Measured by its binding ability in a functional ELISA. Immobilized rhEphA2 at 2 µg/mL (100 µL/well) can bind rmEphrin-A1/Fc Chimera with a linear range of 0.078-5 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human EphA2 protein Gln25-Asn534, with a C-terminal 6-His tag
>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
Binding Activity
Theoretical MW
56.9 kDa. 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
70-75 kDa, reducing conditions
Publications
Read Publications using 3035-A2 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 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 EphA2 Protein, CF
ARCC2
EC 2.7.10
EC 2.7.10.1
Eck
ECKepithelial cell receptor protein tyrosine kinase
EPH receptor A2
EphA2
ephrin type-A receptor 2
Epithelial cell kinase
Myk2
Sek2
soluble EPHA2 variant 1
Tyrosine-protein kinase receptor ECK
Background
EphA2, also known as Eck, Myk2, and Sek2, is a member of the Eph receptor tyrosine kinase family which binds Ephrins A1, 2, 3, 4, and 5 (1, 2, 3, 4). A and B class Eph proteins have a common structural organization. The human EphA2 cDNA encodes a 976 amino acid (aa) precursor including a 24 aa signal sequence, a 510 aa extracellular domain (ECD), a 24 aa transmembrane segment, and a 418 aa cytoplasmic domain. The ECD contains an N-terminal globular domain, a cysteine-rich domain, and two fibronectin type III domains (5). The cytoplasmic domain contains a juxtamembrane motif with two tyrosine residues, which are the major autophosphorylation sites, a kinase domain, and a sterile alpha motif (SAM) (5). The ECD of human EphA2 shares 90 - 94% aa sequence identity with mouse, bovine, and canine EphA2, and approximately 45% aa sequence identity with human EphA1, 3, 4, 5, 7, and 8. EphA2 becomes autophosphorylated following ligand binding (6, 7) and then interacts with SH2 domain-containing PI3-kinase to activate MAPK pathways (8, 9). Reverse signaling is also propagated through the Ephrin ligand. Transcription of EphA2 is dependent on the expression of E-Cadherin (10), and can be induced by p53 family transcription factors (11). EphA2 is upregulated in breast, prostate, and colon cancer vascular endothelium. Its ligand, EphrinA1, is expressed by the local tumor cells (12, 13). In some cases, EphA2 and EphrinA1 are expressed on the same blood vessels (14). EphA2 signaling cooperates with VEGF receptor signaling in promoting endothelial cell migration (13). The gene encoding human EphA2 maps to a region on chromosome 1 which is frequently deleted in neuroectodermal tumors (15).
Poliakov, A. et al. (2004) Dev. Cell 7:465.
Surawska, H. et al. (2004) Cytokine Growth Factor Rev. 15:419.
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