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Monoclonal Antibody Immunoprecipitation Gdp Metabolic Process

Also showing Monoclonal Antibody Immunoprecipitation Guanylate Kinase Activity, Monoclonal Antibody Immunoprecipitation Gmp Metabolic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CASK is an adaptor protein with a calcium/calmodulin-dependent protein kinase domain, an SH3 domain, a guanylate kinase homology domain (GUK), and a PDZ domain. CASK links transmembrane proteins to the cytoskeleton and signaling molecules. In particular, CASK binds to neurexin to stabilize pre- and post-synaptic structures (1). While most CASK protein (~80%) is cytoplasmic, a portion of the protein enters the nucleus, where it acts as a transcriptional coactivator (2). Transgenic mice with CASK insertional mutations die within 24 hours of birth (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Postsynaptic Density Protein 93 (PSD93) is a member of the PSD subfamily of the membrane-associated guanylate kinase (PSD-MAGUK) proteins. Structurally, it most closely resembles PSD95, consisting of an N-terminal variable segment followed by three PDZ domains, an SH3 domain, and an inactive guanylate kinase (GK) domain (1,2). PSD93 is expressed in neuronal cells and located at the synapse where it interacts with neuronal receptors and proteins including the NMDA receptor (2-4), K+ channels (5,6), and the AMPA receptor (7) to regulate their membrane localization and neuronal signaling. Research studies have implicated PSD93 in postsynaptic related persistent pain induction, making PSD93 a potential target for treatment of this syndrome (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Synapse-associated protein 102 (SAP102, DLG3) belongs to the membrane-associated guanylate kinase (MAGUK) protein family and is a homolog of the Drosophila disc large (dlg) tumor suppressor protein. SAP102 consists of three PDZ domains, a Src homology 3 (SH3) domain, and a guanylate kinase (GK) domain (1). The SAP102 protein is more highly expressed in nonproliferating cells than in proliferating cells, indicating a role in the negative regulation of cell growth. SAP102 interacts with the carboxy terminus of the adenomatous polyposis coli (APC) tumor suppressor protein. Furthermore, SAP102 associates with PSD95 in the presence of calcium while the SH3 domain of SAP102 binds calmodulin (2,3). All three PDZ domains of SAP102 participate in binding to the NMDA receptor, interacting specifically with the carboxy-terminal domain of the N-methyl-D-aspartate receptor 2B (NR2B). This SAP102-NR2B interaction may facilitate AMPA receptor withdrawal from the postsynaptic membrane by inhibiting the Erk/MAPK pathway (1,4). Neuronal SAP102 is concentrated at dendritic shafts and spines, axons, and synaptic junctions. At excitatory synapses, SAP102 is involved in NMDA receptor clustering and immobilization and links NMDA receptors to the submembraneous cytomatrix (4). SAP102 and the NMDA receptor function together to mediate plasticity, behavior, and signal transduction (1). A nonsyndromic form of X-linked mental retardation is caused by loss-of-function mutations to the SAP102 gene. The SAP102 protein may be involved in autism since MAGUK proteins in the NMDA receptor complex bind directly to the autism susceptibility gene, neuroligin (1,5).