phosphorylates eIF4E at Ser209 in vivo (3,4). Two Erk and p38 MAPK phosphorylation sites in mouse Mnk1 (Thr197 and Thr202) are essential for Mnk1 kinase activity (3). The carboxy-terminal region of eIF4G also contains serum-stimulated phosphorylation sites, including Ser1108, Ser1148, and Ser1192 (5). Phosphorylation at these sites is blocked by the PI3 kinase inhibitor LY294002 and by the FRAP/mTOR inhibitor rapamycin.

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

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

Background: Eukaryotic initiation factor 4E (eIF4E) binds to the mRNA cap structure to mediate the initiation of translation (1,2). eIF4E interacts with eIF4G, a scaffold protein that promotes assembly of eIF4E and eIF4A into the eIF4F complex (2). eIF4B is thought to assist the eIF4F complex in translation initiation. Upon activation by mitogenic and/or stress stimuli mediated by Erk and p38 MAPK, Mnk1 phosphorylates eIF4E at Ser209 in vivo (3,4). Two Erk and p38 MAPK phosphorylation sites in mouse Mnk1 (Thr197 and Thr202) are essential for Mnk1 kinase activity (3). The carboxy-terminal region of eIF4G also contains serum-stimulated phosphorylation sites, including Ser1108, Ser1148, and Ser1192 (5). Phosphorylation at these sites is blocked by the PI3 kinase inhibitor LY294002 and by the FRAP/mTOR inhibitor rapamycin.

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

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

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

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

Application Methods: Western Blotting

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The initiation of translation is an important biological event and a variety of factors contribute to this process. Members of the eIF4 translation initiation factor family bind to the 5' m7GTP mRNA cap and unwind the mRNA secondary structure (1,2). The amino-terminal portion of eIF4G physically associates with eIF4E to stimulate the binding of eIF4E to the mRNA cap structure (3). eIF4G also interacts with eIF3 and eIF4A and serves as an adaptor molecule in the eIF4 complex (4). Moreover, eIF4G plays a role in internal ribosomal entry site (IRES)-mediated initiation of translation (5,6). The eIF4G family includes eIF4G1 (eIF4GI), eIF4G2 (p97, DAP5 or NAT1), and eIF4G3 (eIF4GII) (7). These factors share a homologous sequence that provides for interaction with initiation factors eIF3 and eIF4A. Both eIF4G1 and eIF4G3 are involved in cap-dependent translation, while eIF4G2 plays a role in IRES-mediated translation of some genes during cell stress (7,8).

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

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

Background: A variety of factors contribute to the initiation of translation. Eukaryotic translation initiation factor 4H (eIF4H) was purified to near homogeneity from rabbit reticulocyte lysate and shown to stimulate translation in an assay deficient in eIF4F and eIF4B (1). eIF4H induces the RNA-dependent ATP hydrolysis catalyzed by the initiation factors eIF4A and eIF4B (1,2). eIF4H was further shown to stimulate the initial rate and extent of eIF4A-mediated mRNA secondary structure unwinding (3). Interaction between eIF4H and the herpes simplex virus shutoff protein (Vhs) appears to be important for Vhs-mediated degradation of mRNA (4). Deletion of a large region of chromosome 7, including the corresponding eIF4H gene, results in Williams-Beuren Syndrome (WBS), an autosomal dominant disorder that can present with cardiovascular problems, mental retardation and distinctive facial features (5).

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

Application Methods: Western Blotting

Background: Eukaryotic translation initiation factor 5 (eIF5) is crucial for the assembly of translation initiation complex and plays an important role in protein synthesis (1). eIF5 interacts with the 43S initiation complex to stimulate hydrolysis of GTP bound to eIF2 (1-3). Studies suggest that eIF5 functions as the GTPase-activating protein (GAP) in the hydrolysis of GTP-bound eIF2 (4,5). This hydrolysis leads to the release of initiation factors from the 40S ribosomal subunit, which is a necessary step in the formation of the 80S initiation complex (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 5A (eIF5A) is an mRNA-binding protein that is involved in translation elongation and plays an important role in promoting translation of polyproline motifs (1-4). The eIF5A (eIF5A1) and eIF5A2 genes encode the two vertebrate eIF5A isoforms. While eIF5A1 is expressed constitutively in all tissues, eIF5A2 is mainly expressed in gonads. eIF5A and eIF5A2 are the only identified proteins that contain the distinctive amino acid hypusine, which is generated posttranslationally from lysine through a highly conserved polyamine metabolism pathway. eIF5A function and hypusine modification are both essential for cell proliferation, as knock down of eIF5A expression or blocking eIF5A hypusine modification suppresses cancer cell proliferation (5-7). Interestingly, eIF5A is an identified component of a tumor suppressor network of the polyamine-hypusine axis. Co-suppression of both eIF5A and adenosylmethionine decarboxylase 1 (AMD1) promotes lymphomagenesis in mice, while heterozygous deletions of the corresponding AMD1 and eIF5A genes often occur together in human lymphomas (8).

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

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

Background: Eukaryotic initiation factor 6 (eIF6) is reqiured for the 60S ribosomal subunit assembly in the nucleolus (1). In the cytoplasm, this protein is bound to 60S ribosome subunits and prevents them from joining 40S ribosome subunits to form 80S ribosomes (2). eIF6 is also shown to associate with the RNA-induced silencing complex (RISC) (3). Deletion of eIF6 abolishes the miRNA-mediated gene silencing (3). eIF6 may play its essential role in miRNA-mediated silencing by inhibiting translation initiation or ribosome recycling (3).

$305
50 assays
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated ELAVL1/HuR (D9W7E) Rabbit mAb #12582.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The ELAVL (embryonic lethal, abnormal vision and Drosophila-like) family of proteins includes ELAVL1/HuR, ELAVL2/HuB, ELAVL3/HuC and ELAVL4/HuD (1). ELAVL1/HuR is ubiquitously expressed whereas expression of the other three members is neuronal-specific (1). ELAVL/Hu proteins are highly conserved RNA-binding proteins (1). Besides three RNA recognition motifs, these proteins also contain nuclear localization signals that enable them to shuttle between nucleus and cytoplasm (2). Upon inhibition of transcription by actinomycin D, ELAVL1/HuR relocates from nucleus to cytoplasm where it binds the AU-rich elements within 3' UTRs to stabilize mRNAs (3, 4). ELAVL1/HuR is suggested to increase translation by binding to mRNAs (5,6). In addition, ELAVL1/HuR interacts with microRNAs (miRNAs) (7).

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

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

Background: The ELAVL (embryonic lethal, abnormal vision and Drosophila-like) family of proteins includes ELAVL1/HuR, ELAVL2/HuB, ELAVL3/HuC and ELAVL4/HuD (1). ELAVL1/HuR is ubiquitously expressed whereas expression of the other three members is neuronal-specific (1). ELAVL/Hu proteins are highly conserved RNA-binding proteins (1). Besides three RNA recognition motifs, these proteins also contain nuclear localization signals that enable them to shuttle between nucleus and cytoplasm (2). Upon inhibition of transcription by actinomycin D, ELAVL1/HuR relocates from nucleus to cytoplasm where it binds the AU-rich elements within 3' UTRs to stabilize mRNAs (3, 4). ELAVL1/HuR is suggested to increase translation by binding to mRNAs (5,6). In addition, ELAVL1/HuR interacts with microRNAs (miRNAs) (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The super elongation complex (SEC) plays a critical role in regulating RNA polymerase II (RNAPII) transcription elongation (1). The SEC is composed of AFF4, AFF1/AF4, MLLT3/AF9, and MLLT1/ENL proteins. The pathogenesis of mixed lineage leukemia is often associated with translocations of the SEC subunits joined to the histone H3 Lys4 methyltransferase mixed lineage leukemia (MLL) gene (1-4). The SEC has been found to contain RNAPII elongation factors eleven-nineteen lysine-rich leukemia (ELL), ELL2, and ELL3, along with the associated factors EAF1 and EAF2, which can increase the catalytic rate of RNAPII transcription in vitro, (1,2,5-7). The SEC positive transcription elongation factor b (P-TEFb) phosphorylates the carboxy-terminal domain within the largest subunit of RNAP II at Ser2 of the heptapeptide repeat. The SEC negative transcription elongation factors, DRB-induced stimulating factor (DSIF) and negative elongation factor (NELF), signal the transition from transcription initiation and pausing to productive transcription elongation (2,8-10). The chromosomal translocation of MLL with the members of the SEC leads to SEC recruitment to MLL regulated genes, such as the highly developmentally regulated Hox genes, implicating the misregulation and overexpression of these genes as underlying contributors to leukemogenesis (1,2,9,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Engulfment and cell motility 1 (ELMO1) is a cell motility and migration protein that interacts with DOCK180 to form an atypical, two-part guanine nucleotide exchange factor (GEF) for the small GTPase Rac (1). The resultant localized Rac activation allows actin nucleation via WAVE family proteins, signaling to integrins, formation of lamellipodia and filopodia, and regulation of processes including phagocytosis and cell migration (2-4). Research studies indicate that DOCK180 and ELMO1 regulate cell migration in lymphocytes (5) and in ovarian cancer cells (6). ELMO1 also promotes Rac1-dependent cell motility through its interaction with the adaptor protein Nck-1 (7), and binds Arhgef16 to promote RhoG/Rac1-dependent engulfment of apoptotic cells by phagocytes (8). Polymorphisms in the corresponding ELMO1 gene may be associated with susceptibility to diabetic neuropathy seen in selected populations of type II diabetic patients (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Elongator is a highly conserved transcription elongation factor complex that was first identified in yeast as part of the hyperphosphorylated RNA polymerase II (RNAPII) holoenzyme (1). The Elongator complex consists of 6 subunits, ELP1-6, and has been shown to have acetyltransferase activity (2). The acetylation targets of Elongator include histone H3, which is linked to the transcription elongation function of the complex, and α-tubulin, which is associated with regulation of migration and maturation of projection neurons (3-6).

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

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

Background: Emerin is a broadly expressed integral protein of the nuclear inner membrane (1). It contains a LEM domain and binds to several nuclear proteins, such as BAF (barrier-to-autointegration factor) and A- and B-type lamins, which are important in nuclear functions (2-5). Emerin may regulate gene expression through binding to other transcriptional regulators (6,7). Emerin binds to β-catenin and inhibits its nuclear accumulation (8). Recent studies demonstrate that emerin is required for HIV-1 infectivity (9). Mutations in the gene encoding emerin (EMD) are a major cause of Emery-Dreifuss muscular dystrophy (EDMD), a disorder characterized by progressive skeletal muscle weakening (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Emerin is a broadly expressed integral protein of the nuclear inner membrane (1). It contains a LEM domain and binds to several nuclear proteins, such as BAF (barrier-to-autointegration factor) and A- and B-type lamins, which are important in nuclear functions (2-5). Emerin may regulate gene expression through binding to other transcriptional regulators (6,7). Emerin binds to β-catenin and inhibits its nuclear accumulation (8). Recent studies demonstrate that emerin is required for HIV-1 infectivity (9). Mutations in the gene encoding emerin (EMD) are a major cause of Emery-Dreifuss muscular dystrophy (EDMD), a disorder characterized by progressive skeletal muscle weakening (10).

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

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

Background: Echinoderm microtubule-associated protein-like 4 (EML4) is a 120 kDa microtubule-associated WD-repeat protein of the echinoderm microtubule-associated protein family (1). The expression of EML4 is necessary for correct intracellular microtubule network formation (2). EML4 protein expression is upregulated during mitosis and downregulated during the remaining cell cycle (1). During mitosis, EML4 is heavily phosphorylated and is associated with the mitotic spindle (2). The amino-terminal segment of EML4 is essential for microtubule association and function.

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Echinoderm microtubule-associated protein-like 4 (EML4) is a 120 kDa microtubule-associated WD-repeat protein of the echinoderm microtubule-associated protein family (1). The expression of EML4 is necessary for correct intracellular microtubule network formation (2). EML4 protein expression is upregulated during mitosis and downregulated during the remaining cell cycle (1). During mitosis, EML4 is heavily phosphorylated and is associated with the mitotic spindle (2). The amino-terminal segment of EML4 is essential for microtubule association and function.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Endophilin proteins are part of a large family of Bin/Amphiphysin/Rvs (BAR) domain proteins that are involved in cell membrane remodeling (1). The endophilins are encoded by five genes, which produce endophilin A 1-3 and B 1-2 (2). Endophilins are involved in many cellular mechanisms, such as synaptic vesicle recycling, receptor trafficking, and membrane remodeling processes (2). Research studies indicate that endophilin 1 (endophilin A1, SH3GL2) can induce different membrane shapes (3) and participate in the morphogenesis of dendritic spines (4). Endophilin 1 is also involved in regulating blood brain barrier permeability via the EGFR-JNK pathway (5).

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

Application Methods: Western Blotting

Background: Enolase is an important glycolytic enzyme involved in the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Mammalian enolase exists as three subunits: enolase-1 (α-enolase), enolase-2 (γ-enolase) and enolase-3 (β-enolase) that can form both homo- and heterodimers. Expression of the enolase isoforms differs in a tissue specific manner (1). Enolase-1 plays a key role in anaerobic metabolism under hypoxic conditions and may act as a cell surface plasminogen receptor during tissue invasion (2,3). Abnormal expression of enolase-1 is associated with tumor progression in some cases of breast and lung cancer (4-7). Alternatively, an enolase-1 splice variant (MBP-1) binds the c-myc promoter p2 and may function as a tumor suppressor. For this reason enolase-1 is considered as a potential therapeutic target in the treatment of some forms of cancer (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Enolase is a glycolytic enzyme that is involved in the conversion of 2-phosphoglycerate to phosphoenolpyruvate (1). Mammalian enolase has three subunits: α, β, and γ, that can form homo and heterodimers. Homodimers of γ enolase are neuronal-specific (2). Research studies have shown elevated levels of neuro-specific enolase-2 in neuroblastoma (2) and small-cell lung cancer (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human

Application Methods: 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human

Application Methods: Immunohistochemistry (Paraffin), 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
Bovine, Human

Application Methods: Immunohistochemistry (Paraffin), 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
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).