ephrin receptor

Ephrin-A4 is a member of the ephrin ligand family which binds members of the Eph receptor family. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor binding domain. Ephrin-A4 consists of approximately 125 amino acids and includes four invariant cysteines, It has been shown to bind EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1. Ephrin-A4 binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. It may play a role in the interaction between activated B-lymphocytes and dendritic cells in tonsils.

EphA4 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 60-80 KDa and the accession number is P54764.

Ephrin-A1 is a member of the A-type ephrin family of cell surface proteins that function as ligands for the A-type Eph receptor tyrosine kinase family. Ephrin-A1 can be induced by TNF and IL1B. Its expression levels can be down-regulated in primary glioma tissues compared to the normal tissues. The soluble monomeric form is expressed in the glioblastoma multiforme (GBM) and breast cancer cells. Soluble Ephrin-A1 is necessary for the transformation of HeLa and SK-BR3 cells and participates in the relocalization of EPHA2 away from sites of cell-cell contact during transformation. Ephrin-A1 plays an important role in angiogenesis and tumor neovascularization.

Ephrins-A3 belongs the Ephrins ligand family which involved in a variety of biological processes, especially in the nervous system and in erythropoiesis. It is shown that Ephrin-A3 is expressed in brain, skeletal muscle, spleen, thymus, prostate, testis, ovary, small intestine, and peripheral blood leukocytes. Ephrin-A3 has a GPI anchor following the extracellular sequence and a signal sequence of 22 amino acids. Ephrin-A3 can bind EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, EphA8 and EphB1. Futhermore, it is associated with tumor growth and metastasis.

Ephrin-B2 is a single-pass type I membrane protein and it contains 1 ephrin RBD (ephrin receptor-binding) domain. Ephrin-B2 belongs to the ephrin (EPH) family and it is cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. The ephrins and EPH-related receptors contain the largest subfamily of receptor protein-tyrosine kinases and have been associated with mediating developmental events, particularly in the nervous system and in erythropoiesis. Based upon their structures and sequence relationships, ephrins are allocated 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. It also binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4 and together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration.

Ephrin Type-B Receptor 1 (EPHB1) is a single-pass type I membrane protein that belongs to the Ephrin-B family of receptor tyrosine kinases that is involved in embryonic nervous and vascular system development. EPHB1/EPHT2 contains two fibronectin type-III domains, one protein kinase domain and one SAM (sterile α motif) domain. EPHB1 could stimulate fibroblast motility on extracellular matrix in a kinase-dependent manner, which also correlated with its association with Grb7, an adaptor molecule implicated in the regulation of cell migration. It binds to ephrin-B1, ephrin-B2 and ephrin-B3. EPHB1 plays an important roles in diverse biological processes including nervous system development, angiogenesis, and neural synapsis formation and maturation and may be involved in cell-cell interactions in the nervous system.

Ephrin type-A receptor 2 (EPHA2) is a receptor tyrosine kinase (RTK), whose over-expression has been observed in a variety of cancers, including breast cancer. EPHA2 expression may be causally related to tumorigenesis; therefore, it is important to understand how EPHA2 gene (EPHA2) expression is regulated. EPhA2 Protein, Cynomolgus, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 59.2 kDa and the accession number is Q1KL86.

Ephrin type-A receptor 2 (EPHA2) is a receptor tyrosine kinase (RTK), whose over-expression has been observed in a variety of cancers, including breast cancer. EPHA2 expression may be causally related to tumorigenesis; therefore, it is important to understand how EPHA2 gene (EPHA2) expression is regulated. EPhA2 Protein, Cynomolgus, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-hFc tag. The predicted molecular weight is 83.1 kDa and the accession number is Q1KL86.

Ephrin type-B receptor 2(EPHB2) belongs to the protein kinase superfamily and Ephrin receptor subfamily. EPHB2 contains 1 Eph LBD domain, 2 fibronectin type-III domains, 1 protein kinase domain and 1 SAM domain. 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. The Eph family of 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. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family.

Mouse Ephrin-B1 is a single-pass type I membrane protein which belongs to the ephrin family. It contains an ephrin RBD (ephrin receptor-binding) domain, and expressed in heart, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ephrin-B1 is cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. It binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. It may play a role in cell adhesion and function in the development or maintenance of the nervous system.

EphA4 Protein, Human, Recombinant (hFc) is expressed in HEK293 mammalian cells with C-Fc tag. The predicted molecular weight is 90-120 KDa and the accession number is P54764.

EphA8, also known as Hek3 and Eek, is a 120 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases. The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. Eph-Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. Receptor tyrosine kinase which binds promiscuously GPI-anchored ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The GPI-anchored ephrin-A EFNA2, EFNA3, and EFNA5 are able to activate EPHA8 through phosphorylation. With EFNA5 may regulate integrin-mediated cell adhesion and migration on fibronectin substrate but also neurite outgrowth. During development of the nervous system plays also a role in axon guidance. Downstream effectors of the EPHA8 signaling pathway include FYN which promotes cell adhesion upon activation by EPHA8 and the MAP kinases in the stimulation of neurite outgrowth.

The aim of the present study was to evaluate ephrin type-A receptor 5 (EphA5) expression and its clinicopathological significance in gastric cancer. Gastric cancer tissues were analyzed by immunohistochemistry. The association between EphA5 expression and clinicopathological parameters, human epidermal growth factor receptor 2 (HER2) status and Ki-67 proliferation index was statistically analyzed.

EphB2, a receptor tyrosine kinase for ephrin ligands, is overexpressed in various cancers and plays an important role in tumor progression. EPHB2 promotes endothelial-mesenchymal transition (EMT) and elicits associated pathologic characteristics of glioblastoma multiforme (GBM) such as invasion and migration. EPHB2 is epigenetically overexpressed in hypoxia, a condition highly prevalent in malignancy. Furthermore, HIF-2α is required for EPHB2 stabilization by hypoxia.

Ephrin type-A receptor 5 (EphA5) expression was detected in all non-tumor gastric epithelia but was differentially expressed among gastric cancer samples. EphA5 is differentially expressed in gastric cancer. EphA5 may therefore be a potential therapeutic target and may have clinical utility as a marker for lymph node metastasis in gastric cancer. EPHA5 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 61.73 kDa and the accession number is A0A2K5W6J6.

Ephrin type-A receptor 5 (EphA5) expression was detected in all non-tumor gastric epithelia but was differentially expressed among gastric cancer samples. EphA5 is differentially expressed in gastric cancer. EphA5 may therefore be a potential therapeutic target and may have clinical utility as a marker for lymph node metastasis in gastric cancer. EPHA5 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 61.9 kDa and the accession number is P54756-1.

Ephrin-B2 controls platelet-derived growth factor receptor β (PDGFRβ) distribution in the VSMC plasma membrane, endocytosis, and signaling in a fashion that is highly distinct from its role in the endothelium. Ephrin-B2 is an important regulator of PDGFRβ endocytosis and thereby acts as a molecular switch controlling the downstream signaling activity of this receptor in mural cells.

Ephrin-A1 is a cell membrane protein and contains 1 ephrin RBD (ephrin receptor-binding) domain. EFNA1 belongs to the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. 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. This gene encodes an EFNA class ephrin which binds to the EPHA2, EPHA4, EPHA5, EPHA6, and EPHA7 receptors. Two transcript variants that encode different isoforms were identified through sequence analysis.It belongs to the ephrin family and contains 1 ephrin RBD (ephrin receptor-binding) domain.