EFNB2 Human
Description
Introduction
EFNB2 (Ephrin-B2) is a transmembrane protein encoded by the EFNB2 gene in humans, belonging to the ephrin-B subclass of ligands for receptor tyrosine kinases (EPH receptors). It plays critical roles in developmental processes, cell-cell communication, and disease mechanisms, including cancer, viral entry, and cardiovascular regulation . This article synthesizes structural, functional, and clinical insights into EFNB2, supported by diverse research findings.
Protein Characteristics
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Protein Structure: Comprises 226 amino acids with a C-terminal His-tag in recombinant forms. The molecular weight ranges from 35–40 kDa due to glycosylation .
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Domains:
Biological Roles
EFNB2 mediates bidirectional signaling via interactions with EPH receptors (e.g., EPHB4, EPHA3) :
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Developmental Regulation: Axon guidance, vascular patterning, and neural crest migration .
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Cell-Cell Interaction: Modulates adhesion, migration, and tissue boundary formation .
Table 1: EFNB2 Expression and Cancer Prognosis
Key Findings:
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In neuroblastoma, high EFNB2 combined with TrkA improves survival prediction accuracy (HR = 0.20, P < 0.0005) .
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EFNB2 loss in glioblastoma stem cells (GSCs) blocks anchorage-independent proliferation (G2/M arrest) .
Cardiovascular Regulation
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Blood Pressure: EFNB2 knockout mice exhibit reduced blood pressure. Five SNPs in EFNB2’s 3′ region are linked to hypertension in males (OR = 0.241, P < 0.0005) .
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Vascular Smooth Muscle Cells (VSMCs): Reverse signaling via EFNB2’s intracellular tail (aa 313–331) regulates contractility .
Viral Pathogenesis
EFNB2 serves as a receptor for zoonotic viruses:
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Hendra and Nipah Viruses: Binds viral glycoproteins, enabling pH-independent cell entry .
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African Henipaviruses: Despite low sequence identity (~30%) with Asian strains, GhV-G retains conserved ephrinB2-binding motifs .
Targeted Therapies
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EphB4/EFNB2 Signaling Blockade: Soluble EphB4 extracellular domain inhibits angiogenesis and tumor growth .
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Antibody-Based Inhibition: Anti-EFNB2 antibodies reduce glioblastoma progression in xenografts .
Engineered EFNB2 Variants
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Viral Neutralization: A triple mutant (D62Q + E63K + K128R) enhances specificity for Nipah virus glycoprotein (IC₅₀: 1.2 nM) .
Table 2: Key Genetic Variants in EFNB2
| SNP ID | Association | Population | Effect Size (OR) | P-Value |
|---|---|---|---|---|
| rs10133272 | Hypertension (male) | T2D cohort | 0.32 | 1.2 × 10⁻⁴ |
| rs12869254 | Hypertension (male) | T2D cohort | 0.29 | 3.8 × 10⁻⁵ |
Product Specs
Product Science Overview
Ephrin-B2 is a transmembrane protein that binds to Eph receptors on adjacent cells, leading to bidirectional signaling. This signaling can be divided into two types:
- Forward signaling: Initiated by the Eph receptor.
- Reverse signaling: Initiated by the ephrin ligand.
Ephrin-B2 binds promiscuously to several Eph receptors, including EPHA4, EPHA3, and EPHB4. This interaction is essential for cell migration, repulsion, and adhesion, which are critical for the proper formation of tissues and organs .
Ephrin-B2 plays a pivotal role in the development of the cardiovascular system. It is involved in heart morphogenesis and the regulation of cell adhesion and migration. Ephrin-B2, along with its receptor EPHB4, is crucial for angiogenesis, the process by which new blood vessels form from pre-existing vessels. This process is vital for supplying oxygen and nutrients to tissues during development and in response to injury .
Recombinant human Ephrin-B2 is a laboratory-produced version of the protein, often used in research to study its functions and interactions. It is typically expressed in HEK 293 cells and purified to high levels of purity, making it suitable for various applications such as SDS-PAGE, ELISA, and Western blotting .
Recombinant human Ephrin-B2 is used in various research applications to understand its role in development and disease. It is particularly valuable in studying cardiovascular diseases, cancer progression, and neurodegenerative diseases. By understanding how Ephrin-B2 interacts with its receptors and other cellular components, researchers can develop potential therapeutic strategies for these conditions .
