|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for CDC42(NM_001039802.1) Search again
Product ID:
HQP023454
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CDC42Hs, G25K, TKS
Gene Description:
cell division cycle 42
Target Gene Accession:
NM_001039802.1(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
|
|
| A | B |
|
Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
|
Summary
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.
Gene References into function
- Our findings indicate that different signaling cascades resulting in the activation of ..or Cdc42 can modulate the exocytotic process of neuroendocrine cells.
- Cdc42 is required for capillary lumen formation by vascular endothelial cells in three-dimensional extracellular matrices
- Data show that TGF-beta-induced rearrangements of the actin filament system required the activity of the Rho GTPases Cdc42 and RhoA, because ectopic expression of dominant negative mutant Cdc42 and RhoA abrogated the response.
- signaling to the cytoskeleton involves IQGAP1 as a component
- role for small GTPase CDC42Hs in the generation of skeletal muscle tumors.
- Structural basis for the selective activation of Rho GTPases by Dbl exchange factors
- SopE binds to and locks the switch I and switch II regions of human Cdc42(1-178) in a conformation that promotes guanine nucleotide release.
- Cdc42 play essential role in regulating the formation of dendritic processes by dendritic cell
- Effect of Mg(2+) on the kinetics of guanine nucleotide binding and hydrolysis
- The ability of a Cdc42(D118N) mutant to survive under apoptotic conditions accounts for its superior transforming activity compared to other activated versions of Cdc42.
- Rac1 and Cdc42 are activated independent of RhoG
- Cdc42 is involved in the mediation of intracellular lipid transport.
- Cdc42/Rac1-dependent activation of the p21-activated kinase (PAK) regulates human platelet lamellipodia spreading.
- Rac/Cdc42-dependent activation of MAPK/ERK is a critical event in the immediate phagocytic response of PMNs to microbial challenge.
- Data show that inhibition of endogenous RhoA, Rac1, and Cdc42 by their respective dominant negative mutants inhibits neurotensin-induced interleukin-8 protein production and promoter activity.
- VE-cadherin can serve as a scaffold involved in Cdc42 activation at the endothelial plasma membrane.
- TRE17 coprecipitated specifically with the active forms of Cdc42 and Rac1 in vivo. TRE17 is part of a novel effector complex for Cdc42 and Rac1, potentially contributing to their effects on actin remodeling.
- Upregulation during arachidonic acid mediated HeLa cell adhesion.
- Instead of inducing neurite formation, a constitutively active form of human Cdc42 stimulates the proliferation of rat PC12 cells in the presence of nerve growth factor.
- Cdc42 regulates the activitity of p21-activated protein kinase 5
- Activated CDC42 at the leading edge of a neutrophil in culture helps orient the cell's axis in a signaling complex with G beta gamma, PAK1, and PIXalpha.
- Activated CDC42 helps orient the neutrophil's axis in a signaling complex with Gbeta gamma, PAK1, and PIXalpha.
- Directional sensing requires GNB1-mediated PAK1 and PIX alpha-dependent activation of Cdc42.
- BNIPL-2, a novel homologue of BNIP-2, interacts with Bcl-2 and Cdc42GAP in apoptosis.
- Activation of the small Rho GTPase Cdc42 plays a specific role in the actin reorganization mediated by CD28 in human T cells.
- direct activation of Cdc42 and Rac1 by invasive Salmonella is a prerequisite of Salmonella-mediated death of U937 cells.
- in neutrophils, Rac2 and Cdc42 are involved in FcR- and CR3-induced activation and for properly functioning signal transduction involved in the generation of oxygen radicals.
- The reorganization of actins into podosomes is controlled by CDC42 GTP-binding protein.
- Cdc42 signaling has a role in apoA-I-induced cholesterol efflux
- The delayed activation of Cdc42 represents a negative-feedback mechanism that signals adherens junction reassembly after the increase in endothelial permeability induced by inflammatory mediators such as thrombin.
- Cdc42 synergistically with Rac1 induces lamellipodia and membrane ruffles in EGF-stimulated cells.
- Cdc42 signal transduction to the nucleus requires ACK-1 and ACK-2
- Cdc42 has a role in mediation of UV-induced p38 activation by G protein betagamma subunits
- novel role for Smad7 in TGF-beta-dependent activation of Cdc42
- C. parvum invasion of target epithelia results from the organism's ability to activate a host cell Cdc42 GTPase signaling pathway to induce host cell actin remodeling at the attachment site.
- a specific region in Cdc42 confers the binding specificity to activated Cdc42-associated kinase
- cross-talk between Rac and Cdc42 GTPases regulates generation of reactive oxygen species
- role of frabin, a guanine nucleotide exchange factor specific for Cdc42, in the activation of Cdc42 during Cryptosporidium parvum infection of biliary epithelial cells
- cdc42 has a role in activating c-Jun N-terminal kinase activation with Nck1
- Both Cdc42 & Rac1 control the transport of essential immunostimulatory molecules to the DC surface. Cdc42 and Rac1 signaling controls DC morphology and conditions DCs for efficient CD8(+) T cell stimulation.
- Detailed analysis of backbone dynamics of the single-point mutant of Cdc42Hs(F28L) indicates how the mutation disrupts interactions that destabilize the local structure, leading to multiple time-scale motions of residues in the binding site.
- nucleotide-free Cdc42 might be sequestered by IQGAP1 to prevent signaling
- localized activation in the trans-Golgi apparatus, microtubule-dependent Cdc42 activation at the cell periphery, and activation kinetics precisely coordinated with cell extension and retraction was revealed by a biosensor
- Defined phospholipid oxidation products are capable of increasing EC barrier function via signaling mechanisms mediated by small GTPases Rac and Cdc42 leading to EC cytoskeletal remodeling and barrier restoration.
- actin has opposing roles in Cdc42p polarization
- BNIP-2 in vivo induces cell dynamics by recruiting Cdc42
- Distinct spatial association patterns between Cdc42 and its key effector proteins PAK1 and N-WASP controlling cytoskeletal remodeling were revealed.
- a Cdc42-MRCK signal mediates myosin-dependent cell motility and there is convergence between Rho and Cdc42 signalling
- MMP-1 expression is maintained at a low level by Cdc42 via a repression of the Rac1 and ERK1/2 pathways when cell/extracellular-matrix interactions via integrins induce cytoskeleton organization
- The cdc42 GTP-Binding Protein regulates the intracellular localization of PTEN in leukocytes and human transfected embryonic kidney cells.
- The cdc42 GTP-Binding Protein function was shown to be required for PTEN localization in leukocytes.
- Results describe a quantitative model of allosteric regulation of the Wiskott-Aldrich syndrome protein (WASP) by the Rho GTPase Cdc42.
- Silencing of Cdc42 by small interfering RNA induced massive apoptosis, indicating that tumor cell survival requires a minimal Cdc42 activity.
- Activation of small RhoGTPases is a key step in the mechanism of epithelial mesemchymal transdifferentiation and likely to be a contributor to tubulointerstitial fibrosis.
- a Cdc42 mutant is specifically activated by intersectin
- binding of Cdc42 localizes Pak2 to the endoplasmic reticulum, where autophosphorylation alters association of the two proteins
- the signals induced by integrin alpha6beta1 modulate at the level of PI3K and Cdc42 activity to allow platelets to actively form filopodia
- The two unique glutamates in Cdc42 and basic region of WASp generate favorable electrostatic steering forces that control the accelerated WASp-Cdc42 association reaction.
- Cdc42 induces activation loop phosphorylation and membrane targeting of mixed lineage kinase 3
- Cdc42 regulates AJ permeability by controlling the binding of alpha-catenin with beta-catenin and the consequent interaction of the VE-cadherin/catenin complex with the actin cytoskeleton.
- Results suggest that ABCA1 transduces signals from apolipoprotein A-I (apoA-I) by complexing and activating Cdc42 and downstream kinases and, therefore, acts as a full apoA-I receptor.
- results indicated that VPS28 and Cdc42are associated with the influenza A virus M1 protein and are involved in the influenza virus life cycle
- Cdc42 is a critical regulator of T cell actin dynamics, T cell receptor clustering, and cell cycle entry. Cdc42 activity in specific locations at specific times is most critical for its function in T cell activation.
- PIP3 and Cdc42 maintain stable polarity with a single front and a single back not only by strengthening pseudopods but also, at longer range, by promoting RhoA-dependent actomyosin contraction at the trailing edge.
- NFAT1, a transcription factor connected with breast cancer metastasis, is activated by Wnt-5a through a Ca2+ signaling pathway in human breast epithelial cells which was simultaneously counteracted by a Wnt-5a-induced Yes/Cdc42 signaling pathway.
- Cdc42 is an important downstream factor in the pathway through which PKC mediates morphological and cytoskeletal effects
- Cdc42 exerts its effects on cell migration in part through its effector Ack1, which regulates p130(Cas) signaling.
- Rho family GTPases play a distinct role in Salmonella-induced cellular responses.
- These results support a model whereby the synergic bundling activity of the IRSp53-Eps8 complex, regulated by Cdc42, contributes to the generation of actin bundles, thus promoting filopodial protrusions.
- Complex interplay of Rho, Rac and Cdc42 in the process of EphB-mediated cell retraction-recovery responses.
- Maspin controls mammary tumor cell migration through inhibiting Rac1 and Cdc42, but not RhoA GTPase.
- We propose that increased water influx through AQP9 is critically involved in the formation of membrane protrusions, and that AQP9-induced actin polymerization is augmented by activation of Cdc42 and PKC(zeta).
- Signaling to the actin cytoskeleton by low and high concentrations of resveratrol may be differentially regulated by Rac and Cdc42.
- OxPAPC promoted novel interactions between focal adhesion and adherens junction complexes via paxillin and beta-catenin association, which was critically dependent on Rac and Cdc42 activities.
- Efficient phagosomal maturation and the subsequent eradication of ingested microbes in human neutrophils is dependent on a strictly regulated Cdc42 pathway.
- Results of this study suggest that the Rho-family GTPases are required for efficient invasion of HeLa cells by GBS.
- C. jejuni invade host target cells by a unique mechanism and the activation of the Rho GTPase members Rac1 and Cdc42 plays a crucial role in this entry process.
- These data suggest a mechanism whereby precise spatial guanine nucleotide exchange of Cdc42 by Dbl is dependent on functional ERM proteins and is important for directional cell migration.
- Results describe the neurite outgrowth multiadaptor RhoGAP, NOMA-GAP, and show that it regulates neurite extension through SHP2 and Cdc42.
- IQGAP1 regulates Salmonella invasion through interactions with actin, Rac1, and Cdc42
- FGFR-mediated phosphorylation of ephexin1 enhances the guanine nucleotide exchange activity toward RhoA without affecting the activity to Rac1 or Cdc42.
- Cdc42 signaling contributes to immune escape of cancer
- These results indicate that START-GAP3/DLC3 has characteristics similar to other START-GAPs and the START-GAP family seems to share common characteristics.
- signaling pathway by which G(i)-coupled receptor specifically induces Rac and Cdc42 activation through direct interaction of Gbetagamma with FLJ00018.
- DOCK2 and DOCK9 specifically recognize Rac2 and Cdc42 through their switch 1 as well as beta2-beta3 regions and the mode of recognition via switch 1 appears to be conserved among diverse Rac-specific DHR-2 GEFs
- Theses results support a novel role for FPR stimulation in enhancing intestinal epithelial cell restitution through PI3K-dependent activation of Rac1 and Cdc42.
- Silencing Cdc42 blocks activation of EGFR and Src induced by Ca2+ depletion, resulting in a reduction in E-cadherin degradation
- role of RHO GTPases RAC1 and CDC42 in PGE(2)-mediated migratory responses of extravillous trophoblast cells
- Bioinformatics and functional analyses revealed a spatially compartmentalized Rac/Cdc42 signaling network that operates in conjunction with multiple guanine-nucleotide exchange factors and GTPase-activating proteins to control neurite formation
- LKB1 interacts only with active form of cdc42 and PAK, but not with inactive cdc42. Taken together, these results show that LKB1 is a critical mediator of the NSCLC polarity program in lung cancer cells through a novel LKB1-cdc42-PAK pathway.
- TGFbeta1 stimulates CCN2 expression in human gingival fibroblasts through a RhoA-independent, Rac1/Cdc42-dependent mechanism
- Data show that Cdc42- and Rac1-mediated endothelial lumen formation requires Pak2, Pak4 and Par3, and PKC-dependent signaling.
- analysis of TGF-beta1-independent changes in protein neosynthesis, p38alphaMAPK, and cdc42 in hydrogen peroxide-induced senescence-like morphogenesis
- The purpose of this study was to characterize the significance of Rho processes in the cellular cytoskeleton.
- structural analysis of the influence of effector proteins on the signaling-active state of the small GTPase Cdc42
- These findings suggest a novel MUC1-Src-CrkL-Rac1/Cdc42 signaling cascade following ICAM-1 ligation, through which MUC1 regulates cytoskeletal reorganization and directed cell motility during cell migration.
- Data suggests that actin polymerization and cdc42 are required for activation of integrin alpha2beta1, but not alpha(IIb)beta3, thereby critically regulating platelet adhesion to and activation by collagen.
- salmonella enterica SopB colocalizes with activated Cdc42 near the plasmalemma, but there was no evidence that SopB alone can alter Cdc42 activity
- The exocyst subunits Sec3 and Sec8 interact with the polarity protein IQGAP1 and that this interaction is triggered by active Cdc42 and RhoA, which are essential for matrix degradation.
- strongly activated in HTLV-1 infected T cell lines derived from HAM/TSP patients.
- Fanconi anemia group A proteins influence BM progenitor homing and adhesion via the small GTPase Cdc42-regulated signaling pathway.
- Cdc42 was found to be overexpressed with high incidence (60%) in colorectal cancer samples, and this expression was associated with silencing of ID4 with statistical significance (p<0.05).
- 1) PAK plays a required role in hyperosmotic signaling through the PI3K/pTEN/Cdc42/PP2Calpha/p38 pathway, and 2) PAK and PP2Calpha modulate the effects of this pathway on focal adhesion dynamics.
- IpaC could not be shown to interact directly with Cdc42, a host GTPase closely tied to Shigella invasion.
- Nm23-H1 can negatively regulate cell migration and tumor metastasis by modulating the activity of Cdc42 and possibly other Rho family members through interaction with Dbl-1
- In melanoma, expression of activated Cdc42 induces a mesenchymal-amoeboid transition and increases cell invasion.
- levels of GTPase Cdc42 could be associated with slow growth of BCL2 overexpressing immortalized breast cell line
- the interaction of the RAGE cytoplasmic domain with Dia-1 is required to transduce extracellular environmental cues evoked by binding of RAGE ligands to their cell surface receptor, resulting in Rac-1 and Cdc42 activation and cellular migration
- EB1 is controlled by c-Myc, RhoA, and CDC42, which have all been linked to hepatocellular carcinoma (HCC) malignancy.
- Cdc42 was necessary for the growth and maintenance of already established lymphomas in vivo. These data open perspectives for new therapeutic strategies by revealing a mechanism of regulation of anaplastic large cell lymphoma cell growth through Cdc42
- Cdc42 regulates epithelial tissue morphogenesis by controlling spindle orientation during cell division.
- study found Vibrio VopS could act to covalently modify a conserved threonine residue on Rho, Rac & Cdc42 with AMP; resulting AMPylation prevented interaction of Rho GTPases with downstream effectors, inhibiting actin assembly in the infected cell