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

AdipoGen Life Sciences

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

10

Recognizes human, mouse and rat palmitoylated PSD-95.

ImmunoCytoChemistry, ImmunoHistoChemistry

Research Use Only

Monoclonal

PF11

0.5 mg/ml

>95%

Human

IgG2

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. Recognizes human, mouse and rat palmitoylated PSD-95. Isotype: Human IgG2. Clone: PF11. Applications: ICC, IHC. Liquid. In PBS containing 10% glycerol. 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, Rat

2°C to 8°C,-20°C

12352203