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Polyclonal Antibody Respiratory Gaseous Exchange

Also showing Polyclonal Antibody Western Blotting Respiratory Gaseous Exchange

$303
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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), 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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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, Mink, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The common beta-chain (beta-c) of the granulocyte macrophage colony-stimulating factor (GM-CSF), interleukin-3 (IL-3) and IL-5 receptors is the major signaling subunit of these receptors, coupling ligand binding to multiple biological activities (1-3). Tyrosine phosphorylation of cytokine receptor common beta-chain is one of the first events in GM-CSF, IL-3 and IL-5 receptor activation and in signaling initiation (4). Serine phosphorylation within the 14-3-3 binding sequence of the common beta-chain is also involved in GM-CSF, IL-3 and IL-5 receptor-specific functions (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MAFB belongs to the musculoaponeurotic fibrosarcoma (MAF) family of basic leucine-zipper transcription factors (1). In mouse embryo, MAFB expression is first detected at E10.5 (2, 3). Early in development, MAFB drives differentiation of both glucagon-producing α-cells and insulin-producing β-cells in the pancreas, but later plays a more decisive role in the maturation and maintenance of functional α-cells (4, 5). Consistent with MAFB playing a critical role in mature α-cells, MAFB is enriched in α-cells within 2 weeks of birth in the pancreas (6). Glucagon and insulin secretion is tightly regulated, and imbalances in these hormones contribute to metabolic conditions. Therefore, understanding the role of MAFB in α-cell development, maintenance, and physiological function may contribute to developing deeper insights into how these cells contribute to metabolic diseases like diabetes. MAFB also regulates monocyte differentiation, indicating MAFB functions beyond the pancreas (7).