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Ephrin

Ephrin Background

Available Resources for Ephrin Research

Creative BioMart is your ultimate one-stop shop for all your research needs related to Ephrins. Our extensive range of carefully developed products and customized services are designed to help you delve deep into the world of Ephrins and their vital role in various physiological processes.

  • Our product line includes top-quality recombinant proteins, protein pre-coupled magnetic beads, cell and tissue lysates, and others.
  • We also offer a wealth of resources on Ephrins, covering essential topics such as involved pathways, protein functions, interacting proteins, related articles, and research areas.

Our Featured Products

Cat.# Product name Species Source (Host) Tag
EFNA1-2238H Recombinant Human EFNA1, His tagged Human Human Cell His
Efna2-4047M Active Recombinant Mouse Efna2 protein, His-tagged Mouse HEK293 His
EFNA3-3151H Recombinant Human EFNA3, His tagged Human Human Cell His
Efna4-4057M Active Recombinant Mouse Efna4 protein, His-tagged Mouse HEK293 His
EFNA5-700H Active Recombinant Human EFNA5, His tagged Human HEK293 His
EFNB1-2237H Recombinant Human EFNB1 protein, His-tagged Human HEK293 His
EFNB2-3191H Recombinant Human EFNB2, His tagged Human Human Cell His

About Ephrins

Ephrins are a family of cell surface molecules that serve as the primary ligands for Eph receptors. They play important roles in various biological processes, including development, tissue homeostasis, and cell communication. Ephrins are classified into two subclasses: Ephrin-A and Ephrin-B, based on their binding preference for specific Eph receptors.

Structure of Ephrins

Ephrins are glycosylphosphatidylinositol (GPI)-anchored or transmembrane proteins that consist of an extracellular domain, a single transmembrane domain, and a cytoplasmic domain. The extracellular domain contains the binding site for Eph receptors, while the cytoplasmic domain interacts with intracellular signaling molecules to transmit signals upon receptor binding.

Ephrin-A Subclass

Ephrin-A ligands preferentially bind to EphA receptors. They are attached to the cell membrane through a GPI anchor, which allows them to be localized to lipid rafts. Ephrin-A ligands are characterized by a short cytoplasmic domain that lacks intrinsic signaling activity. Instead, their interaction with EphA receptors initiates bidirectional signaling through the receptor.

Ephrin-B Subclass

Ephrin-B ligands, on the other hand, bind to EphB receptors. They are transmembrane proteins with a cytoplasmic domain that contains conserved regions known as PDZ-binding motifs. The cytoplasmic domain of Ephrin-B ligands can interact with PDZ domain-containing proteins, allowing them to transmit signals independently of Eph receptor activation. This enables them to initiate bidirectional signaling upon binding to EphB receptors.

Bidirectional Signaling

The interaction between Ephrins and Eph receptors leads to bidirectional signaling, meaning that both the ligand-expressing cell and the receptor-expressing cell can transmit signals. This bidirectional signaling is crucial for the regulation of cell-cell communication and tissue patterning during development.

Structure of ephrin ligands. Fig.1 Structure of Ephrin Ligands. The GPI anchor and transmembrane domains of ephrin-A and ephrin-B are shown. Both classes have Eph binding domain on the extracellular side. Ephrin-B contains a cytoplasmic domain and a PDZ domain. (Kou CJ, et al., 2018)

Functions of Ephrins

Ephrins are involved in various biological processes, including:

  • Embryonic Development: Ephrins play critical roles in embryonic development, where they are involved in processes such as tissue boundary formation, axon guidance, cell migration, and organogenesis. They provide positional cues that guide migrating cells and regulate tissue morphogenesis.
  • Neuronal Development: Ephrins, particularly Ephrin-B ligands, are essential for proper neuronal development. They regulate axon guidance, synaptic plasticity, and dendritic spine formation. Ephrin-B/EphB signaling contributes to the precise wiring of the nervous system.
  • Angiogenesis: Ephrins and Eph receptors play roles in angiogenesis, the process of blood vessel formation. They regulate endothelial cell migration, sprouting, and vessel remodeling, ensuring proper vascular development and maintenance.
  • Tissue Homeostasis and Regeneration: Ephrins are involved in maintaining tissue homeostasis and regulating cell-cell interactions in adult tissues. They contribute to processes like tissue regeneration, wound healing, and immune cell interactions.
  • Cancer: Dysregulated Ephrin-Eph signaling has been implicated in cancer progression, metastasis, and tumor angiogenesis. Altered expression or function of Ephrins can disrupt cell-cell interactions, promote tumor growth, and contribute to invasive properties of cancer cells.

Understanding the functions and signaling mechanisms of Ephrins provides insights into their roles in development, tissue homeostasis, and disease. The dynamic interplay between Ephrins and Eph receptors regulates diverse cellular processes, and disruptions in this signaling axis are associated with various diseases. Further research aims to unravel the intricate mechanisms of Ephrin signaling and explore their potential as therapeutic targets in different disease contexts.

If you have any questions, requirements, or cooperation intentions, please feel free to contact us. We very much look forward to working with you and helping you achieve research and commercial success.

Eph receptors and ephrin ligands.Fig.2 Eph receptors and ephrin ligands. (Charmsaz S, et al., 2017)

Related References

  1. Kou CJ, Kandpal RP. Differential expression patterns of Ephrins and Ephrin ligands in human cancers. Biomed Res Int. 2018;2018:7390104. Published 2018 Feb 28.
  2. Pasquale EB. Ephrins and ephrins in cancer: bidirectional signalling and beyond. Nat Rev Cancer. 2010;10(3):165-180.
  3. Charmsaz S, Scott AM, Boyd AW. Targeted therapies in hematological malignancies using therapeutic monoclonal antibodies against Eph family receptors. Exp Hematol. 2017;54:31-39.
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