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anti-Human CDC42 Antikörper:
anti-Mouse (Murine) CDC42 Antikörper:
anti-Rat (Rattus) CDC42 Antikörper:
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Human Polyclonal CDC42 Primary Antibody für IHC, WB - ABIN6672618
Liu, Feng, Chen, Luo, Yan, Chen, Lin, Ding, Wen: Dcf1 Triggers Dendritic Spine Formation and Facilitates Memory Acquisition. in Molecular neurobiology 2018
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Mouse (Murine) Polyclonal CDC42 Primary Antibody für IHC, WB - ABIN3021671
Fang, Li, Han, Zhao, Gao, Yan, Luo: Overexpression cdc42 attenuates isoflurane-induced neurotoxicity in developmental brain of rats. in Biochemical and biophysical research communications 2017
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Human Monoclonal CDC42 Primary Antibody für IF, ELISA - ABIN533151
Erickson, Cerione: Multiple roles for Cdc42 in cell regulation. in Current opinion in cell biology 2001
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Cow (Bovine) Polyclonal CDC42 Primary Antibody für IHC (fro), WB - ABIN549181
Zhang, Zhang, Zhang, Lin, Ge: Quantitative proteomics analysis reveals BAG3 as a potential target to suppress severe acute respiratory syndrome coronavirus replication. in Journal of virology 2010
Human Polyclonal CDC42 Primary Antibody für IHC, WB - ABIN6714597
Cai, Wang, Huang, Chen, Zuo: A novel effect of polychlorinated biphenyls: impairment of the tight junctions in the mouse epididymis. in Toxicological sciences : an official journal of the Society of Toxicology 2014
Cow (Bovine) Polyclonal CDC42 Primary Antibody für IHC (p), WB - ABIN3044385
Han, Zhuang, Chen, Zhu, Cai, Lu et al.: Novel derivative of Paeonol, Paeononlsilatie sodium, alleviates behavioral damage and hippocampal dendritic injury in Alzheimer's disease concurrent with cofilin1/phosphorylated-cofilin1 and ... in PLoS ONE 2017
Human Polyclonal CDC42 Primary Antibody für ELISA, IHC - ABIN6260686
Li, Xiong, Xu, Duan, Yang, Zhou, Tu: miR-29a regulated ER-positive breast cancer cell growth and invasion and is involved in the insulin signaling pathway. in Oncotarget 2018
In Par6A knockout cells, we find that active Cdc42 is more mobile at the apical membrane compared to control cells and that wild type Cdc42 is more diffusely localized throughout the cell, indicating that Par6A is required to restrict Cdc42 signaling.
Our data thus link FMNL2/3 formins to actin assembly-dependent functions of Cdc42 in anterograde transport through the Golgi apparatus.
The data presented improve our understanding of the Cdc42-WASP interface and also add to the body of information available for Cdc42-effector complex formation, therapeutic targeting of which has promise for Ras-driven cancers.
MiR-15a negatively regulates epithelial junctions through Cdc42 in Caco-2 cells and pediatric inflammatory bowel disease patients.
High CDC42 expression is associated with pancreatic cancer.
Cdc42 levels increased in the brains of patients affected by Alzheimer's disease and frontotemporal lobar degeneration (FTLD). Cdc42 levels decreased in the plasma of patients affected by FTLD.
Data suggest that CDC42 binding to Ex-domain of IQGAP2 releases Ex-domain at C-terminal region of GRD2 domain, facilitating IQGAP2 dimerization; this promotes allosteric changes in ras GTPase-activating protein binding site providing binding site for second CDC42; RAC1 binds only to apo-IQGAP2. (IQGAP2 = IQ motif containing GTPase activating protein-2; CDC42 = GTP-binding protein CDC42; RAC1 = Rac family small GTPase-1)
The spatial extent of Rho GTPases gradients governs cell migration, a sharp Cdc42 gradient maximizes directionality while an extended Rac1 gradient controls the speed.
Coincident with the loss of PICK1 by GBF1-activated ARF1, CDC42 recruitment leads to the activation of IRSp53 and the ARP2/3 complex, resulting in a burst of F-actin polymerisation potentially powering scission.
Study revealed that miR3423p levels were significantly inversely correlated with the protein levels of its target CDC42 in nasopharyngeal carcinoma (NPC) tissues. Overexpression of miR-342-3p inhibited NPC cell proliferation and invasion by directly targeting CDC42.
Methylmercury chloride negatively affects the activation of Src, Rac1 and Cdc42, all of which are critical proteins for the regulation of cell movement.
Cdc42BPA and Cdc42 signaling are important for colon cancer invasion, and Cdc42BPA has potential implications for colon cancer prognosis and treatment.
new treatments using small molecules and miRNAs to inhibit the abnormal overexpression of Cdc42 that may slow down the metastasis process, improve cancer therapy and lead to novel strategies for development of antineoplastic drugs.
we present a third patient with TKS. The heterozygous mutation of CDC42 (p.Tyr64Cys) is likely a hot-spot mutation for TKS.
X-ray crystallography reveals that in addition to the canonical PAK4 CDC42/RAC interactive binding (CRIB) domain binding to CDC42 there are unexpected contacts involving the PAK4 kinase C-lobe, CDC42, and the PAK4 polybasic region.
Cdc42 plays a role in regulating the proliferation of PMVECs stimulated with small doses of LPS, and this regulation involves the ERK pathway
Data show that Ras-like without CAAX 1 protein (RIT1) binds the RHO GTPases CDC42 and RAC1, both of which are crucial regulators of actin dynamics upstream of PAK1.
The results show that PTEN controls multicellular assembly through a membrane-associated regulatory protein complex composed of beta-Arrestin1, ARHGAP21 and Cdc42.
CDC42 acts as an essential factor in regulating cell proliferation and also takes part in lipotoxic effects of palmitate.
loss of XIAP enhances filopodia formation in a Cdc42-dependent manner and this phenomenon phenocopies EGF stimulation. Further, XIAP depletion promotes lung colonization of tumor cells in mice in a Cdc42-dependent manner. These observations shed molecular insights into ubiquitin-dependent regulation of Cdc42 and that of actin cytoskeleton.
results identify a novel link between Cdc42 activity and the hematopoiesis-supportive function of mesenchymal stroma cells
Cdc42 is a bona fide regulator of peripheral tolerance through suppression of Th17 aberrant differentiation/pathogenicity and promotion of regulatory T cell differentiation/stability/function involving metabolic signaling.
Elevated expression of miR302-367 in endothelial cells inhibits developmental angiogenesis via CDC42/CCND1 mediated signaling pathways.
This study observed impaired collagen I secretion in mesenchymal stem cells lacking RhoA or Cdc42.
We concluded that CDC42 negatively regulates SEPT12 polymerization and is involved in terminal structure formation of sperm heads.
These results of this study suggest that Cdc42 and Rac1 synergistically function in BG during cerebellar corticogenesis.
Cdc42 and RhoA act as a regulatory circuit downstream of the megakaryocytes -specific mechanoreceptor GPIb to coordinate polarized transendothelial platelet biogenesis.
Cdc42 deficiency impairs endothelial cell function and regeneration after inflammatory vascular injury.
MiR-7 inhibited peripheral nerve injury repair by affecting neural stem cells migration and proliferation through cdc42.
downregulation of Cdc42, but not Rac1, is responsible for the unusual biophysical features of tumor repopulating cells.
Rac1 and Cdc42 have cooperating roles in regulation of bone development.
results suggest epithelium cell-specific Cdc42 deletion leads to tooth hypomaturation and transformation of the enamel prism structure that is likely due to altered ameloblast morphology and the secretion of enamel matrix proteins and proteases. This is the first in vivo evidence suggesting that Cdc42 is essential for proper tooth development and amelogenesis.
Although much of the basic actin machinery was intact, Cdc42 null cells lacked the ability to polarize their Golgi and coordinate motility systems for efficient movement. Loss of Cdc42 de-coupled three main systems: actin assembly via the formin FMNL2 and Arp2/3, active myosin-II localization, and integrin-based adhesion dynamics.
Cdc42 is required for endothelial tip cell selection, directed cell migration and filopodia formation, but dispensable for cell proliferation or apoptosis. Although the loss of Cdc42 seems generally compatible with apical-basal polarization and lumen formation in retinal blood vessels
Cdc42 bypasses the need for exogenous fibronectin by stimulating cellular fibronectin deposition under the newly formed lamellipodia.
Simulated microgravity activates Cdc42 via Rap1GDS1 to promote vascular branch morphogenesis.
In contrast to neuronal cells, Botulinum neurotoxin type B uses a Cdc42-dependent pathway to enter intestinal cells.
We conclude that CRN7 spatiotemporally influences F-actin organization and Golgi integrity in a Cdc42- and N-WASP-dependent manner.
the expression of CDC42 might be regulated by AHR, and both proteins are fundamental to the development of normal spermatozoa and the acrosome reaction.
CDC42 loss suppresses acute myeloid leukemia cell polarity and division asymmetry.
shear-stimulated integrin dynamics induce polarized Cdc42 activity, which induces MTOC localization through the Par6-protein kinase Czeta complex.
This study revealed a novel signaling pathway activated during M. avium subsp. paratuberculosis entry that links the product of MAP3464 gene to activation of Cdc42 in the host cell.
These data are consistent with the idea that migrating corneal epithelial cells use a cdc42/rho "switch" to sort vectoral cues, with cdc42 controlling electrotaxis and rho controlling contact guidance.
Knockdown of fat1 in zebrafish causes pronephric cysts, which is partially rescued by RAC1/CDC42 activators, confirming a role of the two small GTPases in the pathogenesis.
Cdc42 deficiency causes ciliary abnormalities and cystic kidneys.
Cdc42 GTPase and Rac1 GTPase act downstream of p120 catenin and require GTP exchange during gastrulation of zebrafish mesoderm.
These results suggest that Ptenb by antagonizing PI3 kinase and its downstream Akt1 and Cdc42 to regulate actin polymerization that is critical for proper cell motility and migration control during gastrulation in zebrafish.
This suggests that TOCA1 binding to Cdc42 is an early step in the Cdc42-dependent pathways that govern actin dynamics, and the differential binding affinities of the effectors facilitate a handover from TOCA1 to N-WASP, which can then drive recruitment of the actin-modifying machinery.
The small GTPase Cdc42 promotes membrane protrusion during polar body emission via ARP2-nucleated actin polymerization.
these data indicate that the ITSN2 exchange factor regulates the activity of Cdc42 during embryo development affecting actin cytoskeleton in Xenopus embryos.
These results demonstrate that to participate in the control of the actin cytoskeleton, RLIP needs its complete N-terminal region coding for the mu2BD and the GAP domain.
Data show that in Xenopus laevis oocytes, polar body emission requires a RhoA contractile ring and Cdc42-mediated membrane protrusion.
In vivo imaging reveals a role for Cdc42 in spindle positioning and planar orientation of cell divisions during vertebrate neural tube closure.
CDC42 is an indispensable protein during porcine oocyte meiosis, and CDC42 may interact with N-WASP, ROCK, and cofilin in the assembly of actin filaments during porcine oocyte maturation.
Hypoxic pulmonary arterial myocytes challenged with a thromboxane mimetic polymerize actin via the Cdc42 pathway, reflecting increased Cdc42 association with neuronal Wiskott Aldrich Syndrome protein.
Cdc42 is involved in the regulation of alppha-smooth muscle actin promoter activation through p21-activated kinase, p38, myocardin-related transcription factor and serum response factor. Cdc42 may be an important regulator of MRTF cellular localization
Cdc42 controls protrusion formation in a cell non-autonomous manner.
Cdc42 regulates binding of Crumbs protein to the Par-6 CRIB-PDZ module.
We propose that the guanine nucleotide exchange factor GEFmeso is involved in a developmental process that requires the synergistic action of CDC42 and Rac1 during Drosophila development
A proof-of-principle experiment in which the Cdc42 GTPase associates with its alleged partner WASp within neurons during the time and space that coincide with the newly developing CNS.
The distinct buttoning mechanism we propose for dorsal vessel closure is elaborated through signaling pathways regulating Cdc42 activity in this cell type.
there is a mutual dependence between Par proteins and Cdc42 for their localization, regulation of the actin cytoskeleton and, consequently, for the establishment of oocyte polarity
Zir is necessary to activate the Rho-family GTPases Rac2 and Cdc42 during the Drosophila cellular immune response.
Results identify the Cdc42/Par6/atypical protein kinase C (aPKC) Par polarity complex as uniquely and specifically regulating apoptosis-induced compensatory proliferation in Drosophila epithelia.
Wsp activity in within the fly testis is mediated by the small GTPase Cdc42.
Data demonstrate that Cdc42 and Merlin act together with Pak1 to control salivary gland lumen size.
Drosophila Rich (dRich), a conserved Cdc42-selective guanosine triphosphatase-activating protein (GAP), inhibits the Cdc42-Wsp pathway to stimulate postsynaptic Gbb release
Recruitment of Cdc42 and Rac1 to the sites of filopodium and lamellipodium formation is Rab35 dependent and occurs by way of microtubule tracks.
ACK family tyrosine kinase activity is a component of Dcdc42 signaling during dorsal closure in Drosophila melanogaster.
Cdc42 is a regulator for multiple aspects of dendritic development in Drosophila
Both Rac1 and Cdc42 activation induced large growth cones and long filopodia, but Cdc42 did so more efficiently than Rac1. Cdc42 is specifically involved in the regulation of actin filaments in growth cones.
The identification and characterization of a DBL-like guanine nucleotide exchange factor (GEF) in Drosophila, called GEFmeso, as a novel binding target of the Ras-like GTPase Ral.
Rho GTPases may have partially overlapping functions during planar cell polarity generation
In addition to regulating Par-6-aPKC localization, Cdc42 increases aPKC activity by relieving Par-6 inhibition.
Synaptic growth activated by growth factor signaling is controlled at an endosomal compartment via coordinated Nwk and Cdc42-dependent actin assembly.
loss of function is accompanied by the accumulation of apical E-Cad intracellular punctate structures and the disruption of adherens junctions in epithelial cells
genetic interactions with CDC42-related genes MSB1, a putative scaffold protein, and RGD3, a putative Rho GTPase-activating protein (GAP) were identified
The Cdc24 EF-hand motif is essential for polarity establishment but not for polarity maintenance.
Rsr1 focuses Cdc42 activity at hyphal tips and promotes maintenance of hyphal development in Candida albicans.
These results suggest the development of hyphal-specific characteristics is promoted by Cdc42-GTP in a process that also requires the intrinsic GTPase activity of Cdc42.
The distribution patterns of F-actin were compared to the patterns of Wasp and its putative interaction partners: Wasp and RhoB, but not RhoA or Cdc42, localization overlap with F-actin during capacitation and the acrosome reaction.
results suggest that cell division control protein 42(CDC42) activation is favored by the disruption of the caveolin-1-CDC42 interaction, allowing for its participation in the regulation of capacitation and the acrosome reaction
The protein encoded by this gene is a small GTPase of the Rho-subfamily, which regulates signaling pathways that control diverse cellular functions including cell morphology, migration, endocytosis and cell cycle progression. This protein is highly similar to Saccharomyces cerevisiae Cdc 42, and is able to complement the yeast cdc42-1 mutant. The product of oncogene Dbl was reported to specifically catalyze the dissociation of GDP from this protein. This protein could regulate actin polymerization through its direct binding to Neural Wiskott-Aldrich syndrome protein (N-WASP), which subsequently activates Arp2/3 complex. Alternative splicing of this gene results in multiple transcript variants. Pseudogenes of this gene have been identified on chromosomes 3, 4, 5, 7, 8 and 20.
G25K GTP-binding protein
, GTP binding protein, 25kDa
, GTP-binding protein, 25kD
, cell division control protein 42 homolog
, dJ224A6.1.1 (cell division cycle 42 (GTP-binding protein, 25kD))
, dJ224A6.1.2 (cell division cycle 42 (GTP-binding protein, 25kD))
, growth-regulating protein
, small GTP binding protein CDC42
, cell division cycle 42 homolog
, CDC42 GTP-binding protein
, Cell division control protein 42 homolog
, Cdc42 protein homolog
, cell division control protein 42-like protein
, cell division cycle 42 (GTP binding protein, 25kDa)
, likely rho family Ras-like GTPase
, cell division cycle 42