Aktivieren Sie Javascript in Ihrem Browser, um unsere Webseite optimal zu nutzen.

anti-Discs, Large Homolog 4 (Drosophila) (DLG4) Antikörper

Bezeichnung:: anti-Discs, Large Homolog 4 (Drosophila) Antikörper (DLG4)

Auf www.antikoerper-online.de finden Sie aktuell 336 Discs, Large Homolog 4 (Drosophila) (DLG4) Antikörper von 31 unterschiedlichen Herstellern. Zusätzlich bieten wir Ihnen Discs, Large Homolog 4 (Drosophila) Kits (17) und Discs, Large Homolog 4 (Drosophila) Proteine (10) und viele weitere Produktgruppen zu diesem Protein an. Insgesamt sind aktuell 369 Discs, Large Homolog 4 (Drosophila) Produkte verfügbar.

Synonyme:: 11, anon-EST:Posey93, anon-WO03040301.258, anon-WO03040301.260, anon-WO03040301.268, CG1725, CG1730, CPD, d. lg.-1, Discs-large, dlg, dlg-1, dlg-A, Dlg1, DLG4, dlgA, 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, SAP-90, Sap90, SAP90A, SAP97

Alle Antikörper anzeigen	Gen	GeneID	UniProt
	DLG4	13385	Q62108
	DLG4	29495	P31016
	DLG4	1742	P78352
Alle Spezies anzeigen Weitere Synonyme anzeigen

Meistgesuchte Reaktivitäten zu anti-Discs, Large Homolog 4 (Drosophila) (DLG4) Antikörper

Wählen Sie die Spezies und Applikation aus

anti-Mouse (Murine) Antikörper:

anti-Rat (Rattus) Antikörper:

anti-Human Antikörper:

Alle verfügbaren anti-Discs, Large Homolog 4 (Drosophila) Antikörper

Sie gelangen zu unserer vorgefilterten Suche.

Verknüpfte Pathways mit anti-Discs, Large Homolog 4 (Drosophila) Antikörper

Regulation of long-term Neuronal Synaptic Plasticity

Weitere Produktkategorien zu Discs, Large Homolog 4 (Drosophila) Antikörper

Am meisten referenzierte anti-Discs, Large Homolog 4 (Drosophila) Antikörper

Mammalian Monoclonal DLG4 Primary Antibody für ISt, IHC - ABIN1304919 : Higuchi, Macke, Lee, Miller, Xu, Ikeda, Ikeda: Genetic basis of age-dependent synaptic abnormalities in the retina. in Mammalian genome : official journal of the International Mammalian Genome Society 2015 (PubMed)
Show all 336 Pubmed References
Human Monoclonal DLG4 Primary Antibody für BP, ChIP - ABIN4348100 : Fogel, Akins, Krupp, Stagi, Stein, Biederer: SynCAMs organize synapses through heterophilic adhesion. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2007 (PubMed)
Show all 15 Pubmed References
Human Polyclonal DLG4 Primary Antibody für IP, WB - ABIN1742271 : Li, Hu, Höfer, Wong, Cooper, Birnbaum, Hammer, Hofmann: DHHC5 interacts with PDZ domain 3 of post-synaptic density-95 (PSD-95) protein and plays a role in learning and memory. in The Journal of biological chemistry 2010 (PubMed)
Show all 10 Pubmed References
Human Polyclonal DLG4 Primary Antibody für IF (p), IHC (p) - ABIN725930 : Zhao, Li, Wei, Savage, Zhou, Ma: Ketamine administered to pregnant rats in the second trimester causes long-lasting behavioral disorders in offspring. in Neurobiology of disease 2014 (PubMed)
Show all 6 Pubmed References
Mammalian Monoclonal DLG4 Primary Antibody für ISt, IHC - ABIN1304920 : Gonzalez-Lozano, Klemmer, Gebuis, Hassan, van Nierop, van Kesteren, Smit, Li: Dynamics of the mouse brain cortical synaptic proteome during postnatal brain development. in Scientific reports 2016 (PubMed)
Show all 3 Pubmed References
Cow (Bovine) Polyclonal DLG4 Primary Antibody für WB - ABIN550147 : Kim, Sheng: PDZ domain proteins of synapses. in Nature reviews. Neuroscience 2004 (PubMed)
Show all 2 Pubmed References
Human Polyclonal DLG4 Primary Antibody für WB - ABIN6712999 : Xie, Wang, Lu, Pan, Chen, Liao: UCH-L1 inhibition involved in CREB dephosphorylation in hippocampal slices. in Journal of molecular neuroscience : MN 2014 (PubMed)
Human Monoclonal DLG4 Primary Antibody für IF, IHC - ABIN6675311 : Tan, Yao, Hu, Lv, Wan, Zhang, Zhu: Alleviating neuropathic pain mechanical allodynia by increasing Cdh1 in the anterior cingulate cortex. in Molecular pain 2016 (PubMed)
Human Polyclonal DLG4 Primary Antibody für IHC, IP - ABIN6679262 : Liu, Feng, Chen, Luo, Yan, Chen, Lin, Ding, Wen: Dcf1 Triggers Dendritic Spine Formation and Facilitates Memory Acquisition. in Molecular neurobiology 2018 (PubMed)

Weitere Antikörper gegen Discs, Large Homolog 4 (Drosophila) Interaktionspartner

Fruit Fly (Drosophila melanogaster) Discs, Large Homolog 4 (Drosophila) (DLG4) Interaktionspartner

findings reveal that Scrib's PDZ1 domain functions in the interaction with Gukh and that the Scrib-Gukh interaction has a key role in epithelial tissue development in Drosophila
The authors find that the tumor suppressor Discs large (Dlg) links the Par complex component atypical Protein Kinase C (aPKC) to the essential spindle orientation factor GukHolder (GukH).
The structure of dlg1 reveals that the core of the dimer is formed by a distinctive six-helix assembly, involving all three conserved helices from each subunit (monomer). The homodimer interface is extended by the C-terminal tail of the L27 domain of Dlg1, which forms a two-stranded antiparallel beta-sheet. The structure reconciles and provides a structural context for a large body of available mutational data.
Strikingly the absence of any of DLG proteins at the presynaptic terminal disrupts the clustering and localization of the calcium channel DmCa1A subunit (Cacophony), decreases the action potential-evoked release probability and alters short-term plasticity.
Exon junction complex (EJC) activity is indispensable for Wg signaling by maintaining an appropriate level of Dsh protein for Wg ligand reception in Drosophila. Genetic and biochemical experiments demonstrate that Dlg1 protein acts independently from its role in cell polarity to protect Dsh protein from lysosomal degradation.
Banderuola (Bnd) is a novel regulator of asymmetric cell division (ACD). The data place Bnd at the top of the hierarchy of the factors involved in ACD, suggesting that its main function is mediating localization and function of Dlg tumor suppressor.
The inactivation of cellular cortex polarization is the most likely target of dlg inactivation in mitosis.
Loss of scrib, dlg and lgl had no effect on gonad formation, but Dlg and Scrib in the gonadal mesoderm acted critically in the somatic wrapping of the pole cells and the internal structure of the Drosophila embryonic gonads.
Gliotactin and Discs large are co-regulated to maintain epithelial integrity.
Hts regulates Dlg targeting to the neuromuscular junction in muscle and the lateral membrane of epithelial cells.
Electron microscopy reveals that during metamorphosis the subsynaptic reticulum vacuolizes in the early stages of synapse dismantling, concomitant with diffuse localization of Dlg.
DlgS97-Metro-DLin-7-type complexes control the proper organization of a synaptic junction; findings accentuate the importance of perisynaptic scaffold complexes for synaptic stabilization and organization
Study provide evidence that scrib and dlg function differentially in anterior and posterior patterning of the follicular epithelium at oogenesis. Further genetic analysis indicates that scrib and dlg act in a common pathway to regulate PFC fate induction.
integrins act through CaMKII activation to control the localization of dlg in the development of NMJ synaptic morphology
conclude that Dlg/Scrib/Lgl are important in regulating cortical polarity, cell size asymmetry and mitotic spindle asymmetry in Drosophila neuroblasts
Isoforms of Dlg are fundamental for neuronal development in Drosophila
role in development of cell boundaries for cell nuclei in Drosophila embryos in conjunction with Strabismus protein
recruitment of DLin-7 to MAGUK-based protein complexes is defined by cell-type specific mechanisms; DLin-7 acts downstream of Sdt in epithelia and downstream of Dlg at synapses
DLG controls glutamate receptor subunit (GluR) composition by selectively stabilizing GluRIIB subunit-containing receptors at the synapse.
Novel spatiotemporal patterns of epithelial tumor invasion in Drosophila disc large egg chambers were studied.

Zebrafish Discs, Large Homolog 4 (Drosophila) (DLG4) Interaktionspartner

Presenilin-1 targeted morpholino induces cognitive deficits, increased brain Abeta1-42 and decreased synaptic marker PSD-95

Mouse (Murine) Discs, Large Homolog 4 (Drosophila) (DLG4) Interaktionspartner

UV exposure to the skin decreased doublecortin-positive immature neurons and synaptic proteins, including N-methyl-D-aspartate receptor 2 A and postsynaptic density protein-95, in the hippocampus. Moreover, we observed that UV irradiation to the skin down-regulated brain-derived neurotrophic factor expression and ERK signaling in the hippocampus, which are known to modulate neurogenesis and synaptic plasticity.
The present study aims to show PSD-95 distribution in 3 dimensions.
Study found robust hypersocial behavior in the dyadic interaction test in both PSD95(+/-) males and females. Additionally, male PSD95(+/-) mice exhibited higher levels of aggression and territoriality, while female PSD95(+/-) mice showed increased vocalization upon exposure to an anesthetized female mouse. Both male and female PSD95(+/-) mice revealed mild hypoactivity in the open field but no obvious motor deficit.
PSD95 was essential for Arc assembly into 1.5-MDa complexes and activity-dependent recruitment to excitatory synapses.
Results show the binding of PSD95 to GluN subunit 2A is modulated by CIN.
these data identify PSD95 nanoclusters as a basic structural unit, or building block, of excitatory synapses and their number characterizes synapse size and structural diversity
This study demonstrated that in Chronic social defeat stress leads to changes PSD-95 in hippocampus of young mice.
The authors present evidence that synGAP-alpha1 regulates the composition of the postsynaptic density by restricting binding to the PDZ domains of PSD-95.
In Fmr1 KO neurons, Mdm2 is hyperphosphorylated, nuclear localized basally, and unaffected by MEF2 activation, which our data suggest due to an enhanced interaction with Eukaryotic Elongation Factor 1alpha (EF1alpha), whose protein levels are elevated in Fmr1 KO. Expression of a dephosphomimetic of Mdm2 rescues PSD-95 ubiquitination, degradation and synapse elimination in Fmr1 KO neurons.
tested the effect of five targeted mouse mutations on the assembly of known PSD95 interactors, Kir2.3, Arc, IQsec2/BRAG1 and Adam22
Therefore, our study suggests that CREB and PSD95 are novel substrates of PERK, so inhibition of PERK phosphorylation using GSK2656157 would be beneficial against memory impairment after TBI.
PSD95 and SYP may originate from the different sites, but they are closely related to the formation and maturation of synapse.
Expression levels of brain derived neurotrophic factor, postsynaptic density 95, and p-cyclic-AMP response element binding protein levels were significantly elevated in the testosterone (T) group, but flutamide reduced the T-induced effects in these biomarkers to control levels.
The results suggest that the neurological mechanisms of chronic stress on cognition might be associated with a decrease in hippocampal SYN and PSD95 expression, which is critical for structural synaptic plasticity.
critical roles of PSD-95 in regulating synaptic kainate receptors.
Phenylketonuric mice given a specific nutrient combination showed a significant reduction in PSD-95 expression in the hippocampus, specifically in the granular cell layer of the dentate gyrus, with a similar trend seen in the cornus ammonis 1 (CA1) and cornus ammonis 3 (CA3) pyramidal cell layer.
Lambda-cyhalothrin (LCT) could increase the PSD95 protein level via the ERalpha-dependent Akt pathway, and LCT might disrupt the up-regulation effect of estradiol on PSD95 protein expression via this signaling pathway.
Data indicate a contribution of D2 dopamine receptors to the effects of repetitive transcranial magnetic stimulation (rTMS) on postsynaptic density protein-95 (PSD-95) and cyclin-dependent kinase 5 (CDK5) levels.
Data show that in adult PSD-95 knockout mice, ocular dominance plasticity in visual cortex (V1) was preserved after a stroke lesion in somatosensory cortex (S1).
adult mice lacking interleukin-1 receptor 1 (IL-1R1) exhibit increased expression of both the excitatory scaffolding protein postsynaptic density-95 (PSD-95) and inhibitory scaffolding proteingephyrin, respectively, in the hippocampus.

Human Discs, Large Homolog 4 (Drosophila) (DLG4) Interaktionspartner

Crystallographic structures of the following have been solved: a truncated form of the third PDZ domain of the neuronal postsynaptic density protein 95 from which alpha3 has been removed, D332P and D332G variants of the protein, and a new crystal form of this domain showing the binding of Asp332 to the carboxylate-binding site of a symmetry-related molecule.
Here we report an evaluation of the effect of the truncation of this additional helix on the folding and unfolding kinetics of PSD-95 (PDZ3). Fluorescent variants of full length and truncated PDZ3 were produced and stopped-flow fluorescence measurements were made under different experimental conditions (pH, ionic strength and temperature) to investigate the folding kinetics of the respective variant.
DNA methylation of DLG4 and of human hippocampus and prefrontal cortex in major depression is unchanged in comparison to healthy individuals.
results suggest that rare missense mutations in the candidate PSD genes may increase susceptibility to SZ and/or ASD. These findings may strengthen the theory that rare, non-synonymous variants confer substantial genetic risks for these disorders
in postsynaptic densities, PSD95 palmitoylation, conformation, and its interactions are dynamic when associated with AMPARs and more stable when associated with NMDARs
a dual role for PSD-95 in stabilizing synaptic NMDARs by binding directly to GluN2B but also by promoting synaptic exclusion and degradation of the negative regulator STEP61.
the authors integrate molecular and imaging data from animal models and preterm infants, and find that microglial expression of DLG4 plays a role.
Phosphorylation at Y397 induced a significant increase in affinity for stargazing. The strategy presented here to generate site-specifically phosphorylated PDZ domains provides a detailed understanding of the role of phosphorylation in the regulation of PSD95 interactions.
This study demonstrated that a significant decrease in the protein level of PSD-95 in major depression disorder.
These results indicate that PKC promotes synaptogenesis by activating PSD-95 phosphorylation directly through JNK1 and calcium/calmodulin-dependent kinase II and also by inducing expression of PSD-95 and synaptophysin.
The differences in cortical NMDAR expression and post-synaptic density protein 95 are present in psychiatric disorders and suicide completion and may contribute to different responses to ketamine.
Mutation C>T at the rs13331 in the PSD95 gene is strikingly associated with an increased risk of autism spectrum disorders.
Data demonstrate a role for SNAP-25 in controlling PSD-95 clustering and open the possibility that genetic reductions of the protein levels may contribute to the pathology through an effect on postsynaptic function and plasticity.
Data indicate the very high affinities of the trimeric ligands to postsynaptic density protein 95 (PSD-95) PDZ domains.
In this review, we focus on palmitoylation of PSD-95, which is a major postsynaptic scaffolding protein and makes discrete postsynaptic nanodomains in a palmitoylation-dependent manner and discuss a determinant role of local palmitoylation cycles
An association was found between reduced PSD95 in the prefrontal cortex and cognitive impairment in patients with either dementia with Lewy bodies or Parkinson's disease dementia.
Docosahexaenoic acid-containing phosphatidylcholines and PSD-95 decrease after loss of synaptophysin and before neuronal loss in patients with Alzheimer's disease.
The postsynaptic membrane protein PSD95 was increased in schizophrenia in CA3 tissue, but not in CA1 tissue.
The crystal structures of the Dlg4 GK domain in complex with two phosphor-Lgl2 peptides reveal the molecular mechanism underlying the specific and phosphorylation-dependent Dlg/Lgl complex formation.
PSD-95 mRNA G-rich region folds into alternate G quadruplex conformations that coexist in equilibrium and miR-125a forms a stable complex with PSD-95 mRNA.

Discs, Large Homolog 4 (Drosophila) (DLG4) Antigen-Profil

Beschreibung des Gens

This gene encodes a member of the membrane-associated guanylate kinase (MAGUK) family. It heteromultimerizes with another MAGUK protein, DLG2, and is recruited into NMDA receptor and potassium channel clusters. These two MAGUK proteins may interact at postsynaptic sites to form a multimeric scaffold for the clustering of receptors, ion channels, and associated signaling proteins. Multiple transcript variants encoding different isoforms have been found for this gene.

Alternative names and synonyms associated with Discs, Large Homolog 4 (Drosophila) (DLG4)

discs large 1 (dlg1) Antikörper
discs, large homolog 4 (dlg4) Antikörper
discs large MAGUK scaffold protein 4 (DLG4) Antikörper
discs, large homolog 4b (Drosophila) (dlg4b) Antikörper
discs, large homolog 4 (Drosophila) (Dlg4) Antikörper
discs large MAGUK scaffold protein 4 (Dlg4) Antikörper

11 Antikörper
anon-EST:Posey93 Antikörper
anon-WO03040301.258 Antikörper
anon-WO03040301.260 Antikörper
anon-WO03040301.268 Antikörper
CG1725 Antikörper
CG1730 Antikörper
CPD Antikörper
d. lg.-1 Antikörper
Discs-large Antikörper
dlg Antikörper
dlg-1 Antikörper
dlg-A Antikörper
Dlg1 Antikörper
DLG4 Antikörper
dlgA Antikörper
Dlgh4 Antikörper
dlgS97 Antikörper
Dmel\\CG1725 Antikörper
Drodlg Antikörper
l(1)10Bf Antikörper
l(1)bwn Antikörper
l(1)d.lg-1 Antikörper
l(1)d.lg.-1 Antikörper
l(1)discs large Antikörper
l(1)dlg Antikörper
l(1)dlg-1 Antikörper
l(1)dlg1 Antikörper
l(1)G0276 Antikörper
l(1)G0342 Antikörper
l(1)G0456 Antikörper
l(1)G19 Antikörper
l(1)l.pr.-2 Antikörper
l(1)L11 Antikörper
l(1)lpr-2 Antikörper
LLGL1 Antikörper
misb Antikörper
PSD-95 Antikörper
psd95 Antikörper
SAP-90 Antikörper
Sap90 Antikörper
SAP90A Antikörper
SAP97 Antikörper

Bezeichner auf Proteinebene für DLG4

, , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , CG1725-PA CG1725-PB CG1725-PC CG1725-PD CG1725-PE CG1725-PF CG1725-PG CG1725-PH CG1725-PI CG1725-PJ CG1725-PK CG1725-PL CG1725-PM CG1725-PN CG1725-PO CG1725-PP CG1725-PQ CG1725-PR CG1725-PS CG1725-PT CG1725-PU Disc-large Discs-large disc large discs large discslarge disk large dlg1-PA dlg1-PB dlg1-PC dlg1-PD dlg1-PE dlg1-PF dlg1-PG dlg1-PH dlg1-PI dlg1-PJ dlg1-PK dlg1-PL dlg1-PM dlg1-PN dlg1-PO dlg1-PP dlg1-PQ dlg1-PR dlg1-PS dlg1-PT dlg1-PU lethal(1)benign wing imaginal disc neoplasm lethal(1)discs large lethal(1)discs-large lethal(2)discs large discs, large homolog 4 postsynaptic density protein 95 disks large homolog 4 PSD-95 PSD95/SAP90 PSD-95 alpha 2b PSD-95 beta SAP-90 discs large homolog 4 synapse-associated protein 90 synapse-associated protein SAP90 Tax interaction protein 15 post-synaptic density protein 95

GENE ID	SPEZIES
32083	Drosophila melanogaster
779559	Xenopus (Silurana) tropicalis
468444	Pan troglodytes
489462	Canis lupus familiaris
100137840	Bos taurus
405796	Danio rerio
13385	Mus musculus
29495	Rattus norvegicus
1742	Homo sapiens
100339587	Oryctolagus cuniculus

Ausgewählte Anbieter für anti-Discs, Large Homolog 4 (Drosophila) (DLG4) Antikörper

Haben Sie etwas anderes gesucht?

Telefon:	+1 877 302 8632
Fax:	+1 888 205 9894 (Toll-free)
E-Mail:	orders@antikoerper-online.de

Show all anti-Discs, Large Homolog 4 (Drosophila) (DLG4) Antikörper with Pubmed References