Recombinant Human Ephrin-A4 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized rmEphA7/Fc Chimera at 2 µg/mL (100 µL/well) can bind rhEphrin-A4/Fc Chimera with a linear range of 0.16-10 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human Ephrin-A4 protein
Human Ephrin-A4 (Leu26 - Gly171) Accession # P52798
>90%, 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
Binding Activity
Theoretical MW
43.7 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
50 kDa, reducing conditions
Publications
Read Publications using 369-EA 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
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Ephrin-A4 Fc Chimera Protein, CF
EFL4
EFL-4
EFNA4
EPH-related receptor tyrosine kinase ligand 4
EphrinA4
Ephrin-A4
EPLG4MGC125826
LERK-4
LERK4FLJ57652
ligand of eph-related kinase 4
Background
Ephrin-A4, also known as LERK-4 and EFL-4, (1) is a member of the ephrin ligand family which binds members of the Eph receptor family. All ligands share a conserved extracellular sequence, which most likely corresponds to the receptor binding domain. This conserved sequence consists of approximately 125 amino acids and includes four invariant cysteines. The A-class ligands have a GPI anchor following the conserved sequence. Ephrin-A4 has been shown to bind EphA2, EphA3, EphA4, EphA5, EphA6, EphA7, and EphB1 (2, 3). The extracellular domains of human and mouse Ephrin-A4 share 80% amino acid identity. Only membrane-bound or Fc-clustered ligands are capable of activating the receptor in vitro. While soluble monomeric ligands bind the receptor, they do not induce receptor autophosphorylation and activation (2). In vivo, the ligands and receptors display reciprocal expression (3). It has been found that nearly all receptors and ligands are expressed in developing and adult neural tissue (3). The Eph/ephrin families also appear to play a role in angiogenesis (3).
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