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Validated All-in-One™ qPCR Primer for EPHB4(NM_004444.4) Search again
Product ID:
HQP004945
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CMAVM2, HFASD, HTK, LMPHM7, MYK1, TYRO11
Gene Description:
EPH receptor B4
Target Gene Accession:
NM_004444.4(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:
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| A | B |
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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. |
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Summary
Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins.
Gene References into function
- accelerates differentiation of select human hematopoietic cells
- role of EphB4 receptor in erythropoiesis
- Eph B4 stimulates migration and proliferation and may play a role in angiogenesis
- EphB4 is pro-adhesive and stimulates endothelial cell migration and sprouting angiogenesis. EphrinB2-mediated repulsive signals are transduced by EphB4.
- HoxA9 binds to the EphB4 promoter & stimulates its expression resulting in an increase of endothelial cell migration and tube forming activity. Thus, modulation of EphB4 expression may contribute to the proangiogenic effect of HoxA9 in endothelial cells.
- in hyperinflammatory lesions, ephrinB2 was predominantly expressed in macrophage-like cells and EphB4 in small venules; syntenin and syndecan-1 were up-regulated in EphB4-positive endothelial cells after stimulation with preclustered ephrinB2
- EphB4 and ephrin-B2 molecules, which have specific expression patterns during artery and vein development, respectively, were expressed in the placenta
- These results suggest that activation of EphB4 participates in adhesive but not repulsive signals independently of its tyrosine kinase activity in hematopoietic cells.
- analysis of EphB1, EphB2, and EphB4-binding peptides interaction with antagonists with ephrin-like affinity
- EphB4 protein levels are high in the PC3 prostate cancer cell line and several folds higher in a metastatic clone of PC3 (PC3M) where overexpression was accompanied by EphB4 gene amplification.
- EPHB4 regulates chemokine-evoked trophoblast responses: a mechanism for incorporating the human placenta into the maternal circulation.
- EphB4 is expressed in prostate cancer cell lines with increased expression in human prostate cancers when compared with matched normal tissue
- EphB4 knockdown in an in vivo murine tumor xenograft model led to a nearly 80% reduction in tumor volume associated with reduced tumor proliferation, increased apoptosis and reduced tumor microvasculature
- EphB4 and ephrin-B2 are instrumental in the establishment of a functional placental structure and of the utero-placental circulation.
- EphB4 acts as a negative regulator of blood vessel branching and vascular network formation, switching the vascularization program from sprouting angiogenesis to circumferential vessel growth.
- Overexpression of EphB4 is associated with squamous cell carcinoma of the head and neck
- novel link between EphB forward signaling and SDF-1-induced signaling demonstrates a mechanism for cooperative regulation of endothelial cell movement.
- The results provide critical information on the EphB4*ephrinB2 protein interfaces and their mode of interaction, which will facilitate development of small molecule compounds inhibiting the EphB4*ephrinB2 interaction as novel cancer therapeutics.
- Study provides evidence showing that promoter methylation regulates EPHB4 transcription and that EPHB4 can regulate the long-term clonogenic potential of colorectal tumor cells, revealing EPHB4 as a potential tumor suppressor gene in colorectal cancer.
- demonstrates that Eph B4 and Ephrin B2 interaction may play an important role in the oncogenesis and angiogenesis of cervical carcinomas
- Notch signaling by induction of Dll1 was necessary & sufficient to induce EphB4-dependent branching morphogenesis in human arterial EC.
- Overexpression of EphB4 is associated with ovarian cancer
- activation of EphB4 enhances proangiogenic capacity through induction of PSGL-1 expression and adhesion to E selectin and P selectin
- EphB4 expression was found in 44 (72.1%) out of 61 cancer tissues analysed.
- Overexpression of EphB4 is associated with tumour advancement of ovarian cancers
- EphB4 is a critical component of the CYP2C9- and 11,12-EET-activated signaling cascade that promotes angiogenesis in vitro as well as in vivo.
- EphB4 receptor activation by ephrin B2 in osteoarthritis subchondral bone could affect abnormal metabolism in this tissue by inhibiting resorption factors and their activities