Recombinant Rat Disks Large Homolog 4 (DLG4) Protein (His&Myc)

Name: Recombinant Rat Disks Large Homolog 4 (DLG4) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06446P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Rat Disks Large Homolog 4 (DLG4) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P31016
Target Symbol	DLG4
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDAGDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL
Expression Range	1-724aa
Protein Length	Full Length
Mol. Weight	87.9 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
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
Database References	KEGG: rno:29495 STRING: 10116.ENSRNOP00000059045 UniGene: PMID: 29592780 PSD-95 mediates the dendrite arborization-promoting effect of BDNF. PMID: 28698933 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 Structure of the PSD-95/MAP1A complex reveals a unique target recognition mode of the MAGUK GK domain. PMID: 28701415 These results indicate that reelin/ApoER2/PSD95 signaling is important for neuronal structure maintenance in mature neurons. PMID: 27653801 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 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 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 results demonstrate that MAGUKs are required for anchoring both types of glutamate receptors at the PSD PMID: 26604311 Rph3A interacts with GluN2A and PSD-95 forming a complex that regulates NMDARs stabilization at postsynaptic membranes. PMID: 26679993 PSD-95 phosphorylation in cortical neurons by Src protein facilitates the integration of Pyk2 to the PSD-95 complex. PMID: 24981431 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 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 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 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 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 These findings suggest that PSD95 mediates a vasodilator complex with beta1AR and KV1 channels in cVSMCs PMID: 25966954 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 Rats overexpressing neuroserpin also showed a significant decrease in the levels of postsynaptic density protein 95, a major postsynaptic scaffolding protein. PMID: 24608243 the developmental increase in synaptic expression of PSD95 obstructs the synaptic clustering of NR2B-NMDARs, and thereby restricts reactivation of dendritic branching. PMID: 24705401 Capping of the N-terminus of PSD-95 by calmodulin triggers its postsynaptic release. PMID: 24705785 PSD-95 promotes the stabilization of young synaptic contacts. PMID: 24298137 gp120 injures neurons via an increase of NR2B and a decrease of PSD-95 expressions PMID: 24491052 PSD-95 expression was unchanged in the hippocampus. PMID: 23239444 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 These findings provide a molecular basis for the differential association of NMDA receptor subtypes with PSD-95 MAGUK scaffold proteins. PMID: 22375001 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 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 Wnt-5a/JNK pathway modulates the postsynaptic region of mammalian synapse directing the clustering and distribution of protein, PSD-95. PMID: 19332546 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 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 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 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 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 the association between PSD-95 and nNOS undergoes substantial alteration after spinal cord injury PMID: 18053028 Synaptic strength can be regulated by phosphorylation-dephosphorylation of ser-295 of PSD-95;synaptic depression requires the dephosphorylation of ser-295. PMID: 17988632 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 These findings indicate that PSD-95 and nNOS might collectively participate in spinal cord development. PMID: 17904695 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 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 PSD-95 may modulate microtubules to regulate neuronal dendritic outgrowth and branching. PMID: 17021172 This study reveals a role of the interactions between 5-HT2A receptors and PDZ proteins in the pathophysiological pathways of inflammatory pain. PMID: 24058620 expression of the excitatory postsynaptic scaffolding protein PSD95 unexpectedly covaried with neuroligin 2 overexpression PMID: 23891900 The expression of PSD-95 in brain was significantly increased following administration of NMDA receptor antagonist, memantine. PMID: 23800465 our current study identified a functional interplay between PSD-95 and synapse-associated protein 102 (SAP102) to regulate synaptic AMPA receptors PMID: 23946397 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 the structural preferences and interdomain dynamics of the MAGUK core (PDZ3-SH3-guanylate kinase) from postsynaptic density-95 PMID: 23395180 PSD-95 molecules colocalized with clustered cell-surface AMPA-type glutamate receptors in cultured rat hippocampal neurons. PMID: 23719161 Vangl2 is a new component of the PSD that forms a complex with PSD-95 in the adult brain. PMID: 23567299 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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