Detects human EphB4 in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant human EphA1, A2, A5, A6, A10, B2, B3, B6, recombinant mouse EphA3, A4, or recombinant rat EphB1 is observed.
Monoclonal Rat IgG1 Clone # 395810
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human EphB4 Ala16-Ala539 Accession # AAH52804
Supplied in a saline solution containing BSA and Sodium Azide.
Detection of EphB4 in MCF‑7 Human Cell Line by Flow Cytometry.
MCF‑7 human breast cancer cell line was stained with Rat Anti-Human EphB4 Fluorescein‑conjugated Monoclonal Antibody (Catalog # FAB3038F, filled histogram) or isotype control antibody (Catalog # IC005F, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
EphB4, also known as Htk, Myk1, Tyro11, and Mdk2, is a member of the Eph receptor tyrosine kinase family and binds Ephrin-B2. The A and B class Eph proteins have a common structural organization (1‑4). The human EphB4 cDNA encodes a 987 amino acid precursor that includes a 15 amino acid (aa) signal sequence, a 524 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 427 aa cytoplasmic domain (5). The ECD contains an N-terminal globular domain, a cysteine‑rich domain, and two fibronectin type III domains. The cytoplasmic domain contains a juxtamembrane motif with two tyrosine residues which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) (5). Activation of kinase activity occurs after membrane-bound or clustered ligand recognition and binding. The ECD of human EphB4 shares 89% aa sequence identity with mouse EphB4 and 42‑45% aa sequence identity with human EphB1, 2, and 3. EphB4 is expressed preferentially on venous endothelial cells (EC) and inhibits cell-cell adhesion, chemotaxis, and angiogenesis. Opposing effects are induced by signaling through Ephrin-B2 expressed on arterial EC: adhesion, endothelial cell migration, and vessel sprouting (6). EphB4 singaling contributes to new vascularization by guiding venous EC away from Ephrin-B2 expressing EC. Ephrin-B2 signaling induces arterial EC to migrate towards nascent EphB4 expressing vessels (6). The combination of forward signaling through EphB4 and reverse signaling through Ephrin-B2 promotes in vivo mammary tumor growth and tumor‑associated angiogenesis (7). EphB4 promotes the differentiation of megakaryocytic and erythroid progenitors but not granulocytic or monocytic progenitors (8, 9).
Poliakov, A. et al. (2004) Dev. Cell 7:465.
Surawska, H. et al. (2004) Cytokine Growth Factor Rev. 15:419.
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