Ephrin-B2/EFNB2 Protein, Human (HEK293, His-Fc)

Ephrin-B2/EFNB2 is a key transmembrane ligand of Eph receptors that coordinates migration, repulsion, and adhesion in developing neurons, blood vessels, and epithelia. It induces bidirectional signaling, binding to EPHA4, EPHA3 and EPHB4, which is critical for cardiac morphogenesis and angiogenesis. Ephrin-B2/EFNB2 Protein, Human (HEK293, His-Fc) is the recombinant human-derived Ephrin-B2/EFNB2 protein, expressed by HEK293 , with C-hFc, C-His labeled tag. The total length of Ephrin-B2/EFNB2 Protein, Human (HEK293, His-Fc) is 202 a.a., with molecular weight of ~62 kDa.

Ephrin-B2, also recognized as EFNB2, emerges as a pivotal cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases critical in orchestrating migration, repulsion, and adhesion during neuronal, vascular, and epithelial development. Displaying a propensity to bind promiscuously to Eph receptors on adjacent cells, Ephrin-B2 instigates contact-dependent bidirectional signaling, delineated into forward signaling downstream of the receptor and reverse signaling downstream of the ephrin ligand. Its binding affinity extends to receptor tyrosine kinases, including EPHA4, EPHA3, and EPHB4, with the latter forming a crucial partnership in heart morphogenesis and angiogenesis, governing cell adhesion and migration. In EPHB4-mediated forward signaling, Ephrin-B2 regulates cellular repulsion and segregation from EFNB2-expressing cells, potentially influencing the orientation of longitudinally projecting axons. Notably, Ephrin-B2 assumes a unique role as a receptor for Hendra virus and Nipah virus during microbial infection, adding an intriguing facet to its multifaceted functions.

Human

HEK293

C-hFc;C-His

P52799 (I28-A229)

1948  [NCBI]

MAVRRDSVWKYCWGVLMVLCRTAISKSIVLEPIYWNSSNSKFLPGQGLVLYPQIGDKLDIICPKVDSKTVGQYEYYKVYMVDKDQADRCTIKKENTPLLNCAKPDQDIKFTIKFQEFSPNLWGLEFQKNKDYYIISTSNGSLEGLDNQEGGVCQTRAMKILMKVGQDASSAGSTRNKDPTRRPELEAGTNGRSSTTSPFVKPNPGSSTDGNSAGHSGNNILGSEVALFA

Approximately 62 kDa

Greater than 95% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.