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anti-Human CDC42 Antibodies:
anti-Mouse (Murine) CDC42 Antibodies:
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Human Polyclonal CDC42 Primary Antibody for 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
Cdc42BPA (show CDC42BPA Antibodies) and Cdc42 signaling are important for colon cancer invasion, and Cdc42BPA (show CDC42BPA Antibodies) 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 (show PTK6 Antibodies). The heterozygous mutation of CDC42 (p.Tyr64Cys) is likely a hot-spot mutation for TKS (show PTK6 Antibodies).
X-ray crystallography reveals that in addition to the canonical PAK4 (show PAK4 Antibodies) CDC42/RAC (show AKT1 Antibodies) interactive binding (CRIB (show SCRIB Antibodies)) domain binding to CDC42 there are unexpected contacts involving the PAK4 (show PAK4 Antibodies) kinase C-lobe, CDC42, and the PAK4 (show PAK4 Antibodies) polybasic region.
Cdc42 plays a role in regulating the proliferation of PMVECs stimulated with small doses of LPS (show IRF6 Antibodies), and this regulation involves the ERK (show EPHB2 Antibodies) pathway
Data show that Ras-like without CAAX 1 (show RIT1 Antibodies) protein (RIT1 (show RIT1 Antibodies)) binds the RHO GTPases CDC42 and RAC1, both of which are crucial regulators of actin dynamics upstream of PAK1 (show PAK1 Antibodies).
The results show that PTEN controls multicellular assembly through a membrane-associated regulatory protein complex composed of beta-Arrestin1 (show ARRB1 Antibodies), ARHGAP21 (show ARHGAP21 Antibodies) 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.
Cdc42 can affect multiple morphogenetic processes during angiogenic sprouting and ultimately impact the architecture of the vasculature.
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 (show FN1 Antibodies) by stimulating cellular fibronectin (show FN1 Antibodies) deposition under the newly formed lamellipodia.
Simulated microgravity activates Cdc42 via Rap1GDS1 (show RAP1GDS1 Antibodies) to promote vascular branch morphogenesis.
In contrast to neuronal cells, Botulinum neurotoxin type B (show BoNT/B Antibodies) 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 (show AHR Antibodies), and both proteins are fundamental to the development of normal spermatozoa and the acrosome reaction.
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 (show FAT1 Antibodies) 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 (show RACGAP1 Antibodies) and Rac1 GTPase (show RACGAP1 Antibodies) act downstream of p120 catenin (show CTNND1 Antibodies) and require GTP (show AK3 Antibodies) 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 (show RHOA Antibodies) 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 (show CDKN1A Antibodies)-activated kinase, p38 (show MAPK14 Antibodies), myocardin (show MYOCD Antibodies)-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 (show PARD6A Antibodies) CRIB (show SCRIB Antibodies)-PDZ (show INADL Antibodies) 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 (show RAC2 Antibodies) and Cdc42 during the Drosophila cellular immune response.
Results identify the Cdc42/Par6 (show PARD6A Antibodies)/atypical protein kinase C (show PRKCZ Antibodies) (aPKC) Par (show AFG3L2 Antibodies) 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 (show RACGAP1 Antibodies) Cdc42.
Data demonstrate that Cdc42 and Merlin (show NF2 Antibodies) act together with Pak1 (show PAK1 Antibodies) to control salivary gland lumen size.
genetic interactions with CDC42-related genes MSB1, a putative scaffold protein, and RGD3, a putative Rho GTPase-activating protein (GAP) were identified
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 (show AK3 Antibodies) in a process that also requires the intrinsic GTPase (show RACGAP1 Antibodies) 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 (show CAV1 Antibodies)-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