epha2 expression  (Cell Signaling Technology Inc)

 
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    Name:
    EphA2 Antibody
    Description:
    The Eph receptors are the largest known family of receptor tyrosine kinases RTKs They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands EphA receptors bind to a glycosylphosphatidylinositol anchored ephrin A ligand EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain 1 2 Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer 3 Both ephrin A and B ligands have dual functions As RTK ligands ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor expressing cells The ephrin extracellular domain is sufficient for this function as long as it is clustered 4 The second function of ephrins has been described as reverse signaling whereby the cytoplasmic domain becomes tyrosine phosphorylated allowing interactions with other proteins that may activate signaling pathways in the ligand expressing cells 5 Various stimuli can induce tyrosine phosphorylation of ephrin B including binding to EphB receptors activation of Src kinase and stimulation by PDGF and FGF 6 Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo 7 EphA2 is overexpressed in various tumor cells and it has been suggested that EphA2 may promote malignancy However several studies demonstrate that EphA2 plays an important role in tumor suppression 8 The role of EphA2 in tumor development may depend upon regulation of its tyrosine kinase activity
    Catalog Number:
    3974
    Price:
    None
    Applications:
    Western Blot
    Category:
    Primary Antibodies
    Source:
    Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr930 of human EphA2. Antibodies are purified by protein A and peptide affinity chromatography.
    Reactivity:
    Human
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    Structured Review

    Cell Signaling Technology Inc epha2 expression
    <t>EphA2</t> dimerization induced by the monomeric ephrinA1 ligand. a MSE vs. oligomer order for EphA2 wild-type and the L223R/L254R/V255R and G131Y mutants in the presence of 200 nM m-ephrinA1. The MSEs are all minimized for n = 2, indicating dimerization. b Comparison of EphA2 dimerization propensity in the presence and absence of m-ephrinA1 shows that m-ephrinA1 significantly enhances EphA2 dimerization. c Dimerization curves in the presence of m-ephrinA1 show that the dimerization propensity of EphA2 wild-type and the L223R/L254R/V255R mutant are the same, while the G131Y mutant has a reduced dimerization propensity, indicating the involvement of the dimerization interface. d A representative Western blot showing Y772 phosphorylation of EphA2 wild-type and the indicated mutants following a 15 min stimulation with m-ephrinA1 and FBS. e Quantification of Y772 phosphorylation from three to four independent measurements is shown as solid circles. The bars represent the averages and the standard errors. EphA2 wild-type and the L223R/L254R/V255R mutant exhibit similar levels of Y772 phosphorylation while the G131Y mutant shows significantly lower phosphorylation (** p
    The Eph receptors are the largest known family of receptor tyrosine kinases RTKs They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands EphA receptors bind to a glycosylphosphatidylinositol anchored ephrin A ligand EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain 1 2 Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer 3 Both ephrin A and B ligands have dual functions As RTK ligands ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor expressing cells The ephrin extracellular domain is sufficient for this function as long as it is clustered 4 The second function of ephrins has been described as reverse signaling whereby the cytoplasmic domain becomes tyrosine phosphorylated allowing interactions with other proteins that may activate signaling pathways in the ligand expressing cells 5 Various stimuli can induce tyrosine phosphorylation of ephrin B including binding to EphB receptors activation of Src kinase and stimulation by PDGF and FGF 6 Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo 7 EphA2 is overexpressed in various tumor cells and it has been suggested that EphA2 may promote malignancy However several studies demonstrate that EphA2 plays an important role in tumor suppression 8 The role of EphA2 in tumor development may depend upon regulation of its tyrosine kinase activity
    https://www.bioz.com/result/epha2 expression/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    epha2 expression - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures"

    Article Title: The EphA2 receptor is activated through induction of distinct, ligand-dependent oligomeric structures

    Journal: Communications Biology

    doi: 10.1038/s42003-018-0017-7

    EphA2 dimerization induced by the monomeric ephrinA1 ligand. a MSE vs. oligomer order for EphA2 wild-type and the L223R/L254R/V255R and G131Y mutants in the presence of 200 nM m-ephrinA1. The MSEs are all minimized for n = 2, indicating dimerization. b Comparison of EphA2 dimerization propensity in the presence and absence of m-ephrinA1 shows that m-ephrinA1 significantly enhances EphA2 dimerization. c Dimerization curves in the presence of m-ephrinA1 show that the dimerization propensity of EphA2 wild-type and the L223R/L254R/V255R mutant are the same, while the G131Y mutant has a reduced dimerization propensity, indicating the involvement of the dimerization interface. d A representative Western blot showing Y772 phosphorylation of EphA2 wild-type and the indicated mutants following a 15 min stimulation with m-ephrinA1 and FBS. e Quantification of Y772 phosphorylation from three to four independent measurements is shown as solid circles. The bars represent the averages and the standard errors. EphA2 wild-type and the L223R/L254R/V255R mutant exhibit similar levels of Y772 phosphorylation while the G131Y mutant shows significantly lower phosphorylation (** p
    Figure Legend Snippet: EphA2 dimerization induced by the monomeric ephrinA1 ligand. a MSE vs. oligomer order for EphA2 wild-type and the L223R/L254R/V255R and G131Y mutants in the presence of 200 nM m-ephrinA1. The MSEs are all minimized for n = 2, indicating dimerization. b Comparison of EphA2 dimerization propensity in the presence and absence of m-ephrinA1 shows that m-ephrinA1 significantly enhances EphA2 dimerization. c Dimerization curves in the presence of m-ephrinA1 show that the dimerization propensity of EphA2 wild-type and the L223R/L254R/V255R mutant are the same, while the G131Y mutant has a reduced dimerization propensity, indicating the involvement of the dimerization interface. d A representative Western blot showing Y772 phosphorylation of EphA2 wild-type and the indicated mutants following a 15 min stimulation with m-ephrinA1 and FBS. e Quantification of Y772 phosphorylation from three to four independent measurements is shown as solid circles. The bars represent the averages and the standard errors. EphA2 wild-type and the L223R/L254R/V255R mutant exhibit similar levels of Y772 phosphorylation while the G131Y mutant shows significantly lower phosphorylation (** p

    Techniques Used: Mutagenesis, Western Blot

    Cartoon representation of the findings: EphA2 can associate into two types of dimers as well as clusters, depending of the nature of the activating ligand. TK tyrosine kinase, FP fluorescent protein
    Figure Legend Snippet: Cartoon representation of the findings: EphA2 can associate into two types of dimers as well as clusters, depending of the nature of the activating ligand. TK tyrosine kinase, FP fluorescent protein

    Techniques Used:

    Effect of the R103E mutation on EphA2 dimerization in the presence of monomeric ephrinA1 ligand. a MSE vs. oligomer order for the EphA2 R103E mutant in the presence of m-ephrinA1. The MSE is miminized for n = 2, indicating dimerization. b Dimerization propensity of the EphA2 R103E mutant in the absence and in the presence of m-ephrinA1. The ligand slightly enhances dimerization, indicating that the EphA2 R103E mutation does not completely abrogate m-ephrinA1 binding. c Dimerization curves for EphA2 wild-type and the R103E mutant in the presence of m-ephrinA1. The R103E mutation decreases the stability of the dimers, most likely because it severely impairs m-ephrinA1 binding
    Figure Legend Snippet: Effect of the R103E mutation on EphA2 dimerization in the presence of monomeric ephrinA1 ligand. a MSE vs. oligomer order for the EphA2 R103E mutant in the presence of m-ephrinA1. The MSE is miminized for n = 2, indicating dimerization. b Dimerization propensity of the EphA2 R103E mutant in the absence and in the presence of m-ephrinA1. The ligand slightly enhances dimerization, indicating that the EphA2 R103E mutation does not completely abrogate m-ephrinA1 binding. c Dimerization curves for EphA2 wild-type and the R103E mutant in the presence of m-ephrinA1. The R103E mutation decreases the stability of the dimers, most likely because it severely impairs m-ephrinA1 binding

    Techniques Used: Mutagenesis, Binding Assay

    EphA2 dimerization in the presence of the monomeric YSA peptide ligand. a MSE vs. oligomer order for EphA2 wild-type and the L223R/L254R/V255R, G131Y, and R103E mutants. In all cases, the MSE minimum occurs at n = 2, indicating dimerization. b Dimerization curves show that the dimerization propensity of EphA2 wild-type and the G131Y mutant are the same, while the L223R/L254R/V255R mutant has reduced dimerization propensity. Data for the wild-type and the L223R/L254R/V255R mutant are from ref. 30 . c Dimerization curves for EphA2 wild-type and the R103E mutant show that the mutant has reduced dimerization propensity
    Figure Legend Snippet: EphA2 dimerization in the presence of the monomeric YSA peptide ligand. a MSE vs. oligomer order for EphA2 wild-type and the L223R/L254R/V255R, G131Y, and R103E mutants. In all cases, the MSE minimum occurs at n = 2, indicating dimerization. b Dimerization curves show that the dimerization propensity of EphA2 wild-type and the G131Y mutant are the same, while the L223R/L254R/V255R mutant has reduced dimerization propensity. Data for the wild-type and the L223R/L254R/V255R mutant are from ref. 30 . c Dimerization curves for EphA2 wild-type and the R103E mutant show that the mutant has reduced dimerization propensity

    Techniques Used: Mutagenesis

    Dimeric ephrinA1-Fc induces EphA2 receptor clustering. a Portion of a HEK293T cell expressing EphA2-mTurq and EphA2-eYFP in hypo-osmotic medium, imaged when mTurq was excited. A plasma membrane region of homogeneous fluorescence, a few µm in length (yellow box), is analyzed to determine the EphA2-mTurq concentration, the EphA2-eYFP concentration and the FRET efficiency, as described in the Materials and methods. The scale bar is 5 μm. b FRET efficiency vs. acceptor (EphA2-eYFP) concentration. Each data point corresponds to one plasma membrane region. c Donor (EphA2-mTurq) concentration vs. acceptor (EphA2-eYFP) concentration in the selected membrane regions. In b and c , 275 cells were imaged in four independent experiments, yielding 858 data points. d Mean square error (MSE) vs. oligomer order. MSE is minimized for n > 4, indicating the presence of oligomers that are larger than dimers (i.e., clusters). e Clustered EphA2 receptor fraction as a function of total EphA2 concentration. The data were binned and the averages are shown along with the standard errors. The solid line represents the theoretical best fit to the data. f Mean FRET efficiencies vs. mean acceptor fractions, determined as shown in Supplementary Figure 1 . The plot is based on more than 1000 data points. The dependence deviates from a linear function, supporting the conclusion that exposure to ephrinA1-Fc induces preferentially the formation of EphA2 clusters
    Figure Legend Snippet: Dimeric ephrinA1-Fc induces EphA2 receptor clustering. a Portion of a HEK293T cell expressing EphA2-mTurq and EphA2-eYFP in hypo-osmotic medium, imaged when mTurq was excited. A plasma membrane region of homogeneous fluorescence, a few µm in length (yellow box), is analyzed to determine the EphA2-mTurq concentration, the EphA2-eYFP concentration and the FRET efficiency, as described in the Materials and methods. The scale bar is 5 μm. b FRET efficiency vs. acceptor (EphA2-eYFP) concentration. Each data point corresponds to one plasma membrane region. c Donor (EphA2-mTurq) concentration vs. acceptor (EphA2-eYFP) concentration in the selected membrane regions. In b and c , 275 cells were imaged in four independent experiments, yielding 858 data points. d Mean square error (MSE) vs. oligomer order. MSE is minimized for n > 4, indicating the presence of oligomers that are larger than dimers (i.e., clusters). e Clustered EphA2 receptor fraction as a function of total EphA2 concentration. The data were binned and the averages are shown along with the standard errors. The solid line represents the theoretical best fit to the data. f Mean FRET efficiencies vs. mean acceptor fractions, determined as shown in Supplementary Figure 1 . The plot is based on more than 1000 data points. The dependence deviates from a linear function, supporting the conclusion that exposure to ephrinA1-Fc induces preferentially the formation of EphA2 clusters

    Techniques Used: Expressing, Fluorescence, Concentration Assay

    Interfaces involved in EphA2 receptor clustering induced by ephrinA1-Fc. a Crystal structure showing a lateral view of four EphA2 extracellular regions (gray) bound to four ephrinA1 molecules (light blue; PDB ID: 3MX0). The receptor tetramer is stabilized via two interfaces: the “clustering” interface (approximately outlined in orange), which includes contacts mediated by L223, L254, and V255 in the cysteine-rich domain, and the dimerization interface (approximately outlined in wine), which includes contacts mediated by G131 in the ligand-binding domain 18 . b Comparison of raw FRET data for EphA2 wild-type and the L223R/L254R/V255R mutant in the presence of ephrinA1-Fc. In this experiment, 275 cells were imaged in four independent experiments to obtain 858 data points for the wild-type, and 196 cells were imaged in four independent experiments to obtain 563 data points for the L223R/L254R/V255R mutant. c Comparison of raw FRET data for EphA2 wild-type and the G131Y mutant in the presence of ephrinA1-Fc. A total of 618 cells were imaged in six independent experiments to yield 2310 data points for the G131Y mutant. d MSE vs. oligomer order for the L223R/L254R/V255R and G131Y mutants in the presence of ephrinA1-Fc. The MSE minimum for the L223R/L254R/V255R mutant occurs at n = 6. The MSE for the G131Y mutant is the same for n ≥ 2. As previously shown 21 , these results indicate that the EphA2 receptor is preferentially assembled into clusters, although the presence of some dimers cannot be excluded. e Representation of the clustered fractions for EphA2 wild-type and the L223R/L254R/V255R and G131Y mutants as a function of total receptor concentration shows that mutation of both interfaces decreases the fraction of clustered EphA2
    Figure Legend Snippet: Interfaces involved in EphA2 receptor clustering induced by ephrinA1-Fc. a Crystal structure showing a lateral view of four EphA2 extracellular regions (gray) bound to four ephrinA1 molecules (light blue; PDB ID: 3MX0). The receptor tetramer is stabilized via two interfaces: the “clustering” interface (approximately outlined in orange), which includes contacts mediated by L223, L254, and V255 in the cysteine-rich domain, and the dimerization interface (approximately outlined in wine), which includes contacts mediated by G131 in the ligand-binding domain 18 . b Comparison of raw FRET data for EphA2 wild-type and the L223R/L254R/V255R mutant in the presence of ephrinA1-Fc. In this experiment, 275 cells were imaged in four independent experiments to obtain 858 data points for the wild-type, and 196 cells were imaged in four independent experiments to obtain 563 data points for the L223R/L254R/V255R mutant. c Comparison of raw FRET data for EphA2 wild-type and the G131Y mutant in the presence of ephrinA1-Fc. A total of 618 cells were imaged in six independent experiments to yield 2310 data points for the G131Y mutant. d MSE vs. oligomer order for the L223R/L254R/V255R and G131Y mutants in the presence of ephrinA1-Fc. The MSE minimum for the L223R/L254R/V255R mutant occurs at n = 6. The MSE for the G131Y mutant is the same for n ≥ 2. As previously shown 21 , these results indicate that the EphA2 receptor is preferentially assembled into clusters, although the presence of some dimers cannot be excluded. e Representation of the clustered fractions for EphA2 wild-type and the L223R/L254R/V255R and G131Y mutants as a function of total receptor concentration shows that mutation of both interfaces decreases the fraction of clustered EphA2

    Techniques Used: Ligand Binding Assay, Mutagenesis, Concentration Assay

    Dimerization of EphA2 wild-type and the L223R/L254R/V255R, G131Y and R103E mutants in the absence of ligand binding. a MSE vs. oligomer order for EphA2 wild-type and the three mutants. MSE is minimized at n = 2 for all, indicating the presence of dimers. b Dimerization curves for EphA2 wild-type and the L223R/L254R/V255R and G131E mutants. The L223R/L254R/V255R mutations reduce dimerization, while the G131Y mutation has no effect. Thus, the unliganded dimer is stabilized through the “clustering interface”. c Dimerization curves for EphA2 wild-type and the R103E mutant. The R103E mutant exhibits a reduced dimerization propensity, despite the fact that this residue is not part of the clustering interface. d A representative Western blot comparing Y772 phosphorylation for EphA2 wild-type and the G131Y mutant. e Quantification from three independent experiments (shown as solid circles) shows no statistically significant difference ( p > 0.05 from Student’s t -test). f A representative Western blot image comparing S897 phosphorylation for EphA2 wild-type and the G131Y mutant. g Quantification from four independent experiments (shown as solid circles) shows no statistically significant difference ( p > 0.05 from Student’s t -test). h Representative Western blot images comparing Y772 phosphorylation for EphA2 wild-type and the R103E mutant. i Quantification from three independent experiments (shown as solid circles) shows that the R103E mutant has lower Y772 phosphorylation than EphA2 wild-type (*** p
    Figure Legend Snippet: Dimerization of EphA2 wild-type and the L223R/L254R/V255R, G131Y and R103E mutants in the absence of ligand binding. a MSE vs. oligomer order for EphA2 wild-type and the three mutants. MSE is minimized at n = 2 for all, indicating the presence of dimers. b Dimerization curves for EphA2 wild-type and the L223R/L254R/V255R and G131E mutants. The L223R/L254R/V255R mutations reduce dimerization, while the G131Y mutation has no effect. Thus, the unliganded dimer is stabilized through the “clustering interface”. c Dimerization curves for EphA2 wild-type and the R103E mutant. The R103E mutant exhibits a reduced dimerization propensity, despite the fact that this residue is not part of the clustering interface. d A representative Western blot comparing Y772 phosphorylation for EphA2 wild-type and the G131Y mutant. e Quantification from three independent experiments (shown as solid circles) shows no statistically significant difference ( p > 0.05 from Student’s t -test). f A representative Western blot image comparing S897 phosphorylation for EphA2 wild-type and the G131Y mutant. g Quantification from four independent experiments (shown as solid circles) shows no statistically significant difference ( p > 0.05 from Student’s t -test). h Representative Western blot images comparing Y772 phosphorylation for EphA2 wild-type and the R103E mutant. i Quantification from three independent experiments (shown as solid circles) shows that the R103E mutant has lower Y772 phosphorylation than EphA2 wild-type (*** p

    Techniques Used: Ligand Binding Assay, Mutagenesis, Western Blot

    Effect of the R103E mutation on EphA2 clustering induced by ephrinA1-Fc. a , b Side and top views of a crystal structure of four EphA2 molecules (gray) bound to four ephrinA1 molecules (light blue; PDB ID: 3MX0). The position of the R103E mutation in two of the EphA2 molecules is shown in magenta, and indicated by an arrow in one. c Comparison of raw FRET data for EphA2 wild-type and the R103E mutant in the presence of ephrinA1-Fc. 275 cells were imaged in four independent experiments to obtain 858 data points for the wild type. A total of 201 cells were imaged in three independent experiments to obtain 474 data points for R03E mutant. d MSE vs. oligomer order for EphA2 R103E in the presence of ephrinA1-Fc. The MSE value is the same for all n ≥ 2, indicating oligomerization with predominance of clusters. e Comparison of EphA2 wild-type and R103E mutant clustered fractions in the presence of saturating concentration of ephrinA1-Fc shows that the R103E mutation severely destabilizes the clusters
    Figure Legend Snippet: Effect of the R103E mutation on EphA2 clustering induced by ephrinA1-Fc. a , b Side and top views of a crystal structure of four EphA2 molecules (gray) bound to four ephrinA1 molecules (light blue; PDB ID: 3MX0). The position of the R103E mutation in two of the EphA2 molecules is shown in magenta, and indicated by an arrow in one. c Comparison of raw FRET data for EphA2 wild-type and the R103E mutant in the presence of ephrinA1-Fc. 275 cells were imaged in four independent experiments to obtain 858 data points for the wild type. A total of 201 cells were imaged in three independent experiments to obtain 474 data points for R03E mutant. d MSE vs. oligomer order for EphA2 R103E in the presence of ephrinA1-Fc. The MSE value is the same for all n ≥ 2, indicating oligomerization with predominance of clusters. e Comparison of EphA2 wild-type and R103E mutant clustered fractions in the presence of saturating concentration of ephrinA1-Fc shows that the R103E mutation severely destabilizes the clusters

    Techniques Used: Mutagenesis, Concentration Assay

    Related Articles

    FLAG-tag:

    Article Title: Generation and characterization of a single-chain anti-EphA2 antibody
    Article Snippet: .. Binding of anti-EphA2 scFv anti-bodies to overexpressed EphA2 and EphA7 receptors was detected by rabbit anti-DYKDDDDK (FLAG) Tag Antibody (#2368, Cell Signaling Technologies Inc., Danvers, MA) in non-permeabilized cells. .. As controls, commercial rabbit anti-EphA2 and rat anti-EphA7 (Santa Cruz Biotechnology Inc., Dallas TX) were used in similar manner.

    other:

    Article Title: The dystroglycan receptor maintains glioma stem cells in the vascular niche
    Article Snippet: IF analysis showed a significant overlap in the membrane of EphA2, EphA3 and αDG in the four primary GBM cell lines tested (Fig. a).

    Expressing:

    Article Title: A Small Peptide Promotes EphA2 Kinase-Dependent Signaling by Stabilizing EphA2 Dimers
    Article Snippet: .. Total EphA2 expression, Ser897 phosphorylation and Tyr772 phosphorylation were probed using anti-EphA2 antibodies (Cell Signalling, MA), anti-phospho-Ser897 antibodies (Cell Signaling, MA), and anti-phospho-Tyr772 antibodies (Cell Signaling, MA), respectively. .. Anti-rabbit HRP conjugated antibodies (Promega) were used as secondary antibodies to visualize the EphA2 expression and phosphorylation bands.

    Article Title: The dystroglycan receptor maintains glioma stem cells in the vascular niche
    Article Snippet: .. Results show strong overlapping expression of αDG with EphA2, EphA3, CD49f (integrin α6), CD133 and CD15 (Fig. c). .. We repeated this analysis using both Amnis and standard flow cytometry using the panel of GBM cell lines (n = 4).

    Western Blot:

    Article Title: Claudin-4 controls the receptor tyrosine kinase EphA2 pro-oncogenic switch through β-catenin
    Article Snippet: .. The eluates were assessed by Western blot analysis using pan anti-phosphotyrosine antibody (R & D Systems, Minneapolis, MN) and anti-EphA2 antibody (Cell Signaling Technology). .. Biotinylation of plasma membrane proteins Assay of cell surface levels of EphA2 in the 2008/SCB, CLDN4KD, HEY/mc and HEY/mc-CLDN4 was performed using the Cell Surface Protein Isolation kit (Thermo Scientific; Rockford, IL).

    Binding Assay:

    Article Title: Generation and characterization of a single-chain anti-EphA2 antibody
    Article Snippet: .. Binding of anti-EphA2 scFv anti-bodies to overexpressed EphA2 and EphA7 receptors was detected by rabbit anti-DYKDDDDK (FLAG) Tag Antibody (#2368, Cell Signaling Technologies Inc., Danvers, MA) in non-permeabilized cells. .. As controls, commercial rabbit anti-EphA2 and rat anti-EphA7 (Santa Cruz Biotechnology Inc., Dallas TX) were used in similar manner.

    SDS Page:

    Article Title: EphA2 is an epithelial cell pattern recognition receptor for fungal β-glucans
    Article Snippet: .. The lysates were separated by SDS/PAGE, and the phosphorylated proteins were detected by immunoblotting with phospho-specific antibodies, including anti-phospho-EphA2 (Cell signaling; #6347), anti-phospho-Stat3 (Cell signaling; #9134), anti-phospho-c-Fos (Cell signaling; #5348), anti-phospho-MEK1/2 (Cell signaling; #9154), anti-phospho-p65 (Cell signaling; # 3033). .. The blots were then stripped, and total protein levels and β-actin were detected by immunoblotting with appropriate antibodies against EphA2 (Cell signaling; #6997), EphB2 (Cell signaling; #83029), EphA4 (Santa Cruz; sc-365503), Stat3 (Cell signaling; # 12640), c-Fos (Cell signaling; # 4384), MEK1/2 (Cell signaling; # 9122), p65 (Cell signaling; # 8242), and β-actin (Cell signaling # 3700).

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  • 99
    Cell Signaling Technology Inc epha2
    The expression and inverse correlation of miR-302b and <t>EphA2</t> in gastric cancer tissues.A and B.qRT-PCR was used to detect the expression of miR-302b(A) and EphA2(B) in 125 gastric carcinoma tissues and the adjacent non-cancerous tissues. (C) Pearson's correlation analysis was employed to evaluate the correlation between the expression of miR-302b and EphA2. ** P
    Epha2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/epha2/product/Cell Signaling Technology Inc
    Average 99 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    epha2 - by Bioz Stars, 2020-09
    99/100 stars
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    99
    Cell Signaling Technology Inc anti epha2 antibodies
    The YSA peptide promotes dimerization of the <t>EphA2</t> L223R/L254R/V255R mutant ) (B) Comparison of the dimerization curves for YSA-bound EphA2 wild-type and mutant.
    Anti Epha2 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti epha2 antibodies/product/Cell Signaling Technology Inc
    Average 99 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    anti epha2 antibodies - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

    Image Search Results


    The expression and inverse correlation of miR-302b and EphA2 in gastric cancer tissues.A and B.qRT-PCR was used to detect the expression of miR-302b(A) and EphA2(B) in 125 gastric carcinoma tissues and the adjacent non-cancerous tissues. (C) Pearson's correlation analysis was employed to evaluate the correlation between the expression of miR-302b and EphA2. ** P

    Journal: Journal of Cancer

    Article Title: The relationship between miR-302b and EphA2 and their clinical significance in gastric cancer

    doi: 10.7150/jca.25235

    Figure Lengend Snippet: The expression and inverse correlation of miR-302b and EphA2 in gastric cancer tissues.A and B.qRT-PCR was used to detect the expression of miR-302b(A) and EphA2(B) in 125 gastric carcinoma tissues and the adjacent non-cancerous tissues. (C) Pearson's correlation analysis was employed to evaluate the correlation between the expression of miR-302b and EphA2. ** P

    Article Snippet: Primary antibodies for EphA2 (#6997, diluted 1: 1000), and GAPD-H (#2118, diluted 1:1000) were purchased from Cell Signaling technology MA, USA.

    Techniques: Expressing, Quantitative RT-PCR

    The YSA peptide promotes dimerization of the EphA2 L223R/L254R/V255R mutant ) (B) Comparison of the dimerization curves for YSA-bound EphA2 wild-type and mutant.

    Journal: Biochimica et biophysica acta

    Article Title: A Small Peptide Promotes EphA2 Kinase-Dependent Signaling by Stabilizing EphA2 Dimers

    doi: 10.1016/j.bbagen.2016.06.004

    Figure Lengend Snippet: The YSA peptide promotes dimerization of the EphA2 L223R/L254R/V255R mutant ) (B) Comparison of the dimerization curves for YSA-bound EphA2 wild-type and mutant.

    Article Snippet: Total EphA2 expression, Ser897 phosphorylation and Tyr772 phosphorylation were probed using anti-EphA2 antibodies (Cell Signalling, MA), anti-phospho-Ser897 antibodies (Cell Signaling, MA), and anti-phospho-Tyr772 antibodies (Cell Signaling, MA), respectively.

    Techniques: Mutagenesis

    YSA binding increases EphA2 Tyr772 phosphorylation and reduces Ser897 phosphorylation Top: Representative Western blots. Bottom: Quantification from three independent experiments. Shown are means and standard errors. *, p

    Journal: Biochimica et biophysica acta

    Article Title: A Small Peptide Promotes EphA2 Kinase-Dependent Signaling by Stabilizing EphA2 Dimers

    doi: 10.1016/j.bbagen.2016.06.004

    Figure Lengend Snippet: YSA binding increases EphA2 Tyr772 phosphorylation and reduces Ser897 phosphorylation Top: Representative Western blots. Bottom: Quantification from three independent experiments. Shown are means and standard errors. *, p

    Article Snippet: Total EphA2 expression, Ser897 phosphorylation and Tyr772 phosphorylation were probed using anti-EphA2 antibodies (Cell Signalling, MA), anti-phospho-Ser897 antibodies (Cell Signaling, MA), and anti-phospho-Tyr772 antibodies (Cell Signaling, MA), respectively.

    Techniques: Binding Assay, Western Blot

    Elevated Dystroglycan Correlates with GBM Patient Outcome and αDG is Abundantly Glycosylated in GBM. a DAG1 expression was correlated with GBM patient survival using the Rembrandt ( n = 523) and TCGA ( n = 453) databases. b QPCR analysis of DAG1, ITGA6, EPHA2 and EPHA3 mRNA expression in GBM tissue specimens ( n = 28). c Flow cytometric analysis for αDG glycosylation (IIH6 mAb) was performed on primary GBM cell lines grown as serum-free GNS cultures, compared to isotype control. See also Online Research 1d for full analysis. d αDG glycosylation was assessed by western blot in four primary GBM cell lines. e αDG glycosylation was assessed by western blot following cell fractionation to compare cytoplasmic versus membrane localisation. β-actin was used as a loading control. f Flow cytometric analysis was performed for αDG glycosylation (IIH6 mAb) and EphA3 (IIIA4 mAb) in 10 early passage primary GBM cultures, mean channel fluorescence (mcf) was used to determine the correlation coefficient between EphA3 and glycosylated αDG ( r = 0.899). GBM subtypes: MES mesenchymal, PN proneural, CL classical

    Journal: Acta Neuropathologica

    Article Title: The dystroglycan receptor maintains glioma stem cells in the vascular niche

    doi: 10.1007/s00401-019-02069-x

    Figure Lengend Snippet: Elevated Dystroglycan Correlates with GBM Patient Outcome and αDG is Abundantly Glycosylated in GBM. a DAG1 expression was correlated with GBM patient survival using the Rembrandt ( n = 523) and TCGA ( n = 453) databases. b QPCR analysis of DAG1, ITGA6, EPHA2 and EPHA3 mRNA expression in GBM tissue specimens ( n = 28). c Flow cytometric analysis for αDG glycosylation (IIH6 mAb) was performed on primary GBM cell lines grown as serum-free GNS cultures, compared to isotype control. See also Online Research 1d for full analysis. d αDG glycosylation was assessed by western blot in four primary GBM cell lines. e αDG glycosylation was assessed by western blot following cell fractionation to compare cytoplasmic versus membrane localisation. β-actin was used as a loading control. f Flow cytometric analysis was performed for αDG glycosylation (IIH6 mAb) and EphA3 (IIIA4 mAb) in 10 early passage primary GBM cultures, mean channel fluorescence (mcf) was used to determine the correlation coefficient between EphA3 and glycosylated αDG ( r = 0.899). GBM subtypes: MES mesenchymal, PN proneural, CL classical

    Article Snippet: IF analysis showed a significant overlap in the membrane of EphA2, EphA3 and αDG in the four primary GBM cell lines tested (Fig. a).

    Techniques: Expressing, Real-time Polymerase Chain Reaction, Flow Cytometry, Western Blot, Cell Fractionation, Fluorescence

    Glycosylated αDG is expressed in the vascular niche and discretely on Mesenchymal-like glioma tissue. a H E section of a Gliosarcoma (GS) patient specimen showing characteristic biphasic gliomatous (glial-like) and sarcomatous (mesenchymal-like) tumour elements. b IHC analysis of a GS specimen to identify the mesenchymal-like, vimentin + , tumour element. c IHC analysis of sequential (#1–6) GS tissue sections was performed to assess expression patterns of EphA2, EphA3, αDG, βDG, CD31 and GFAP. d IF dual staining of a GBM specimen showing localisation of αDG expression (IIH6—green) surrounding (CD31 + —red) tumour blood vessels, nuclei DAPI—blue). See also Online Resource 2 for additional IHC and IF analysis in GBM tissue specimens

    Journal: Acta Neuropathologica

    Article Title: The dystroglycan receptor maintains glioma stem cells in the vascular niche

    doi: 10.1007/s00401-019-02069-x

    Figure Lengend Snippet: Glycosylated αDG is expressed in the vascular niche and discretely on Mesenchymal-like glioma tissue. a H E section of a Gliosarcoma (GS) patient specimen showing characteristic biphasic gliomatous (glial-like) and sarcomatous (mesenchymal-like) tumour elements. b IHC analysis of a GS specimen to identify the mesenchymal-like, vimentin + , tumour element. c IHC analysis of sequential (#1–6) GS tissue sections was performed to assess expression patterns of EphA2, EphA3, αDG, βDG, CD31 and GFAP. d IF dual staining of a GBM specimen showing localisation of αDG expression (IIH6—green) surrounding (CD31 + —red) tumour blood vessels, nuclei DAPI—blue). See also Online Resource 2 for additional IHC and IF analysis in GBM tissue specimens

    Article Snippet: IF analysis showed a significant overlap in the membrane of EphA2, EphA3 and αDG in the four primary GBM cell lines tested (Fig. a).

    Techniques: Immunohistochemistry, Expressing, Staining

    αDG Interacts with EphA2 and EphA3 Receptors and is Expressed on GSCs. a IF staining was performed to compare membrane localisation of glycosylated αDG (IIH6 mAb—red), compared to either EphA2 (1F7 mAb—green) or EphA3 (IIIA4 mAb—green), in four primary GBM cultures. b Immunoprecipitation (IP) for EphA3 was performed from 1 mg of lysate from four early passage primary GBM cultures to compare membrane association of EphA2, EphA3 and glycosylated αDG. Protein G only was used as a control. c Amnis flow cytometric analysis was performed on a dissociated GBM patient tissue specimen ( n = 1) to assess membrane localisation of glycosylated αDG, with known GSC markers (CD15, CD133, CD49f, EphA2 and EphA3). d Amnis analysis and flow cytometry was performed on primary GBM cultures to assess membrane localisation of glycosylated αDG, with known GSC markers. e αDG high versus αDG low populations were isolated from WK1 cells using FACS and cell morphology and sphere number assessed 7 days post-sort (* p

    Journal: Acta Neuropathologica

    Article Title: The dystroglycan receptor maintains glioma stem cells in the vascular niche

    doi: 10.1007/s00401-019-02069-x

    Figure Lengend Snippet: αDG Interacts with EphA2 and EphA3 Receptors and is Expressed on GSCs. a IF staining was performed to compare membrane localisation of glycosylated αDG (IIH6 mAb—red), compared to either EphA2 (1F7 mAb—green) or EphA3 (IIIA4 mAb—green), in four primary GBM cultures. b Immunoprecipitation (IP) for EphA3 was performed from 1 mg of lysate from four early passage primary GBM cultures to compare membrane association of EphA2, EphA3 and glycosylated αDG. Protein G only was used as a control. c Amnis flow cytometric analysis was performed on a dissociated GBM patient tissue specimen ( n = 1) to assess membrane localisation of glycosylated αDG, with known GSC markers (CD15, CD133, CD49f, EphA2 and EphA3). d Amnis analysis and flow cytometry was performed on primary GBM cultures to assess membrane localisation of glycosylated αDG, with known GSC markers. e αDG high versus αDG low populations were isolated from WK1 cells using FACS and cell morphology and sphere number assessed 7 days post-sort (* p

    Article Snippet: IF analysis showed a significant overlap in the membrane of EphA2, EphA3 and αDG in the four primary GBM cell lines tested (Fig. a).

    Techniques: Staining, Immunoprecipitation, Flow Cytometry, Cytometry, Isolation, FACS