4 μg(R: reducing conditions)
Product Details
Product Details
Product Specification
Species | Mouse |
Synonyms | Disks large homolog 4, Postsynaptic density protein 95(PSD-95), Synapse-associated protein 90 (SAP-90; SAP90), Dlg4, Dlgh4, Psd95 |
Accession | Q62108 |
Amino Acid Sequence | Protein sequence (Q62108, Glu65-Lys299, with C-His tag) EITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKIIEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAK |
Expression System | E.coli |
Molecular Weight | Predicted MW: 26.8 kDa Observed MW: 30 kDa |
Purity | >95% by SDS-PAGE |
Endotoxin | <0.1EU/μg |
Conjugation | Unconjugated |
Tag | with C-His tag |
Physical Appearance | Lyophilized Powder |
Storage Buffer | Lyophilized from a 0.2 μm filtered solution of 0.2M PBS, pH7.4. |
Reconstitution | Reconstitute no more than 1 mg/mL according to the size in deionized water after rapid centrifugation. |
Stability & Storage | 12 months from date of receipt, -20 to -70 °C as supplied. |
Background
PSD-95 (postsynaptic density protein 95) also known as SAP-90 (synapse-associated protein 90). PSD-95 is a member of the membrane-associated guanylate kinase (MAGUK) family. With PSD-93 it is recruited into the same 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. Like all MAGUK-family proteins, its basic structure includes three PDZ domains, an SH3 domain, and a guanylate kinase-like domain (GK) connected by disordered linker regions. It is almost exclusively located in the post synaptic density of neurons, and is involved in anchoring synaptic proteins. Its direct and indirect binding partners include neuroligin, NMDA receptors, AMPA receptors, and potassium channels. It plays an important role in synaptic plasticity and the stabilization of synaptic changes during long-term potentiation.
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