References |
Synonyms |
- Postsynaptic Density Protein 95
|
Formulation |
Protein G affinity-purified IgG at a concentration of 1 mg/ml in PBS, pH 7.4, containing 0.09% sodium azide and 50% glycerol |
Stability |
1 year |
Storage |
-20°C |
Shipping |
Wet ice
in continental US; may vary elsewhere
|
Specificity |
Murine PSD95 |
+ |
Rat PSD95 |
+ |
Bovine PSD95 |
+ |
|
Background Reading
Chetkovich, D.M., Bunn, R.C., Kuo, S., et al. Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms. J Neurosci 22(15) 6415-6425 (2002).
Cline, H. Synaptogenesis: A balancing act between excitation and inhibition. Curr Biol 15 R203-R205 (2005).
Cao, J., Viholainen, J.I., Dart, C., et al. The PSD95-nNOS interface: A target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death. J Cell Biol 168(1) 117-126 (2005).
Irie, M., Hata, Y., Takeuchi, M., et al. Binding of neuroligins to PSD-95. Science 277 1511-1515 (1997).
Cai, C., Li, H., Rivera, C., et al. Interaction between SAP97 and PSD-95, two Maguk proteins involved in synaptic trafficking of AMPA receptors. J Biol Chem 281(7) 4267-4273 (2006).
Yao, W., Gainetdinov, R.R., Arbuckle, M.I., et al. Identification of PSD-95 as a regulator of dopamine-mediated synaptic and behavioral plasticity. Neuron 41 625-638 (2004).
Kennedy, M.B. The postsynaptic density at glutamatergic synapses. Trends Neurosci 20(6) 264-268 (1997).
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Size |
Global Purchasing |
25 µg |
|
100 µg |
|
Description
Antigen:
rat recombinant PSD95
·
Clone designation:
6G6
·
Host:
mouse
·
Isotype:
IgG2a
·
Application(s):
WB and ICC
·
Postsynaptic Density protein 95 (PSD95), also known as synapse associated protein 90 kDa, 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 domains localize NMDA receptors and K+ channels to synapses, and the third binds to neuroligins which are neuronal cell adhesion molecules that interact with β-neurexins and form intercellular junctions. PSD95 also binds to neuronal nitric oxide synthase, possibly through interactions between PDZ domains present on both proteins.2 Thus different PDZ domains of PSD95 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
1
Chetkovich, D.M., Bunn, R.C., Kuo, S., et al. Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms. J Neurosci 22(15) 6415-6425 (2002).
2
Cao, J., Viholainen, J.I., Dart, C., et al. The PSD95-nNOS interface: A target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death. J Cell Biol 168(1) 117-126 (2005).
3
Kennedy, M.B. The postsynaptic density at glutamatergic synapses. Trends Neurosci 20(6) 264-268 (1997).
4
Irie, M., Hata, Y., Takeuchi, M., et al. Binding of neuroligins to PSD-95. Science 277 1511-1515 (1997).
5
Cai, C., Li, H., Rivera, C., et al. Interaction between SAP97 and PSD-95, two Maguk proteins involved in synaptic trafficking of AMPA receptors. J Biol Chem 281(7) 4267-4273 (2006).
6
Yao, W., Gainetdinov, R.R., Arbuckle, M.I., et al. Identification of PSD-95 as a regulator of dopamine-mediated synaptic and behavioral plasticity. Neuron 41 625-638 (2004).
7
Cline, H. Synaptogenesis: A balancing act between excitation and inhibition. Curr Biol 15 R203-R205 (2005).
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