Recombinant Rat Disks large homolog 4(Dlg4)

Code CSB-YP006938RA
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Source Yeast
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Code CSB-EP006938RA
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Source E.coli
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Code CSB-EP006938RA-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP006938RA
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Source Baculovirus
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Code CSB-MP006938RA
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names Dlg4
Uniprot No. P31016
Alternative Names Dlg4; Dlgh4; Psd95Disks large homolog 4; Postsynaptic density protein 95; PSD-95; Synapse-associated protein 90; SAP-90; SAP90
Species Rattus norvegicus (Rat)
Expression Region 1-724
Target Protein Sequence MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY ELQVNGTEGE MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII PGGAAAQDGR LRVNDSILFV NEVDVREVTH SAAVEALKEA GSIVRLYVMR RKPPAEKVME IKLIKGPKGL GFSIAGGVGN QHIPGDNSIY VTKIIEGGAA HKDGRLQIGD KILAVNSVGL EDVMHEDAVA ALKNTYDVVY LKVAKPSNAY LSDSYAPPDI TTSYSQHLDN EISHSSYLGT DYPTAMTPTS PRRYSPVAKD LLGEEDIPRE PRRIVIHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDQIL SVNGVDLRNA SHEQAAIALK NAGQTVTIIA QYKPEEYSRF EAKIHDLREQ LMNSSLGSGT ASLRSNPKRG FYIRALFDYD KTKDCGFLSQ ALSFRFGDVL HVIDAGDEEW WQARRVHSDS ETDDIGFIPS KRRVERREWS RLKAKDWGSS SGSQGREDSV LSYETVTQME VHYARPIIIL GPTKDRANDD LLSEFPDKFG SCVPHTTRPK REYEIDGRDY HFVSSREKME KDIQAHKFIE AGQYNSHLYG TSVQSVREVA EQGKHCILDV SANAVRRLQA AHLHPIAIFI RPRSLENVLE INKRITEEQA RKAFDRATKL EQEFTECFSA IVEGDSFEEI YHKVKRVIED LSGPYIWVPA RERL
Protein Length Full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Function
Postsynaptic scaffolding protein that plays a critical role in synaptogenesis and synaptic plasticity by providing a platform for the postsynaptic clustering of crucial synaptic proteins. Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression.
Gene References into Functions
  1. downregulation of spinal neuroligin1 expression may ameliorate postoperative pain through inhibiting neuroligin1/PSD-95 interaction and synaptic targeting of GluA1 subunit. PMID: 29592780
  2. PSD-95 mediates the dendrite arborization-promoting effect of BDNF. PMID: 28698933
  3. Data suggest that phosphorylation of PSD95 (postsynaptic density protein 95) at Ser561 in guanylate kinase domain is mediated by Par1/Pard1 (partitioning-defective 1 kinase), regulates a conformational switch, and is important for bidirectional neuronal plasticity (as found in cultured hippocampal neurons from embryonic rats). PMID: 28790172
  4. Structure of the PSD-95/MAP1A complex reveals a unique target recognition mode of the MAGUK GK domain. PMID: 28701415
  5. These results indicate that reelin/ApoER2/PSD95 signaling is important for neuronal structure maintenance in mature neurons. PMID: 27653801
  6. Study demonstrates the existence, evolutionary relevance, and mechanism of conditionally neutral mutations in PSD95, a member of the PDZ family of protein interaction modules. PMID: 27321669
  7. The PDZ interaction enhanced the protein interactions between PSD-95 and Prickle2, which is another planar cell polarity factor that is localised at the postsynaptic density. PMID: 26257100
  8. Our study revealed that PSD95 might be involved in the mechanism of POCD, which could provide clues for preventing POCD in clinical operations. PMID: 26365118
  9. results demonstrate that MAGUKs are required for anchoring both types of glutamate receptors at the PSD PMID: 26604311
  10. Rph3A interacts with GluN2A and PSD-95 forming a complex that regulates NMDARs stabilization at postsynaptic membranes. PMID: 26679993
  11. PSD-95 phosphorylation in cortical neurons by Src protein facilitates the integration of Pyk2 to the PSD-95 complex. PMID: 24981431
  12. The PSD-95 is important for overactivity of NMDA receptor function due to facilitating NR2B tyrosine phosphorylation dependent on Fyn kinase by regulating interactions of Fyn with NR2B under the pathological conditions of LID. PMID: 25565773
  13. ephrin-B3 specifies the synaptic localization of PSD-95 and likely links the synaptic stability of PSD-95 to changes in neuronal activity PMID: 26479588
  14. results provided the first evidence that SRC-1 mediated endogenous estrogen regulation of hippocampal synaptic plasticity by targeting the expression of synaptic protein PSD-95 PMID: 26223010
  15. CURP program is used to calculate the energy flow within the third PDZ domain of the PSD-95, and the results were used to illustrate the energy exchange network of inter-residue interactions based on atomistic molecular dynamics simulations. PMID: 26147235
  16. CaMKII, Src family kinase & calpain play role in regulating activity-dependent separation of PSD95 from NMDA receptors (NDMAR), GluN2A or GluN2B. PSD95-NMDAR separation is implicated in synaptic remodeling. PMID: 25393018
  17. These findings suggest that PSD95 mediates a vasodilator complex with beta1AR and KV1 channels in cVSMCs PMID: 25966954
  18. This study observed a statistically significant (P < 0.05) decrease in the abundance of each of the three proteins (DISC1, PSD95, and NOS1) in ipsilateral traumatic brain injury tissues. PMID: 25399920
  19. Rats overexpressing neuroserpin also showed a significant decrease in the levels of postsynaptic density protein 95, a major postsynaptic scaffolding protein. PMID: 24608243
  20. the developmental increase in synaptic expression of PSD95 obstructs the synaptic clustering of NR2B-NMDARs, and thereby restricts reactivation of dendritic branching. PMID: 24705401
  21. Capping of the N-terminus of PSD-95 by calmodulin triggers its postsynaptic release. PMID: 24705785
  22. PSD-95 promotes the stabilization of young synaptic contacts. PMID: 24298137
  23. gp120 injures neurons via an increase of NR2B and a decrease of PSD-95 expressions PMID: 24491052
  24. PSD-95 expression was unchanged in the hippocampus. PMID: 23239444
  25. Spatiotemporal changes of PSD95 expression after optic nerve crush (ONC) suggest that the mRNA and protein level of PSD95 expression is down-regulated one day after ONC and is progressively elevated from 2 to 7 days after ONC. PMID: 21927888
  26. These findings provide a molecular basis for the differential association of NMDA receptor subtypes with PSD-95 MAGUK scaffold proteins. PMID: 22375001
  27. PSD-95-interacting myotubularin related protein (MTMR)2 contributes to the maintenance of excitatory synapses by inhibiting excessive endosome formation and destructive endosomal traffic to lysosomes. PMID: 20410104
  28. Neonatal PSD-95 level was very low, but dramatically increased within the first month In the adult hippocampus, OVX decreased PSD-95 expression within the first week, and recovered to adult levels 2 weeks later. PMID: 20842722
  29. Wnt-5a/JNK pathway modulates the postsynaptic region of mammalian synapse directing the clustering and distribution of protein, PSD-95. PMID: 19332546
  30. Postsynaptic density-95 inhibitors administrated 3 hours after stroke onset reduced infarct volumes and improved long-term neurobehavioral functions in a wide therapeutic window. PMID: 18617669
  31. Results suggest that SrcPTKs are involved in PSD-95 phosphorylation. Tyr(523) phosphorylation is responsible for the increased tyrosine phosphorylation of PSD-95 induced by ischaemia in the rat hippocampus. PMID: 18721130
  32. Co-expression of PSD-95 and GLT1b anchors the transporter close to the post-synaptic glutamate receptors, thereby permitting the fine regulation of glutamate concentrations in this microenvironment. PMID: 18248606
  33. The homogenous distribution of PSD-95 and PSD-93 throughout the PSD is consistent with their being part of a backbone that stabilizes their various binding partners within the PSD PMID: 18392731
  34. These results suggest a correlation of post-synaptic density-95 up-regulation with neuronal nitric oxide synthase in reactive Schwann cells of crushed sciatic nerve. PMID: 18095156
  35. the association between PSD-95 and nNOS undergoes substantial alteration after spinal cord injury PMID: 18053028
  36. Synaptic strength can be regulated by phosphorylation-dephosphorylation of ser-295 of PSD-95;synaptic depression requires the dephosphorylation of ser-295. PMID: 17988632
  37. findings clarify the crosstalk between the two signaling modules, PSD-95 and JIP1 and the molecular mechanism underlying MLK3 activation in rat hippocampus after global ischemia PMID: 17348686
  38. These findings indicate that PSD-95 and nNOS might collectively participate in spinal cord development. PMID: 17904695
  39. The postsynaptic complex of scaffolding protein PSD-95 and neuroligin can modulate the release probability of transmitter vesicles at synapse in a retrograde way, resulting in altered presynaptic short-term plasticity. PMID: 17237775
  40. The consensus GK-binding sequence in MAP1a is determined. PSD-95 can use a similar interaction mode to bind diverse protein partners. PSD-95 GK has adopted the conformational flexibility of the ancestral enzyme to bind its varied ligands. PMID: 17220895
  41. PSD-95 may modulate microtubules to regulate neuronal dendritic outgrowth and branching. PMID: 17021172
  42. This study reveals a role of the interactions between 5-HT2A receptors and PDZ proteins in the pathophysiological pathways of inflammatory pain. PMID: 24058620
  43. expression of the excitatory postsynaptic scaffolding protein PSD95 unexpectedly covaried with neuroligin 2 overexpression PMID: 23891900
  44. The expression of PSD-95 in brain was significantly increased following administration of NMDA receptor antagonist, memantine. PMID: 23800465
  45. our current study identified a functional interplay between PSD-95 and synapse-associated protein 102 (SAP102) to regulate synaptic AMPA receptors PMID: 23946397
  46. Findings unravel an unsuspected role for cortactin acetylation in the regulation of PSD95 dendritic clustering, which may work in concert with cortactin's role in spine development. PMID: 23038781
  47. the structural preferences and interdomain dynamics of the MAGUK core (PDZ3-SH3-guanylate kinase) from postsynaptic density-95 PMID: 23395180
  48. PSD-95 molecules colocalized with clustered cell-surface AMPA-type glutamate receptors in cultured rat hippocampal neurons. PMID: 23719161
  49. Vangl2 is a new component of the PSD that forms a complex with PSD-95 in the adult brain. PMID: 23567299
  50. PSD-95 stabilizes AMPA receptors at postsynaptic sites and provides insight into the dynamic interplay between PSD-95 and AMPA receptors in live neurons PMID: 23342049

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Subcellular Location Cell membrane; Lipid-anchor; Cytoplasmic side. Cell junction, synapse, postsynaptic density. Cell junction, synapse. Cytoplasm. Cell projection, axon. Cell projection, dendritic spine. Cell projection, dendrite. Cell junction, synapse, presynapse.
Protein Families MAGUK family
Tissue Specificity Expressed in brain (at protein level). Detected in juxtaparanodal zones in the central nervous system and at nerve terminal plexuses of basket cells in the cerebellum. Expressed in cerebrum. Expressed in hippocampal neurons (at protein level). Isoform 1 a
Database Links

KEGG: rno:29495

STRING: 10116.ENSRNOP00000059045

UniGene: Rn.9765

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