|
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 CDH5(NM_001795.4) Search again
Product ID:
HQP000052
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
7B4, CD144
Gene Description:
cadherin 5
Target Gene Accession:
NM_001795.4(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
This gene is a classical cadherin from the cadherin superfamily and is located in a six-cadherin cluster in a region on the long arm of chromosome 16 that is involved in loss of heterozygosity events in breast and prostate cancer. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. Functioning as a classic cadherin by imparting to cells the ability to adhere in a homophilic manner, the protein may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. An alternative splice variant has been described but its full length sequence has not been determined. [provided by RefSeq].
Gene References into function
- Imaging studies of VE-cadherin in a flow model show neutrophil and monocyte transmigration occurring exclusively at the cell borders through formation of transient gaps in VE-cad distribution, as well as through preexisting gaps.
- Loss of vascular endothelial cadherin-mediated cell-cell adhesion increases the permeability of bone marrow endothelial cell monolayers and stimulates the transendothelial migration of CD34+ cells in response to stromal cell-derived factor-1 alpha.
- An octapeptide in the juxtamembrane domain of VE-cadherin is important for p120ctn binding and cell proliferation.
- results suggest that the inadequate trophoblastic invasion, induced by antiphospholipid antibodies, can be the result of decreased alpha1 integrin and VE-cadherin and increased alpha5 integrin and E-cadherin expression in the trophoblast
- VEC may influence the constitutive organization of the actin cytoskeleton.
- TNF-alpha affects VE-cadherin gene expression on the transcriptional level, inducing a downregulation of the VE-cadherin expression.
- Results show that P2X4 and P2X6 receptors are associated with VE-cadherin at HUVEC adherens junctions.
- TNFalpha significantly increased permeability and induced p38 and ERK MAPK activation compared with controls (P < 0.05). These changes were associated with a loss of membrane-associated VE cadherin
- tyrosine phosphorylation of VE cadherin is an important regulatory pathway associated with TNF-induced endothelial barrier dysfunction.
- ADAM15 colocalizes with vascular endothelial (VE)-cadherin, which mediates endothelial cell adherens junction formation
- During transmigration of neutrophils through umbilical vein endothelium, VE-cadherin moved away to different ends of the transmigration site so that VE-cadherin-containing adherent junctions were relocated aside.
- Data show that VE-cadherin and beta-catenin are only weakly associated with the actin-based cytoskeleton in cultured human vascular endothelial cells.
- cleavage of VE cadherin by neutrophil surface-bound proteases induces formation of gaps through which neutrophils transmigrate
- VE-cadherin actively participates in inside-out signaling at the plasma membrane, leading to the development of endothelial membrane protrusions.
- results provide new insights into the mechanisms of VE-cadherin processing and degradation in microvascular endothelial cells
- Human Schlemm's canal cells express the endothelial adherens proteins, VE-cadherin and PECAM-1.
- Modification by protein kinase C contributes to vascular endothelium barrier dysregulation induced by thrombin
- the intracellular association of VE-cadherin with beta-catenin-linked cytoskeleton is essential to the maintenance of endothelial junctional integrity and microvascular permeability.
- elevated plasma levels in coronary artherossclerosis
- interacts with p120 catenin to mediate cell locomotion and proliferation
- Histamine interrupts cadherin adhesion and this effect on cadherin adhesion is independent of capacitive calcium flux.
- Serum VE-cadherin decreases significantly in both estradiol and raloxifene treated postmenopausal women.
- VE-cadherin is involved in transendothelial migration of TCs, and replacement of DECs by TCs is not the result of apoptosis.
- cAMP-Epac-Rap1 signaling promotes decreased cell permeability by enhancing VE-cadherin-mediated adhesion lined by the rearranged cortical actin
- cleaved by Porphyromonas gingivalis gingipains in endothelial cells
- promoter is subjected to bFGF induction, silencer elements may be located elsewhere in the gene
- upregulation of MIP-1beta and downregulation of VE-cadherin may strongly participate in human acute heart rejection.
- G alpha12 interaction with alphaSNAP induces VE-cadherin localization at endothelial junctions and regulates barrier function
- A single phosphorylation event within the VE-cadherin cytoplasmic tail is sufficient to maintain cells in a mesenchymal state.
- Results suggest that in human umbilical vein endothelial cells Epac1 controls VE-cadherin-mediated cell junction formation and induces reorganization of the actin cytoskeleton.
- 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.
- VE-cadherin and EphA2 act in a coordinated manner as a key regulatory element in the process of melanoma vasculogenic mimicry.
- Thus, VEC limits cell proliferation by retaining VEGFR-2 at the membrane and preventing its internalization into signaling compartments.
- Tyrosine phosphorylation mediated by Src kinase on cadherin 5 residue Tyr685 is a process that appears to be critical for vascular endothelial growth factor (VEGF)-induced endothelial cell migration.
- Surprisingly, the VE-cadherin-associated PAR protein complex lacks aPKC. Ectopic expression of VE-cadherin in epithelial cells affects tight junction formation.
- Here, we show that, in some transformed lines, cadherin adhesion molecules exhibit a flow-like movement in a basal-apical direction at the cell junction and that this flow is associated with reorganizing actin filaments.
- OxidizedLDL downregulated VE Cadherin on endothelial junctions in an in vitro model of transendothelial monocyte migration
- Strategies targeting signals in the marrow microenvironment that amplify the Bcr-abl/VE-cadherin/beta-catenin axis may have utility in sensitizing drug-resistant leukemic stem cells.
- basal Rho kinase activity was essential for proper expression of the adhesion molecule VE-cadherin in human vascular endothelial cells
- Endothelial cell junctional proteins respond to flow transiently by increasing the strength of intercellular attachments early after flow onset, supporting the view on the active role of intercellular adhesions in mechanotransduction.
- VE-cadherin has a role in modulating c-Src activation in VEGF signaling
- a new pathway regulating angiogenesis and endothelial survival, via the transcription factor Erg and the adhesion molecule VE-cadherin.
- Addition of PBMCs to DV-2-infected HUVECs decreased the levels of mRNA transcripts and cell-surface expression of VE-cadherin.
- results suggest that VE-cadherin and beta-catenin binding dynamics are important determinants in microvascular barrier regulation
- VE-cadherin promotes breast cancer progression via transforming growth factor beta signaling
- These data indicate that VE-cadherin is a positive and endothelial cell-specific regulator of TGF-beta signalling.
- Describe reproducible flow cytometric endothelial progenitor cell determination in human peripheral blood as CD34+/CD144+/CD3- lymphocyte sub-population.
- ADAM10 is a novel regulator of vascular permeability and demonstrates a hitherto unknown function in the regulation of VE-cadherin-dependent endothelial cell functions and leukocyte transendothelial migration
- Sox-9, ER81 and VE-cadherin have roles in retinoic acid-mediated trans-differentiation of breast cancer cells
- Report a vessel type-specific expression pattern for VE-cadherin in regular human lung tissue, which is not influenced by age or sex.
- VE-cad gap formation is required for leukocyte transmigration and identify p120 as a critical intracellular mediator of this process through its regulation of VE-cad expression at junctions.
- VE-cadherin levels are not directly related to N-cadherin levels but may be inversely related due to competition for cadherin-associated Src substrate p120.
- VE-cadherin function in endothelial cells is intimately linked to vascular integrity and endothelial barrier plasticity.
- Data show that cilengitide activated cell surface alphaVbeta3, stimulated phosphorylation of FAK, Src and VE-cadherin, increased cell permeability and decreased cell adhesion in endothelial cells.