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Validated All-in-One™ qPCR Primer for EPHA2(NM_004431.4) Search again
Product ID:
HQP004657
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ARCC2, CTPA, CTPP1, CTRCT6, ECK
Gene Description:
EPH receptor A2
Target Gene Accession:
NM_004431.4(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
This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands. [provided by RefSeq].
Gene References into function
- estrogen and Myc negatively regulate EphA2 expression in mammary epithelial cells
- negative regulation by Cbl
- EphA2 receptor tyrosine kinase is a substrate for low molecular weight tyrosine phosphatase and has a role in neoplastic transformation progression
- a peptide has been identified which has ephrin-like activity in that it stimulates EphA2 tyrosine phosphorylation and signaling
- Eph A receptors inhibit tumor angiogenesis and progression in vivo.
- We demonstrate that tyrosine phosphorylated EphA2 interacts with the PTB and SH2 domains of SHC. We show that the interaction of EphA2 with GRB2 is mediated by SHC and that this complex is necessary for EphA2-mediated activation of ERK kinases.
- Patients with EphA2 overexpression have a poorer prognosis than those without.
- Blockade of EphA2 activation inhibits vascular endothelial growth factor-induced angiogenesis.
- c-Cbl-dependent EphA2 protein degradation is induced by ligand binding.
- Levels predict lung cancer (NSCLC) recurrence and survival.
- Recent studies have demonstrated that the EphA2 receptor tyrosine kinase is frequently overexpressed and functionally altered in aggressive tumor cells, and that these changes promote metastatic character
- differentially regulated in normal and malignant cells.
- Overexpression of EphA2 decreases estrogen dependence. EphA2-transfected cells show increased growth in vitro & larger & more aggressive tumors in vivo. Overexpression decreases tamoxifen's ability to inhibit breast cancer cell growth & tumorigenesis.
- EphA2/ephrin-A3 interactions may play a role in the localization and network of Langerhans cells in the epithelium and in the regulation of their trafficking.
- EphA2 increases as prostatic epithelial cells have more aggressive phenotype. EphA2 functions as a powerful oncogene. Presence of high levels of EphA2 suggests opportunities for prostate cancer prevention and treatment.
- EphA2 is a tumor rejection antigen. Two immunogenic HLA-A*0201 restricted peptides identified by reverse immunology approach.
- EphA2 and E-cadherin may play an important role in tumor metastasis in colorectal cancer
- involvement of EPHA2 in colon carcinogenesis, mainly in stages I and II, and probably through their effect on microvessel induction.
- found the prototype ephrin-A1 receptor, EphA2, localized in several placental cell types
- We show that EphA2 overexpression induces a FAK-dependent increase in MMP-2 expression and invasiveness.
- EPHA2 may have a role in progression of ovarian cancer
- EphA2 selectively inhibits cell-cell adhesions by increasing cell attachment and up-regulating the extracellular matrix protein fibronectin
- Renal medullary EphA2 expression may represent an adaptive response to medullary hypertonicity or urea exposure
- EPHA2 and EFNA1 expression may influence the behavior of human gastric cancer.
- EphA2 may have a role in progression of surgically treated renal cell carcinoma
- low molecular weight protein-tyrosine phosphatase acts as terminator of EphA2 signaling causing efficient negative feedback loop on biological response mediated by ephrinA1; tyrosine phosphorylation main event orchestrating repulsive response
- EphA2 attenuates the growth factor-induced activation of Ras and a negative feedback loop is created that regulates Ras activity.
- receptor phosphorylation and kinase activity of the EphA2 receptor, at least in part, contribute to tumor malignancy
- EphA2 moderates the function of tight junctions via phosphorylation of claudin-4
- High expression of EphA2 is associated with urinary bladder carcinoma.
- VE-cadherin and EphA2 act in a coordinated manner as a key regulatory element in the process of melanoma vasculogenic mimicry.
- increased levels of ephrins A1 and A5 in the presence of high expression of Ephs A1 and A2 lead to a more aggressive ovarian cancer phenotype
- p53 appears to regulate EphA2 expression and clinical outcome in ovarian cancer.
- Our findings show that p53 is a transcriptional regulator of ECK in mediating apoptosis. The discovery of the novel p53-binding motif in the promoter may lead to the identification of a new class of p53 target genes.
- EphA2 was overexpressed in 76% of tumors and was associated with advanced-stage disease and high-grade histology.
- Ephrin-A1 serves as a critical negative regulator in the tumorigenesis of gliomas by down-regulating EphA2 and FAK.
- Ligand activation of EphA2 and EphA2 knockdown by small interfering RNA inhibit EGF-induced cell motility of EGFR-overexpressing human cancer cells, indicating a functional role of EphA2 in EGFR-expressing cancer cells.
- EphA2 may be a new biomarker for astrocytic tumors and may also affect the proliferation and apoptosis of tumor cells and be an attractive therapy target for astrocytic tumors.
- Increasing ephrin-A expression enhances T-cell interactions not only with purified integrin ligands but also endothelial cells, while EphA activation down-regulates these interactions.
- Required for Raf-induced AKT inhibition and cell cycle arrest.
- EphA2 cooperates with ErbB2 to promote tumor progression in mice and may provide a novel therapeutic target for ErbB2-dependent tumors in humans.
- this study define the expression pattern of EphA2 in both primary and recurrent glioblastoma and suggest an important role of EphA2 in the pathogenesis of GBM.
- IL-13R alpha 2, EphA2, and Fra-1 are attractive therapeutic targets representing molecular denominators of high-grade astrocytomas. One hundred percent of GBM tumors overexpress at least one of these proteins.
- overexpression of a wild-type EPHA2, but not a signaling-defective cytoplasmic truncation mutant (DeltaC), in human mammary epithelial cells weakens E-cadherin-mediated cell-cell adhesion
- EphA2 might be involved in the early development of HNSCC although not directly responsible for its progression
- EphA2 promotes tumor growth by enhancing cell-ECM adhesion, increasing anchorage-independent growth and promoting angiogenesis
- EphA2 and EphrinA-1 may play an important role in the development of a subset of early cervical cancers
- overexpression of HuR as found in many progressive tumors could be causative for disarranged Eph receptor to ephrin ligand ratios leading to a higher degree of tissue invasiveness
- NMR and ITC (isothermal titration calorimetry) studies on the Sam domain of Ship2 revealing its three-dimensional structure and its possible mode of interaction with the Sam domain from the EphA2 receptor
- EPHA2, which functions in the Eph-ephrin bidirectional signaling pathway of mammalian cells, plays a vital role in maintaining lens transparency.
- The function of EphA2 and ephrinA1 in tumorigenesis and tumor progression is complex and seems to be dependent on cell type and microenvironment