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Monoclonal Antibody Western Blotting Glutamate Binding

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

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

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system. During neurotransmission, glutamate is released from vesicles of the pre-synaptic cell, and glutamate receptors (e.g. NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing post-synaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels. In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion. Five EAATs (EAAT1-5) are characterized: EAAT2 (GLT-1) is primarily expressed in astrocytes but is also expressed in neurons of the retina and during fetal development (1). Homozygous EAAT2 knockout mice have spontaneous, lethal seizures and an increased predisposition to acute cortical injury (2). PKC phosphorylates Ser113 of EAAT2 and coincides with glutamate transport (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: During neurotransmission, glutamate is released from vesicles of the presynaptic cell, and glutamate receptors (e.g., NMDA Receptor, AMPA Receptor) bind glutamate for activation at the opposing postsynaptic cell. Excitatory amino acid transporters (EAATs) regulate and maintain extracellular glutamate concentrations below excitotoxic levels (1,2). In addition, glutamate transporters may limit the duration of synaptic excitation by an electrogenic process in which the transmitter is cotransported with three sodium ions and one proton, followed by countertransport of a potassium ion (1,2). Five EAATs (EAAT1-5) have been identified. EAAT1 and EAAT2 are expressed mainly in glia, while EAAT3, EAAT4, and EAAT5 are considered to be neuronal transporters (2). EAAT3 is found in the perisynaptic areas and cell bodies of glutamatergic and GABAergic neurons (3). Research studies have implicated abnormal EAAT3 expression in the pathophysiology of Schizophrenia (4,5).

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

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

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Glutamate-ammonia ligase (GLUL), also known as glutamine synthetase (GS), catalyzes the de novo synthesis of glutamine from glutamate and ammonia. GLUL is ubiquitously expressed with particularly high expression in the muscle, liver, and brain (1). GLUL expression is elevated in various cancers. Its expression is upregulated by oncogenic c-Myc (2). High expression of GLUL in breast cancer patients is associated with larger tumor size and high level of HER2 expression. It is a predictor of poor survival in patients with glioma and liver cancers (3-6).

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

Application Methods: Western Blotting

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Metabotropic glutamate receptor 2 (mGluR2) is a class C G protein-coupled receptor for the neurotransmitter glutamate in the mammalian brain. Unlike ionotropic receptors, metabotropic receptors do not form an ion channel pore themselves but are indirectly linked to ion channels (1). While mGluR1 and mGluR5 activate phospholipase C, mGluR2, mGluR3, mGluR4, and mGluR6 are coupled to the inhibitory G protein Gα(i/o) and inhibit adenylyl cyclase (AC) activity (1). Research studies have suggested that mGluR2/3 receptors may be potential targets for the treatment of Schizophrenia (2). Furthermore, mGluR2 interacts with the 5HT2A serotonin receptor to form a hetero-complex in the brain. This complex is a potential pharmacological target for hallucinogenic drugs (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: mGluR5, a metabotropic glutamate receptor, is a class C G protein-coupled receptor that signals through the Gaq/11-PLC-inositol 1,4,5 triphosphate pathway (1). mGluR5 is comprised of a large N-terminal extracellular domain, seven transmembrane domains, and a C-terminal intracellular domain. Glutamate binding to mGluR5 leads to an increase in intracellular calcium levels and stimulation of PKC activity (2). In neurons, mGluR5 is found in the post-synapse, in a complex with NMDA receptors, PSD-95, SHANK, and Homer (3). mGluR5 is also expressed in microglia and astrocytes (4). Neuronal mGluR5 has been shown to interact with amyloid beta oligomers, and mGluR5 antagonists exhibit neuroprotective effects (5) placing mGluR5 as a potential therapeutic target for Alzheimer’s disease. In glial cells, mGluR5 appears to play an anti-inflammatory role by negatively regulating the release of inflammatory factors (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Metabotropic glutamate receptor 1 (mGluR1) is a G protein-coupled receptor (GPCR) for the neurotransmitter glutamate in the mammalian brain. Unlike ionotropic receptors, metabotropic receptors do not form an ion channel pore themselves but are indirectly linked to ion channels (1). Both mGluR1 and mGluR5 are coupled to phospholipase C and activate inositol phospholipid metabolism via G protein-mediated mechanisms. Upon phosphatidylinositol activation, the second messenger calcium is released and generates a calcium-activated chloride current. Metabotropic glutamate receptors other than mGluR1 and mGluR5 inhibit adenylate cyclase (1-3). mGluR1 does not share sequence homology with conventional GPCRs (1). mGluR1 forms a homodimer and is linked to synaptic plasticity, as well as long-term potentiation and long-term depression. Furthermore, mGluR1 is a potential therapeutic target for various psychiatric and neurological diseases, including schizophrenia, epilepsy, and Parkinson and Alzheimer diseases (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

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

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

Background: Glutamate dehydrogenase is a mitochondrial enzyme that catalyzes the oxidative deamination of glutamate to α-ketoglutarate through association with the cofactor nicotinamide adenine dinucleotide phosphate (1). Glutamate dehydrogenase is highly expressed in various tissues such as the liver, brain, kidney, heart, pancreas, ovaries, and testis. Two isoforms produced by two distinct genes are found in mammalian tissues. The GLUD1 gene is ubiquitously expressed (2), while the GLUD2 gene is specifically expressed in testicular tissues and astrocytes (3,4). Glutamate dehydrogenase links glutamate to the Krebs cycle, thereby playing a critical role in the regulation of energy homeostasis. Research studies have shown that changes in glutamate dehydrogenase activity in pancreatic β-cells can cause a hyperinsulinism syndrome (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

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

Background: The enzyme glutamate decarboxylase (GAD) is responsible for the synthesis of the essential neurotransmitter gamma-aminobutyric acid (GABA) from L-glutamic acid (1). GAD1 (GAD67) and GAD2 (GAD65) are expressed in nervous and endocrine systems (2) and are thought to be involved in synaptic transmission (3) and insulin secretion (4), respectively. Autoantibodies against GAD2 may serve as markers for type I diabetes (5). Many individuals suffering from an adult onset disorder known as Stiff Person Syndrome (SPS) also express autoantibodies to GAD2 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Formimidoyltransferase-cyclodeaminase (FTCD) catalyzes two key consecutive reactions in the histidine degradation pathway and links histidine catabolism to one-carbon metabolism. It converts tetrahydrofolate (THF) to 5, 10-methenyl-THF (1,2). Loss of FTCD decreases the sensitivity of cancer cells to chemotherapeutic drug methotrexate, an inhibitor of dihydrofolate reductase (DHFR). DHFR reduces dihydrofolate to tetrahydrofolate, an essential cofactor for nucleotide biosynthesis. Lack of FTCD leads to higher levels of tetrahydrofolate in methotrexate-treated cells, therefore reducing the effect of methotrexate. Conversely, greater depletion of tetrahydrofolate by FTCD through enhanced histidine degradation pathway may boost the efficacy of methotrexate (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The x(c)(-) cysteine/glutamate antiporter consists of a light chain subunit (xCT/SLC7A11) that confers substrate specificity and a glycosylated heavy chain subunit (4F2hc/SLC3A2) located on the cell surface (1,2). The heterodimeric amino acid transport system x(c)(-) provides selective import of cysteine into cells in exchange for glutamate and regulating intracellular glutathione (GSH) levels, which is essential for cellular protection from oxidative stress (3). Research studies have shown that xCT expression increases in various tumors, including gliomas, and have implicated xCT in GSH-mediated anticancer drug resistance (4,5). Researchers have found that xCT provides neuroprotection by enhancing glutathione export from non-neuronal cells (6). Moreover, investigators identified xCT as the fusion-entry receptor for Kaposi's sarcoma-associated herpesvirus (7).