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Human EFNB2/Ephrin-B2  Antibody

All EFNB2 Reagents

EFNB2/Ephrin-B2
Reactivity: Human  
Application: ELISA  
10881-T16-50
10881-T16-200
10881-T16-100
50 µg 
200 µg 
100 µg 
Add to Cart
    Reactivity: Human  
    Application: ELISA  
    10881-RP01-400
    10881-RP01-200
    10881-RP01-100
    400 µg 
    200 µg 
    100 µg 
    Add to Cart
      10881-H08HL-300 
      10881-H03HL-300 
      10881-HCCHL-300 

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        EFNB2/Ephrin-B2 Related Protein, Antibody, cDNA Gene, and ELISA Kits

        EFNB2/Ephrin-B2 Related Protein, Antibody, cDNA Gene, and ELISA Kits

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        EFNB2/Ephrin-B2 Summary & Protein Information

        EFNB2/Ephrin-B2 Related Information

        EFNB2/Ephrin-B2 Background

        Gene Summary: This gene encodes a member of 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 EFNB class ephrin which binds to the EPHB4 and EPHA3 receptors.
        General information above from NCBI
        Subunit structure: Interacts with PDZRN3 (By similarity). Binds to the receptor tyrosine kinases EPHA4, EPHB4 and EPHA3. Binds to Hendra virus and Nipah virus G protein. {ECO:0000250, ECO:0000269|PubMed:16007075, ECO:0000269|PubMed:16477309, ECO:0000269|PubMed:16867992, ECO:0000269|PubMed:19836338, ECO:0000269|PubMed:19875447}.
        Subcellular location: Membrane; Single-pass type I membrane protein.
        Tissue specificity: Lung and kidney.
        Post-translational: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. {ECO:0000250}.
        Sequence similarity: Belongs to the ephrin family. {ECO:0000255|PROSITE-ProRule:PRU00884}.; Contains 1 ephrin RBD (ephrin receptor-binding) domain. {ECO:0000255|PROSITE-ProRule:PRU00884}.
        General information above from UniProt

        EphrinB2 also known as EFNB2 is a member of the ephrin family. EphrinB2 is involved in establishing arterial versus venous identity and perhaps in anastamosing arterial and venous vessels at their junctions. The transmembrane-associated ephrin ligands and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. Eph receptors and ephrins are divided into two subclasses, A and B, based on binding specificities. Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. An exception is the EphA4 receptor, which binds both subclasses of ephrins. EphrinB2 expression progressively extends from the arterial endothelium to surrounding smooth muscle cells and to pericytes, suggesting that ephrin-B2 may play an important role during formation of the arterial muscle wall.

        EFNB2/Ephrin-B2 Alternative Name

        EFNB2/Ephrin-B2 Related Studies

      • Wang HU, et al. (1998) Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell. 93(5): 741-53.
      • Gale NW, et al. (2001) Ephrin-B2 selectively marks arterial vessels and neovascularization sites in the adult, with expression in both endothelial and smooth-muscle cells. Dev Biol. 230(2): 151-60.
      • Shin D, et al. (2001) Expression of ephrinB2 identifies a stable genetic difference between arterial and venous vascular smooth muscle as well as endothelial cells, and marks subsets of microvessels at sites of adult neovascularization. Dev Biol. 230(2): 139-50.
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