EFNB2 Antibody

$138.92$232.63

SKU: 57957 Categories: ,

Description

Aliases

EPH-related receptor tyrosine kinase ligand 5, LERK-5, HTK ligand, HTK-L, EFNB2, EPLG5, HTKL, LERK5

Antibody Type

Polyclonal Antibody

Species

Human

Uniprot ID

P52799

Immunogen

Recombinant human Ephrin-B2 protein (28-229AA)

Raised In

Rabbit

Species Reactivity

Human

Tested Applications

ELISA, IHC;Recommended dilution:IHC:1:20-1:200

Background / Function

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. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons.

Isotype

IgG

Conjugate

Unconjugated

Storage Buffer

PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Form

Liquid

Storage

Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze.

Purity

Antigen Affinity Purified

Literature

[1]Structural characterization of the EphA4-Ephrin-B2 complex reveals new features enabling Eph-ephrin binding promiscuity.”Qin H., Noberini R., Huan X., Shi J., Pasquale E.B., Song J.J. Biol. Chem. 285:644-654(2010). [2]Structural plasticity of EPH receptor A4 facilitates cross-class ephrin signaling.”Bowden T.A., Aricescu A.R., Nettleship J.E., Siebold C., Rahman-Huq N., Owens R.J., Stuart D.I., Jones E.Y.Structure 17:1386-1397(2009). [3]Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2.”Bowden T.A., Aricescu A.R., Gilbert R.J., Grimes J.M., Jones E.Y., Stuart D.I.Nat. Struct. Mol. Biol. 15:567-572(2008).

Additional information

Size

50μl, 100μl

Certificate of Analysis