anti-PSD-95, Rabbit Monoclonal (RM288)

RevMAb Biosciences

anti-PSD-95, Rabbit Monoclonal (RM288)

5

Western Blot, ImmunoHistoChemistry

Research Use Only

Monoclonal

RM288

DLG4

discs large MAGUK scaffold protein 4

discs large homolog 4; disks large homolog 4; MRD62; post-synaptic density protein 95; PSD95; SAP90; SAP-90; synapse-associated protein 90; Tax interaction protein 15

Rabbit

IgG

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. - Recombinant Antibody. This antibody reacts to human and mouse PSD95. It may also react to rat PSD95, as predicted by immunogen homology. Applications: WB, IHC. Source: Rabbit. Liquid. 50% Glycerol/PBS with 1% BSA and 0.09% sodium azide. 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.

Human, Mouse

-20°C

12352203