Recombinant Human Ephrin-B1 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Mouse EphB3 Fc Chimera (Catalog # 432-B3) is coated at 2 μg/mL, Recombinant Human Ephrin-B1 Fc Chimera binds with an apparent KD <0.2 nM.
Source
Mouse myeloma cell line, NS0-derived human Ephrin-B1 protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
49.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
62-67 kDa, reducing conditions
Publications
Read Publications using 7654-EB in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 400 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Ephrin-B1 Fc Chimera Protein, CF
Cek5-L
EFL3
EFL-3
EFNB1
ELK ligand
ELK-L
EphrinB1
Ephrin-B1
LERK-2
STRA-1
Background
Ephrin-B1, also known as Elk Ligand, LERK2, and Eplg2, is an approximately 45 kDa member of the Ephrin-B family of transmembrane ligands that bind and induce the tyrosine autophosphorylation of Eph receptors. The extracellular domains (ECD) of Ephrin-B ligands are structurally related to GPI-anchored Ephrin-A ligands. Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression. Ephrin-B1 preferentially interacts with receptors in the EphB family. The binding of Ephrin-B1 to EphB proteins also triggers reverse signaling through Ephrin-B1 (1, 2). Mature human Ephrin-B1 consists of a 210 amino acid (aa) ECD, a 21 aa transmembrane segment, and an 88 aa cytoplasmic domain (3, 4). Within the ECD, human Ephrin-B1 shares approximately 94% aa sequence identity with mouse and rat Ephrin-B1. Ligation by EphB2 enhances shedding of a 35 kDa fragment of the Ephrin-B1 ECD (5). The residual membrane-bound portion is then cleaved by gamma-secretase to release the intracellular domain (6). Ephrin-B1 also associates in cis with Claudin-1, -4, and -5 (7, 8). It is expressed on glomerular podocyte slit diaphragms, developing thymocytes, peripheral T cells, monocytes, macrophages, vascular endothelial cells, cardiomyocytes, osteoclasts, and luteinizing granulosa cells in the ovary (8-13). In the developing nervous system, Ephrin-B1 plays a role in cellular migration, axon guidance, and presynaptic development (14-16). It also regulates developing thymocyte survival, monocyte migration, osteoclast differentiation and function, cardiac muscle morphogenesis, and tumorigenesis (5, 8, 10-12). Ephrin-B1 is up‑regulated on reactive astrocytes and on macrophages and T cells found in atherosclerotic plaques (11, 17).
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