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Monoclonal Antibody Western Blotting Positive Regulation of Vasodilation

$260
100 µl
APPLICATIONS
REACTIVITY
Rat

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

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).

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

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

Background: Calcitonin gene-related peptide (CGRP) is a peptide of 37 amino acids that belongs to the calcitonin (CT) family of peptide hormones. The calcitonin gene (CALCA) encodes a number of tissue-specific peptides through alternative splicing of mRNA transcripts and precursor protein cleavage (1). Both calcitonin and α-CGRP are produced from the CALCA gene, while a second gene (CALCB) encodes the related β-CGRP protein (2). α-CGRP and β-CGRP share similar activities and differ by three or fewer residues depending on the species (3). The CGRP peptide activates a heterotrimeric receptor complex that consists of the seven transmembrane-spanning calcitonin receptor-like receptor, the single transmembrane-spanning RAMP1 protein, and an intracellular receptor component protein (4,5). CGRP is expressed in the central and peripheral nervous system in mammals, where it exhibits several important physiologic roles. Research studies demonstrate that CGRP is a potent vasodilatator (6) and a modulator of acetylcholine receptor function at neuromuscular junctions (7). Additional studies indicate that CGRP peptide is involved in feeding (8) and inflammatory pain (9). CGRP peptide also plays a key role in the physiology of migraine attacks. Specifically, CGRP peptide levels increase during acute migraine attacks, which can be ameliorated through treatment with CGRP antagonists (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: There are four major Adrenergic Receptor (AR) subtypes (α1, α2, β1, β2). Each of the subtypes has been classified by their unique responses to agonists and antagonists. Adrenergic receptors belong to the family of guanine nucleotide-binding, regulatory protein-coupled receptors (GPCR) which transverse the plasma membrane seven times. The transmembrane regions are hydrophobic and are interconnected by hydrophilic loops (1). β2-Adrenergic Receptor (β2AR) is the most studied receptor of the catecholamine system. β2AR stimulation occurs through the catecholamines epinephrine (adrenaline) and norepinephrine (noradrenaline) acting as neuromodulators in the central nervous system and as hormones in the vascular system. β2AR activation results in coupling to heterotrimeric G proteins and activation of the second messengers cAMP and phosphatidylinositol, ultimately leading to changes in cellular physiology. GPCR kinases (GRKs) terminate β2AR signaling through phosphorylation of the GPCR and by recruiting β-arrestin. β-arrestin binding uncouples the receptor from the G protein, thereby terminating G protein–mediated signaling (desensitization), and initiating clathrin-mediated endocytosis (internalization) of β2AR (2). β-adrenergic blocking agents (beta blockers) are drugs that block catecholamines from binding to βAR and are prescribed for cardiac arrhythmias, cardioprotection after myocardial infarction (heart attack), and hypertension (3).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: p300/CBP-associated factor (PCAF), also known as lysine acetyl-transferase 2B (KAT2B), is a transcriptional adaptor protein and histone acetyl-transferase (HAT) that functions as the catalytic subunit of the PCAF transcriptional co-activator complex (1). PCAF is 73% homologous to GCN5L2, another HAT protein found in similar complexes (1,2). Like GCN5L2, PCAF acetylates histone H3 on Lys14 and histone H4 on Lys8, both of which contribute to gene activation by modulating chromatin structure and recruiting additional co-activator proteins that contain acetyl-lysine binding bromo-domains (3). PCAF also acetylates non-histone proteins including transcriptional activators (p53, E2F1, MyoD), general transcription factors (TFIIEβ and TFIIF) and architectural DNA binding proteins (HMGA1 and HMG17) (4-10). Acetylation of these proteins regulates their nuclear localization, protein stability, DNA binding, and co-activator association.

$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
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
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, 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
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).

$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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Connexin 43 (Cx43) is a member of the large family of gap junction proteins. Connexins assemble as a hexamer and are transported to the plasma membrane to create a hemichannel that can associate with hemichannels on nearby cells to create cell-to-cell channels. Clusters of these channels assemble to make gap junctions. Gap junction communication is important in development and regulation of cell growth. Phosphorylation of Cx43 is important in regulating assembly and function of gap junctions (1,2). Ser368 of Cx43 is phosphorylated by protein kinase C (PKC) after activation by phorbol esters, which decreases cell-to-cell communication (3). Src can interact with and phosphorylate Cx43 to alter gap junction communication (4,5).

$269
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$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
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Heme oxygenase (HO) is the rate-limiting enzyme in the catabolism of heme that results in the release of carbon monoxide, iron, and biliverdin (1). The products of this enzymatic reaction play important biological roles in antioxidant, anti-inflammatory and cytoprotective functions (2). Heme oxygenase comprises two isozymes, including the constitutively expressed HO-2 isozyme and the inducible HO-1 isozyme (3). Inducible HO-1 is expressed as an adaptive response to several stimuli, including heme, metals, and hormones (4). The induction of HO-1 has been implicated in numerous disease states, such as transplant rejection, hypertension, atherosclerosis, Alzheimer disease, endotoxic shock, diabetes, inflammation, and neurological disorders (1,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: PAR2 (F2RL1) belongs to the PAR (Protease-activated Receptor) family of G protein-coupled receptors. These membrane receptors are activated through N-terminal cleavage of the receptor by a serine protease such as thrombin, trypsin, or matrix metalloproteinases (1,2). This cleavage exposes the ‘tethered-ligand’ fragment of the receptor, which binds to a second extracellular loop of the receptor and leads to receptor activation. PAR2 is specifically activated by trypsin or trypsin-like proteases. Activated PAR2 stimulates phosphoinositide hydrolysis and calcium mobilization, interacts with β-arrestin, and eventually leads to ERK activation (3). PAR2 expression and activation are mainly associated with inflammatory diseases (3), but may also play a role in cancer development (4,5).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Pig

Application Methods: Immunoprecipitation, Peptide ELISA (DELFIA), 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: 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
Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The Silent Information Regulator (SIR2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of these genes is Saccharomyces cerevisiae SIR2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT1, the mammalian ortholog of Sir2, is a nuclear protein implicated in the regulation of many cellular processes, including apoptosis, cellular senescence, endocrine signaling, glucose homeostasis, aging, and longevity. Targets of SirT1 include acetylated p53 (2,3), p300 (4), Ku70 (5), forkhead (FoxO) transcription factors (5,6), PPARγ (7), and the PPARγ coactivator-1α (PGC-1α) protein (8). Deacetylation of p53 and FoxO transcription factors represses apoptosis and increases cell survival (2,3,5,6). Deacetylation of PPARγ and PGC-1α regulates the gluconeogenic/glycolytic pathways in the liver and fat mobilization in white adipocytes in response to fasting (7,8). SirT1 deacetylase activity is inhibited by nicotinamide and activated by resveratrol. In addition, SirT1 activity may be regulated by phosphorylation, as it is phosphorylated at Ser27 and Ser47 in vivo; however, the function of these phosphorylation sites has not yet been determined (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: C-reactive protein (CRP) is a pentraxin family protein involved in several host defense-related functions as a result of its ability to bind to foreign pathogens and damaged host cells (1). CRP is a cyclic, non-covalent pentameric protein and normal constituent of human sera that is produced primarily by hepatocytes (2). Secretion of CRP is induced by proinflammatory cytokines, including IL-6 and IL-1β, and significantly increases during acute phase responses to tissue injury, infection, or other inflammatory stimuli (3,4). The presence of CRP is often utilized as an inflammation marker, and monitoring CRP levels in plasma is a useful tool in assessing disease progression or treatment effectiveness. CRP is also regarded as a risk assessment factor for the development and progression of cardiovascular disease (5).CRP binds to phosphorylcholine that is present on the surface of damaged tissues and in the bacterial cell wall of certain pathogens (6). Through this calcium-dependent interaction, CRP promotes agglutination and initiates the activation of the complement cascade. This results in enhanced opsonization through CRP interaction with FcγRI and FcγRIIA, which facilitates phagocytosis (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Glutathione peroxidase 1 (GPX1) is a cytosolic selenoprotein which reduces hydrogen peroxide to water (1). GPX1 is the most abundant and ubiquitous among the five GPX isoforms identified so far (2). It is an important component in the anti-oxidative defense in cells and is associated with a variety of disease conditions, such as colon cancer (3), coronary artery disease (4) and insulin resistance (1).