PSD95 Antibody
PSD 95 Antibody, Clone 7E3
- SPECIFICATION
- CITATIONS
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- BACKGROUND
Application
| WB, IHC, ICC, AM |
---|---|
Primary Accession | P31016 |
Other Accession | NP_062567.1 |
Host | Mouse |
Isotype | IgG1 |
Reactivity | Human, Mouse, Rat, Bovine |
Clonality | Monoclonal |
Description | Mouse Anti-Rat PSD95 Monoclonal IgG1 |
Target/Specificity | Detects ~100kDa. An additional protein of >100kDa is also detected. Additional cross-reactive bands are detected at ~75kDa and 50kDa in rat and mouse samples. |
Other Names | PSD 95 Antibody, PSD-95 Antibody, DLG4 Antibody, SAP90 Antibody, Synapse-associated protein 90 Antibody, Postsynaptic density protein 95 Antibody, Disks large homolog 4 Antibody |
Clone Names | 7E3 |
Immunogen | Recombinant rat PSD-95 |
Purification | Protein G Purified |
Storage | -20ºC |
Storage Buffer | PBS pH7.4, 50% glycerol, 0.09% sodium azide |
Shipping Temperature | Blue Ice or 4ºC |
Certificate of Analysis | 1 µg/ml was sufficient for detection of PSD-95 on 20 µg rat brain tissue extract by ECL immunoblot analysis using Goat Anti-Mouse IgG: HRP as the secondary. |
Cellular Localization | Cell Membrane | Cell Junction | Synapse | Postsynaptic Cell Membrane | Postsynaptic Density | Cell Projection | Axon |
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Provided below are standard protocols that you may find useful for product applications.
Background
Postsynaptic Density protein 95 (PSD95), also known as Synapse associated protein 90kDa, is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. PSD95 is a scaffolding protein and is involved in the assembly and function of the postsynaptic density complex (1). These family members consist of an N-terminal variable segment followed by three amino-terminal PDZ domains, an upstream SH3 domain and an inactive carboxyl-terminal guanylate kinase (GK) domain. The first and second PDZ domain localize NMDA receptors and K+ channels to synapses, and the third binds to neuroligins which are neuronal cell adhesion molecules that interact with b-neurexins and form intercellular junctions. PSD-95 also binds to neuronal nitric oxide synthase, possibly through interactions between PDZ domains present on both proteins (2). Thus different PDZ domains of PSD-95 might be specialized for distinct functions (3, 4). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (5). The protein is implicated in experience dependent plasticity and plays an indispensable role in learning (6). Mutations in PSD95 are associated with autism (7).
References
1. Chetkovich D.M., Bunn R.C., Kuo S.H., Kawasaki Y., Kohwi M., and Bredt D.S. (2002) J Neurosci. 22(15): 6415-25.
2. Cao J., Viholainen J.I., Dart C., Warwick H.K., Levland M.L. and Courtney M.J. (2005) J Cell Biol. 168(1): 117-26.
3. Kennedy M. (1997) Trends in Neurosci. 6: 264-268.
4. Irie M. et al. (1997) Science 277(5331): 1511-5.
5. Cai C. et al. (2006) J Biol Chem. 281: 4267-73.
6. Yao W.D. et al. (2004) Neuron 41: 625-38.
7. Cline H. (2005) Curr Biol. 15: R203-5.
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