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Discs, Large Homolog 4 (Drosophila) (DLG4) antibody

Details for Product No. ABIN361722, Supplier: Log in to see
Antigen
  • 11
  • anon-EST:Posey93
  • anon-WO03040301.258
  • anon-WO03040301.260
  • anon-WO03040301.268
  • CG1725
  • CG1730
  • CPD
  • d. lg.-1
  • Discs-large
  • Dlg
  • dlg
  • DLG
  • dlg-1
  • DLG-A
  • Dlg-A
  • dlg-A
  • Dlg1
  • DLG4
  • DlgA
  • dlgA
  • Dlgh4
  • dlgh4
  • dlgS97
  • Dmel\\CG1725
  • Drodlg
  • l(1)10Bf
  • l(1)bwn
  • l(1)d.lg-1
  • l(1)d.lg.-1
  • l(1)discs large
  • l(1)dlg
  • l(1)dlg-1
  • l(1)dlg1
  • l(1)G0276
  • l(1)G0342
  • l(1)G0456
  • l(1)G19
  • l(1)l.pr.-2
  • l(1)L11
  • l(1)lpr-2
  • LLGL1
  • misb
  • PSD-95
  • PSD95
  • psd95
  • sap-90
  • SAP-90
  • Sap90
  • sap90
  • SAP90
  • SAP90A
  • SAP97
Reactivity
Cow (Bovine), Human, Mouse (Murine), Rat (Rattus)
170
137
127
56
14
14
3
2
2
2
2
1
1
1
1
1
Host
Mouse
132
72
13
1
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
7
7
6
5
5
5
5
4
4
4
4
4
4
4
4
4
4
3
3
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blotting (WB)
195
111
101
77
29
22
19
17
14
14
14
7
6
5
2
1
Supplier
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Immunogen Recombinant rat PSD-95
Clone 7E3
Specificity Detects ~100 kDa. An additional protein of >100 kDa is also detected. Additional cross-reactive bands are detected at ~75 kDa and 50 kDa in rat and mouse samples.
Sensitivity 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.
Purification Protein G Purified
Alternative Name PSD 95 (DLG4 Antibody Abstract)
Background 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 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).
Cellular Localization: Cell Membrane | Cell Junction | Synapse | Postsynaptic Cell Membrane | Postsynaptic Density | Cell Projection | Axon
Gene ID 29495
NCBI Accession NP_062567
UniProt P31016
Application Notes Recommended Dilution: WB (1:1000), IHC (1:1000), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Western Blotting (WB) image for anti-Discs, Large Homolog 4 (Drosophila) (DLG4) antibody (ABIN361722) western rat membrane 1 in 1000 PSD 95.
Background publications Cai, Li, Rivera, Keinänen: "Interaction between SAP97 and PSD-95, two Maguk proteins involved in synaptic trafficking of AMPA receptors." in: The Journal of biological chemistry, Vol. 281, Issue 7, pp. 4267-73, 2006 (PubMed).

Cao, Viholainen, Dart, Warwick, Leyland, Courtney: "The PSD95-nNOS interface: a target for inhibition of excitotoxic p38 stress-activated protein kinase activation and cell death." in: The Journal of cell biology, Vol. 168, Issue 1, pp. 117-26, 2005 (PubMed).

Cline: "Synaptogenesis: a balancing act between excitation and inhibition." in: Current biology : CB, Vol. 15, Issue 6, pp. R203-5, 2005 (PubMed).

Yao, Gainetdinov, Arbuckle, Sotnikova, Cyr, Beaulieu, Torres, Grant, Caron: "Identification of PSD-95 as a regulator of dopamine-mediated synaptic and behavioral plasticity." in: Neuron, Vol. 41, Issue 4, pp. 625-38, 2004 (PubMed).

Chetkovich, Bunn, Kuo, Kawasaki, Kohwi, Bredt: "Postsynaptic targeting of alternative postsynaptic density-95 isoforms by distinct mechanisms." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 22, Issue 15, pp. 6415-25, 2002 (PubMed).

Irie, Hata, Takeuchi, Ichtchenko, Toyoda, Hirao, Takai, Rosahl, Südhof: "Binding of neuroligins to PSD-95." in: Science (New York, N.Y.), Vol. 277, Issue 5331, pp. 1511-5, 1997 (PubMed).

Kennedy: "The postsynaptic density at glutamatergic synapses." in: Trends in neurosciences, Vol. 20, Issue 6, pp. 264-8, 1997 (PubMed).