Anti-PSD-95 (palmitoylated), mAb (rec.) (PF11)

PSD-95 is a member of proteins located at a specialized postsynaptic membrane region, called the postsynaptic density (PSD). PSD-95 is the most abundant scaffold protein specifically enriched in the PSD. It contains three PDZ domains, an SH3 domain and a guanylate kinase (GuK)-like domain. Through its PDZ domains, PSD-95 assembles various synaptic components at the PSD including intracellular signaling molecules (e.g. SynGAP and kalirin-7), ion channels (e.g. stargazin/AMPA receptors [AMPARs] and NMDA receptors) and cell adhesion molecules (e.g. neuroligin). PSD-95 plays a primary role in synaptic development and maturation and is regulated by palmitoylation at its N-terminal cysteine residues leading to its postsynaptic targeting. Palmitoylation of PSD-95 is triggered by DHHC2, a plasma membrane-inserted palmitoylating enzyme. Palmitoylated PSD-95 is almost exclusively localized at excitatory synapses in neurons. Protein 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. [The UniProt Consortium]