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Ephrin B2 Protein (EFNB2) (Soluble) (His tag)

EFNB2 Origine: Humain Hôte: Escherichia coli (E. coli) Recombinant > 95 % by SDS-PAGE
N° du produit ABIN7539313
  • Antigène Voir toutes Ephrin B2 (EFNB2) Protéines
    Ephrin B2 (EFNB2)
    Type de proteíne
    Recombinant
    Attributs du protein
    Soluble
    Origine
    • 10
    • 6
    • 1
    Humain
    Source
    • 6
    • 4
    • 4
    • 2
    • 1
    Escherichia coli (E. coli)
    Purification/Conjugué
    Cette Ephrin B2 protéine est marqué à la His tag.
    Fonction
    Ephrin-B2, soluble
    Séquence
    MIVLEPIYWN SSNSKFLPGQ GLVLYPQIGD KLDIICPKVD SKTVGQYEYY KVYMVDKDQA DRCTIKKENT PLLNCAKPDQ DIKFTIKFQE FSPNLWGLEF QKNKDYYIIS TSNGSLEGLD NQEGGVCQTR AMKILMKVGQ DASSAGSTRN KDPTRRPELE AGTNGRSSTT SPFVKPNPGS STDGNSAGHS GNNILGSEVA LFALEHHHHH H
    Attributs du produit
    Length (aa):211
    Pureté
    > 95 % by SDS-PAGE
    Top Product
    Discover our top product EFNB2 Protéine
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
  • Antigène
    Ephrin B2 (EFNB2)
    Autre désignation
    Ephrin-B2 (EFNB2 Produits)
    Synonymes
    EFNB2 Protein, efnb2 Protein, ephrin-B2 Protein, htkl Protein, eplg5 Protein, htk-l Protein, lerk5 Protein, ephrinB2 Protein, efnb2a Protein, MGC68890 Protein, efnb2b Protein, ELF-2 Protein, Epl5 Protein, Eplg5 Protein, Htk-L Protein, LERK-5 Protein, Lerk5 Protein, NLERK-1 Protein, EPLG5 Protein, HTKL Protein, LERK5 Protein, ephrin B2 Protein, ephrin-B2 precursor Protein, ephrin B2 L homeolog Protein, ephrin B2 S homeolog Protein, EFNB2 Protein, efnb2 Protein, efnb2.L Protein, efnb2.S Protein, Efnb2 Protein
    Sujet
    EPH-related receptor tyrosine kinase ligand 5, HTK ligand,The large families of Eph receptor tyrosine kinases and their Ephrin ligands transduce signals in a cell-cell contact-dependent fashion. They thereby coordinate the growth, differentiation, and patterning of almost every organ and tissue. Eph/Ephrin interactions can trigger a wide array of cellular responses, including cell adhesion, boundary formation, and repulsion. The exact mechanisms leading to this diversity of responses are unclear but appear to involve differential signaling, proteolytic cleavage of Ephrins, and endocytosis of the ligand-receptor complex. In the developing cardiovascular system, Eph and Ephrin molecules control the angiogenic remodeling of blood vessels and lymphatic vessels and play essential roles in endothelial cells as well as in supporting pericytes and vascular smooth muscle cells. Recent evidence suggests that Ephs and Ephrins may also be involved in pathological angiogenesis, in particular, the neovascularization of tumors. Consequently, the expression, interactions, or signaling of Eph/Ephrin molecules might be targets for future therapeutic approaches. Ephrins are naturally divided into two structural groups. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor-binding domain. This conserved sequence consists of approximately 125 amino acids and includes four invariant cysteines. The B-class ligands are transmembrane proteins, which can be tyrosine phosphorylated upon receptor ligation. Class B ephrins show 33 % amino acid sequence identity in their extracellular segments and 44 % amino acid sequence identity in their cytoplasmic regions.
    Poids moléculaire
    23.4 kDa
    ID gène
    1948
    NCBI Accession
    NM_004093, NP_004084
    UniProt
    P52799
    Pathways
    Signalisation RTK, Regulation of Muscle Cell Differentiation
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