antibody

Anti-PSD-95

MBS502106

0.1 mL

345 USD

polyclonal

rabbit

nonconjugated

Antibody

Anti-PSD-95

PSD-95

disks large homolog 4; Disks large homolog 4; disks large homolog 4; PSD-95; SAP-90; discs large homolog 4; synapse-associated protein 90; postsynaptic density protein 95; synapse-associated protein SAP90; discs, large homolog 4 (Drosophila); Postsynaptic density protein 95; PSD-95; Synapse-associated protein 90

DLG4

Dlg4; Dlg4; Dlgh4; PSD95; Sap90; Dlgh4; Psd95; PSD-95; SAP-90; SAP90

DLG4_RAT

Polyclonal

Rabbit

Rat

724

Affinity Purified (Specific for ~95k PSD-95 protein.)

100 ul in 10 mM HEPES (pH 7.5), 150 mM NaCl, 100 ug per ml BSA and 50% glycerol. Adequate amount of material to conduct 10-mini Western Blots.

Store at -20 degree C; stable for at least one year.

Western Blot (WB)

Quality Control: Western blots performed on each lot. WB: 1:1000

Antigen: Peptide corresponding to amino acid residues from the N-terminal region of rat PSD-95, conjugated to keyhole limpet hemocyanin (KLH). Immunogen Information: Synthetic peptide corresponding to amino acid residues from the N-terminal region conjugated to KLH. Immunogen Species: Rat

Reactivity Assumed Based on 100% Sequence Homology: Bovine, human, mouse, non-human primates and zebra fish. Species Reactivity Note: The antibody has been directly tested for reactivity in Western blots in rat and mouse tissues. It is anticipated that the antibody will also work with bovine, human, non-human primates and zebra fish tissues based on the fact that these species have 100% homology with the amino acid sequence used as antigen. Biological Significance: PSD-95 is a very prominent component of the postsynaptic densities of synapses. It contains three PDZ domains which play key roles in its interactions with other proteins in the synapse. It has been proposed that these PDZ domains organize glutamate receptors and their associated signaling proteins and determine the size and strength of synapses (Kim and Sheng, 2004). Recent work suggests that interaction of the NMDAR with PSD-95 via these PDZ domains can be regulated by phosphorylation (Chung et al., 2004).

Affinity purified rabbit polyclonal antibody

Chung HJ, Huang YH, Lau LF, Huganir RL (2004) Regulation of the NMDA receptor complex and trafficking by activity-dependent phosphorylation of the NR2B subunit PDZ ligand. J Neurosci 24:10248-10259. Kim EJ, Sheng M (2004) PDZ domain proteins of synapses. Nat Rev Neurosci 5:771-781.

9665227

NP_062567.1

NM_019621.1

P31016

95

Activation Of Ca-permeable Kainate Receptor Pathway (936458); Activation Of Kainate Receptors Upon Glutamate Binding Pathway (936455); Activation Of NMDA Receptor Upon Glutamate Binding And Postsynaptic Events Pathway (936445); Axon Guidance Pathway (936266); CREB Phosphorylation Through The Activation Of CaMKII Pathway (936452); CREB Phosphorylation Through The Activation Of Ras Pathway (936448); Cocaine Addiction Pathway (546271); Cocaine Addiction Pathway (546273); Developmental Biology Pathway (936265); Glutamatergic Synapse Pathway (213815)

a molecular scaffolding protein that binds and clusters N-methyl-D-aspartate receptors at neuronal synapses; may be involved in guanine nucleotide-mediated signal transduction pathway [RGD, Feb 2006]

Function: Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Ref.17 Ref.19 Ref.27. Subunit structure: Interacts through its PDZ domains with ANO2 and NETO1. Interacts through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C, GRIN2D, ASIC3, certain splice forms of GRIN1, KCND2, CXADR, SYNGAP1, KCNA1, KCNA2, KCNA3, KCNA4, ERBB4, LRRC4; LRRC4B and SEMA4C. Interacts through its first PDZ domain with GRIK2, KCNA4 and CRIPT. Interacts through its second PDZ domain with the PDZ domain of NOS1 or the C-terminus of CAPON. Interacts through its third PDZ domain with NLGN1 and CRIPT, and probably with NLGN2 and NLGN3. Interacts through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2, DLGAP3, DLGAP4, MAP1A, BEGAIN, SIPA1L1 and KIF13B. Isoform 2 interacts through an L27 domain with HGS/HRS and the first L27 domain of CASK. Interacts with ADR1B, ANKS1B and PRR7. May interact with HTR2A. Interacts with ADAM22, KLHL17 and LGI1. Interacts with FRMPD4 (via C-terminus). Interacts with LRFN1, LRFN2 and LRFN4, but not with LRFN3 nor LRFN5. Interacts (via N-terminus tandem pair of PDZ domains) with GPER1 (via C-terminus tail motif); the interaction is direct and induces the increase of GPER1 protein levels residing at the plasma membrane surface in a estradiol-independent manner. Interacts (via N-terminus tandem pair of PDZ domains) with NOS1 (via N-terminus domain). Interacts with SHANK3. Subcellular location: Cell membrane; Peripheral membrane protein. Cell junction synapse postsynaptic cell membrane postsynaptic density. Cell junction synapse. Note: High levels in postsynaptic density of neurons in the forebrain. Also in presynaptic region of inhibitory synapses formed by cerebellar basket cells on axon hillocks of Purkinje cells. Ref.6 Ref.7 Ref.14. Tissue specificity: Detected in brain (at protein level). Brain. Highest levels of isoform 2 in cerebellum, cortex, hippocampus, and corpus striatum. Ref.14 Ref.16. Domain: The PDZ domain 3 mediates interaction with ADR1B . By similarity.The L27 domain near the N-terminus of isoform 2 is required for HGS/HRS-dependent targeting to postsynaptic density . By similarity. Post-translational modification: Palmitoylation of isoform 1 is required for targeting to postsynaptic density. Ref.12. Sequence similarities: Belongs to the MAGUK family.Contains 1 guanylate kinase-like domain.Contains 3 PDZ (DHR) domains.Contains 1 SH3 domain.

0.1 mL

345 USD