Human EphA7, His Tag (EP7-H5221) is expressed from human 293 cells (HEK293). It contains AA Gln 27 - Ile 556 (Accession # AAI26126).
Predicted N-terminus: Gln 27
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 60.2 kDa. The protein migrates as 70-80 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Less than 1.0 EU per μg by the LAL method.
>98% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human EphA7, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 98%.
Ephrin type-A receptor 7 (EPHA7) is also known as EPH homology kinase 3 (EHK3), EPH-like kinase 11 (HEK11), which belongs to the protein kinase superfamily or tyr protein kinase family or ephrin receptor subfamily. EPHA7 / EHK3 contains 1 Eph LBD (Eph ligand-binding) domain, 2 fibronectin type-III domains, 1 protein kinase domain, 1 SAM (sterile alpha motif) domain. EHK-3 / EPHA7 is widely expressed. The catalytic activity of EPHA7 / EHK3 is “ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate”. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands.