Recombinant Proteins
Product List
EFNA1 Human
Ephrin A1 Human Recombinant
EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
EFNA1 Human, HEK
Ephrin A1 Human Recombinant, HEK
EFNA1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 19-182) containing 170 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 20.2kDa (calculated).
HEK293 cells.
EFNA1 Human, Sf9
Ephrin A1 Human Recombinant, Sf9
EFNA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (19-182a.a.) and having a molecular mass of 46.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
EFNA1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
EFNA3 Human
Ephrin A3 Human Recombinant
EFNA3 Human, Sf9
Ephrin A3 Human Recombinant, Sf9
EFNA3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (23-214aa) and having a molecular mass of 48.7kDa
EFNA3 is fused to a 242 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
EFNA5 Human
Ephrin A5 Human Recombinant
EFNA5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 422 amino acids (21-203 a.a.) and having a molecular mass of 48.1kDa. EFNA5 is expressed with a 239 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
EFNA5 Human, Active
Ephrin A5 Human Recombinant, Active
EFNA5 Human Recombinant is a single, glycosylated, polypeptide chain (21-203 a.a) containing a total of 422 amino acids and having a molecular mass of 48.1 kDa.
EFNA5 is fused to a 239 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.
EFNB1 Human
Ephrin-B1 Human Recombinant
The EFNB1 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
EFNB1 Human, Sf9
Ephrin-B1 Human Recombinant, Sf9
EFNB1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 452 amino acids (28-237a.a.) and having a molecular mass of 50.3kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).
EFNB1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Sf9, Baculovirus cells.
EFNB2 Human
Ephrin- B2 Human Recombinant
EFNB2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
Ephrins, also known as Eph receptor-interacting proteins, are a family of proteins that serve as ligands for the Eph receptor, the largest known subfamily of receptor protein-tyrosine kinases (RTKs) . Ephrins are divided into two subclasses based on their structure and linkage to the cell membrane: ephrin-A and ephrin-B. Ephrin-As are anchored to the membrane by a glycosylphosphatidylinositol (GPI) linkage and lack a cytoplasmic domain, while ephrin-Bs are attached to the membrane by a single transmembrane domain containing a short cytoplasmic PDZ-binding motif .
Ephrins exhibit a variety of biological properties, including their expression patterns and tissue distribution. They are membrane-bound proteins, meaning their signaling can only occur through direct cell-cell interaction . Ephrin ligands and their receptors are expressed in various tissues, playing crucial roles in embryonic development and adult tissue homeostasis . For instance, ephrin-B2 and EphB4 are essential in determining the arterial and venous fate of endothelial cells .
Ephrin-Eph signaling regulates numerous biological processes. During embryonic development, they guide axon growth cones, form tissue boundaries, and facilitate cell migration and segmentation . In adults, they are involved in long-term potentiation, angiogenesis, and stem cell differentiation . Additionally, Eph receptors and ephrins play significant roles in immune responses and pathogen recognition .
Ephrin-Eph interactions follow a bidirectional signaling mechanism. Upon cell-cell contact, high-affinity binding between Eph receptors and ephrin ligands occurs, initiating intracellular signaling events . These events can lead to changes in cell shape, motility, and adhesion . Ephrin-As typically bind EphAs with high affinity through a “lock-and-key” mechanism, while EphBs bind ephrin-Bs with lower affinity via an “induced fit” mechanism .
The expression and activity of ephrins and Eph receptors are tightly regulated through various mechanisms. Transcriptional regulation and post-translational modifications play critical roles in controlling their functions . For example, the Src family kinases and JAK-STAT pathways are involved in the reverse signaling of Eph and ephrins .
Ephrin-Eph signaling has broad applications in biomedical research, diagnostic tools, and therapeutic strategies. They are being explored as potential targets for cancer treatment, particularly in breast cancer, where targeting specific Eph receptors and ephrins can induce apoptosis and tumor regression . Additionally, their roles in angiogenesis and immune responses make them valuable in developing therapies for various diseases .
Ephrins play crucial roles throughout the life cycle, from development to aging and disease. During embryonic development, they guide cell migration and tissue formation . In adulthood, they maintain tissue homeostasis and contribute to processes like neuronal plasticity and vascular remodeling . Dysregulation of ephrin-Eph signaling is associated with various diseases, including cancer and neurodegenerative disorders .
