Anti-PSD-95 (PSD95)

0.5mg/ml if reconstituted with 0.2ml sterile DI water. DLG4 (Discs large homolog 4), also known as Post-synaptic density protein 95 (PSD-95) or SAP-90, is a protein that in humans is encoded by the DLG4 gene. It is a member of the membrane-associated guanylate kinase (MAGUK) family. DLG4 can heteromultimerize with another MAGUK protein, DLG2, and is recruited into NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. Overexpression of DLG4 in hippocampal neurons could drive maturation of glutamatergic synapses. DLG4 can orchestrate synaptic development and it has a role in synapse stabilization and plasticity. Ubiquitination of DLG4 through an MDM2-mediated pathway can regulate AMPA receptor surface expression during synaptic plasticity. Protein function: Postsynaptic scaffolding protein that plays a critical role in synaptogenesis and synaptic plasticity by providing a platform for the postsynaptic clustering of crucial synaptic proteins. 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. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression. Under basal conditions, cooperates with FYN to stabilize palmitoyltransferase ZDHHC5 at the synaptic membrane through FYN-mediated phosphorylation of ZDHHC5 and its subsequent inhibition of association with endocytic proteins (PubMed:26334723). [The UniProt Consortium]