Cell Signaling Technology

Product Pathways - Neuroscience

Phospho-PSD95 (Tyr236/Tyr240) Antibody #3919

Applications Reactivity Sensitivity MW (kDa) Source
W R (H) (M) Endogenous 95 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

Phospho-PSD95 (Tyr236/Tyr240) Antibody detects endogenous levels of PSD95 protein only when phosphorylated at Tyr236 or Tyr240.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr236 and Tyr240 of human PSD95. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from rat brain, either sham operated or subjected to ischemia (15 min) alone or followed by reperfusion (4 hours), using Phospho-PSD95 (Tyr236/Tyr240) Antibody (upper) and PSD95 Antibody #2507 (lower).

Background

Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

Phospho-PSD95 (Tyr236/Tyr240) Antibody is directed against previously unpublished PSD95 tyrosine phosphorylation sites at Tyr236 and Tyr240 that were identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's MS/MS platform for phosphorylation site discovery. Phosphorylation of PSD95 at Tyr236 and Tyr240 was observed in extracts isolated from ischemic rat brain. The sites were independently found in a large-scale identification of tyrosine phosphorylation sites from murine brain (6).

  1. Cao, J. et al. (2005) J. Cell Biol 168, 117-26.
  2. Chetkovich, D.M. et al. (2002) J. Neurosci. 22, 6415-25.
  3. Cai, C. et al. (2006) J. Biol. Chem. 281, 4267-73.
  4. Yao, W.D. et al. (2004) Neuron 41, 625-38.
  5. Cline, H. (2005) Curr. Biol. 15, R203-5.
  6. Ballif, B.A. et al. (2008) J. Proteome Res. 7, 311-8.

Application References

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For Research Use Only. Not For Use In Diagnostic Procedures.

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