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Product listing: ENPP1 (D37B7) Rabbit mAb, UniProt ID P22413 #5342 to EphB4 (D1C7N) Rabbit mAb, UniProt ID P54760 #14960

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Mitotic control is important for normal growth, development, and maintenance of all eukaryotic cells. Research studies have demonstrated that inappropriate control of mitosis can lead to genomic instability and cancer (reviewed in 1,2). A regulator of mitosis, Greatwall kinase (Gwl), was first identified in Drosophila melanogaster (3). Subsequent studies showed that, based on sequence homology and function, microtubule-associated serine/threonine kinase-like (MASTL) is the human ortholog of Gwl (4). Regulation of MASTL/Gwl activation has been shown to be critical for the correct timing of mitosis. Research studies have shown that Gwl is activated by hyperphosphorylation (5). The phosphorylation of human Gwl at Thr194 and Thr207 by active cyclin B1-cdc2 leads to possible autophosphorylation at Ser875 (Ser883 in Xenopus), which stabilizes the kinase. Activated Gwl phosphorylates α-Endosulfine (ENSA) and cAMP-regulated phosphoprotein 19 (ARPP19) at Ser67 and Ser62, respectively. Phosphorylated ENSA and ARPP19 inhibit the activity of the B55 subunit-associated form of protein phosphatase 2A (PP2A-B55), allowing for complete phosphorylation of mitotic substrates by cyclin B1-cdc2 and mitotic entry. When Gwl is inactivated, PP2A-B55 reactivates, which leads to dephosphorylation of cyclin B1-cdc2 and mitotic exit (5,6, reviewed in 7).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated EOMES (D8D1R) Rabbit mAb #81493.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The T-box family of transcription factors is named for their shared homology with the DNA binding domain of the mouse brachyury (T) gene product. Members of this family bind DNA and are capable of transcriptional activation. They also have evolutionarily conserved expression patterns and roles in embryonic development, primarily mesoderm development (1). EOMES, or Tbr2 (T-box brain 2), is a master regulator of mesoderm formation that is also essential for trophoblast formation, gastrulation, neurogenesis and the differentiation of certain T cell subsets. Embryos from EOMES knock-out mice die soon after implantation due to their inability to develop a trophoblast (2,3). Conditional neural knock out mice show defects in development of a specific population of neural progenators known as Intermediate Progenator Cells (IPCs) that give rise only to neurons (4,5). These cells are formed from the radial glia in the ventricular and sub-ventricular zones of the cortex. Expression of EOMES increases as cells develop from radial glia to IPCs and then decreases as IPCs progress to neurons. Recent evidence suggests that EOMES and IPCs may also play a role neurogenesis in the adult hippocampal SGZ (5). EOMES is also a key transcription factor for memory T cells and for full effector differentiation of CD8+ T cells (6). Expression of EOMES is induced in CD8+ T cells following viral infection and bacterial infection where sufficient IL-12 has been produced to elicit acute host cell response (7).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated EOMES (D8D1R) Rabbit mAb #81493.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The T-box family of transcription factors is named for their shared homology with the DNA binding domain of the mouse brachyury (T) gene product. Members of this family bind DNA and are capable of transcriptional activation. They also have evolutionarily conserved expression patterns and roles in embryonic development, primarily mesoderm development (1). EOMES, or Tbr2 (T-box brain 2), is a master regulator of mesoderm formation that is also essential for trophoblast formation, gastrulation, neurogenesis and the differentiation of certain T cell subsets. Embryos from EOMES knock-out mice die soon after implantation due to their inability to develop a trophoblast (2,3). Conditional neural knock out mice show defects in development of a specific population of neural progenators known as Intermediate Progenator Cells (IPCs) that give rise only to neurons (4,5). These cells are formed from the radial glia in the ventricular and sub-ventricular zones of the cortex. Expression of EOMES increases as cells develop from radial glia to IPCs and then decreases as IPCs progress to neurons. Recent evidence suggests that EOMES and IPCs may also play a role neurogenesis in the adult hippocampal SGZ (5). EOMES is also a key transcription factor for memory T cells and for full effector differentiation of CD8+ T cells (6). Expression of EOMES is induced in CD8+ T cells following viral infection and bacterial infection where sufficient IL-12 has been produced to elicit acute host cell response (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The T-box family of transcription factors is named for their shared homology with the DNA binding domain of the mouse brachyury (T) gene product. Members of this family bind DNA and are capable of transcriptional activation. They also have evolutionarily conserved expression patterns and roles in embryonic development, primarily mesoderm development (1). EOMES, or Tbr2 (T-box brain 2), is a master regulator of mesoderm formation that is also essential for trophoblast formation, gastrulation, neurogenesis and the differentiation of certain T cell subsets. Embryos from EOMES knock-out mice die soon after implantation due to their inability to develop a trophoblast (2,3). Conditional neural knock out mice show defects in development of a specific population of neural progenators known as Intermediate Progenator Cells (IPCs) that give rise only to neurons (4,5). These cells are formed from the radial glia in the ventricular and sub-ventricular zones of the cortex. Expression of EOMES increases as cells develop from radial glia to IPCs and then decreases as IPCs progress to neurons. Recent evidence suggests that EOMES and IPCs may also play a role neurogenesis in the adult hippocampal SGZ (5). EOMES is also a key transcription factor for memory T cells and for full effector differentiation of CD8+ T cells (6). Expression of EOMES is induced in CD8+ T cells following viral infection and bacterial infection where sufficient IL-12 has been produced to elicit acute host cell response (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The T-box family of transcription factors is named for their shared homology with the DNA binding domain of the mouse brachyury (T) gene product. Members of this family bind DNA and are capable of transcriptional activation. They also have evolutionarily conserved expression patterns and roles in embryonic development, primarily mesoderm development (1). EOMES, or Tbr2 (T-box brain 2), is a master regulator of mesoderm formation that is also essential for trophoblast formation, gastrulation, neurogenesis and the differentiation of certain T cell subsets. Embryos from EOMES knock-out mice die soon after implantation due to their inability to develop a trophoblast (2,3). Conditional neural knock out mice show defects in development of a specific population of neural progenators known as Intermediate Progenator Cells (IPCs) that give rise only to neurons (4,5). These cells are formed from the radial glia in the ventricular and sub-ventricular zones of the cortex. Expression of EOMES increases as cells develop from radial glia to IPCs and then decreases as IPCs progress to neurons. Recent evidence suggests that EOMES and IPCs may also play a role neurogenesis in the adult hippocampal SGZ (5). EOMES is also a key transcription factor for memory T cells and for full effector differentiation of CD8+ T cells (6). Expression of EOMES is induced in CD8+ T cells following viral infection and bacterial infection where sufficient IL-12 has been produced to elicit acute host cell response (7).

$260
100 µl
REACTIVITY
Human

Background: The T-box family of transcription factors is named for their shared homology with the DNA binding domain of the mouse brachyury (T) gene product. Members of this family bind DNA and are capable of transcriptional activation. They also have evolutionarily conserved expression patterns and roles in embryonic development, primarily mesoderm development (1). EOMES, or Tbr2 (T-box brain 2), is a master regulator of mesoderm formation that is also essential for trophoblast formation, gastrulation, neurogenesis and the differentiation of certain T cell subsets. Embryos from EOMES knock-out mice die soon after implantation due to their inability to develop a trophoblast (2,3). Conditional neural knock out mice show defects in development of a specific population of neural progenators known as Intermediate Progenator Cells (IPCs) that give rise only to neurons (4,5). These cells are formed from the radial glia in the ventricular and sub-ventricular zones of the cortex. Expression of EOMES increases as cells develop from radial glia to IPCs and then decreases as IPCs progress to neurons. Recent evidence suggests that EOMES and IPCs may also play a role neurogenesis in the adult hippocampal SGZ (5). EOMES is also a key transcription factor for memory T cells and for full effector differentiation of CD8+ T cells (6). Expression of EOMES is induced in CD8+ T cells following viral infection and bacterial infection where sufficient IL-12 has been produced to elicit acute host cell response (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: EPAC1 and EPAC2 (exchange proteins activated by cyclic AMP) are guanine nucleotide exchange factors (GEFs) that catalyze the exchange of GDP for GTP, activating Rap1 and Rap2 small GTPases. Rap activation by EPAC is cAMP-dependent and mediates cAMP signaling in part through protein kinase A (PKA) (reviewed in 1). EPAC signaling plays a significant role in a number of cellular processes including migration and focal adhesion formation (2), exocytosis (3), insulin signaling (4), axon growth and guidance (5) and neurotransmitter release (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (D4K8R) XP® Rabbit mAb #36746.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin), Western Blotting

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Pacific Blue™ fluorescent dye and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EpCAM (VU1D9) Mouse mAb #2929.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Epithelial cell adhesion and activating molecule (EpCAM/CD326) is a transmembrane glycoprotein that mediates Ca2+-independent, homophilic adhesions on the basolateral surface of most epithelial cells. EpCAM is not expressed in adult squamous epithelium, but it is highly expressed in adeno and squamous cell carcinomas (1). Research studies identified EpCAM as one of the first tumor-associated antigens, and it has long been a marker of epithelial and tumor tissue. Investigators have shown that EpCAM is highly expressed in cancer cells (reviewed in 2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: 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. While 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).The EphA1 receptor preferentially binds ephrin-A1 as a ligand (6). This ligand-receptor interaction stimulates EphA1 signaling and regulates cell morphology and motility through the ILK-RhoA-ROCK pathway (7). The EphA1 gene has been associated with late-onset Alzheimer's diseases (8,9). The role of EphA1 in cancer development falls into two opposite categories. In some type of cancer such as prostate, gastric and liver cancer, high expression of EphA1 associates with cancer metastasis and invasion (10-12). For other types of cancers, such as colon cancer and nonmelanoma skin cancer, down-regulation of the protein correlates with cancer development (13,14). The bidirectional signaling modulation of Ephrin-Ephrin receptor interaction might contribute this paradox phenomena (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: 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).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: 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. While 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).The EphA3 receptor preferentially binds ephrin-A5. This ligand-receptor interaction stimulates EphA3 signaling, regulates cell adhesion and migration, and induces cellular morphologic responses (6-8). EphA3 plays a critical role in callosal axon guidance (9), retinotectal mapping of neurons (10), as well as cardiac cell migration and differentiation (11). Investigators have shown that somatic mutations in functional domains of EphA3 are linked to lung cancer progression (12). In addition, EphA3 expression levels have been correlated with tumor angiogenesis and progression in gastric and colorectal carcinoma (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: 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. While 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).The EphA7 receptor preferentially binds ephrin-A5 as a ligand. This ligand-receptor interaction stimulates EphA7 signaling and induces apoptotic cell death through TNFR1 and caspase-8 pathway (6,7). EphA7 plays a critical role in organ development during neural tube closure, cortical dendritic development and spine maturation as well as urine tract insertion (8-10). Secreted EphA7 has been shown to promote somatic cell reprogramming through ERK activity reduction (11). Silencing of the secreted form of EphA7 is associated with germinal center B cell lymhomas. The secreted form of EphA7 has been proposed as a soluble tumor suppresor in lymphoma (12-14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: 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).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The ephrin receptor B2 (EphB2) is an ephrin family receptor tyrosine kinase that plays an important role in regulating growth and development of multiple tissues and organs (1,2). The EphB2 transmembrane receptor protein contains a kinase domain, a PDZ motif, and a SAM domain within a conserved cytoplasmic domain. A ligand binding domain, a cysteine-rich domain, and fibronectin type III repeats comprise the conserved EphB2 extracellular domain (3). EphB2 binds with high affinity to ephrin B ligands, and to some ephrin A proteins, to initiate bidirectional signaling between neighboring cells (1,2). Upon binding, EphB2-Ephrin B2 dimers form a heterotetramer and position the receptor-ligand complex on the cell membrane to facilitate bidirectional signal transduction (3). In addition to associating with ephrin ligands, EphB2 also regulates a number of biological processes through interaction with focal adhesion kinase (FAK), NMDA receptor (NMDAR), the Rac1 guanine nucleotide exchange factor Tiam1, and p21-activated kinase (PAK1) (4-7). While some studies support a role for EphB2 as a pro-oncogenic kinase, other research suggests that EphB2 acts as a tumor suppressor (1,2,4,8).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: 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).