glur2

Pep2-EVKI acetate is a cell-permeable peptide. Pep2-EVKI acetate interferes the interaction between protein interacting with C-kinase (PICK1) and GluR2 AMPA receptor subunits.

TAT-GluR23A Fusion Peptide is a bioactive peptide comprising the GluR23A sequence—residues 869 to 877 of GluR23Y with alanine replacing tyrosine—and an 11 amino acid cell-permeable HIV Trans-Activator of Transcription (TAT) protein transduction domain (PTD). It serves as an inactive control counterpart to the glutamate receptor endocytosis inhibitor GluR23Y, devoid of crucial phosphorylation sites.

GluR23Y, a biologically active peptide, was utilized in an ELISA-based cell-surface assay to assess insulin-stimulated endocytosis of native AMPA receptors in cultured hippocampal neurons. GluR23Y effectively inhibited the insulin-induced decrease in receptor presence. The inhibition of insulin effects was achieved by introducing GluR23Y into neurons through fusion with the membrane transduction domain of HIV-1 TAT.

L-Cysteinesulfinic acid monohydrate is a potent agonist at rat metabotropic glutamate receptors (mGluRs) with pEC50s of 3.92, 4.6, 3.9, 2.7, 4.0, and 3.94 for mGluR1, mGluR5, mGluR2, mGluR4, mGluR6, and mGluR8, respectively [1].

pep2m aceate is a Peptide inhibitor of the interaction between the C-terminus of the GluR2 subunit and N-ethylmaleimide-sensitive fusion protein

Myristoylated TFA Pep2m (Myr-Pep2m TFA) is a cell-permeable peptide that effectively disrupts the interactions between the protein kinase ζ (PKMζ) downstream targets—N-ethylmaleimide-sensitive factor/glutamate receptor subunit 2 (NSF/GluR2). PKMζ, an autonomously active isozyme of protein kinase C (PKC), plays a crucial role in these interactions [1] [2].