Recombinant human L5RA protein with C-terminal 6×His tag
Figure 1. Human IL5RA Protein, His Tag on SDS-PAGE under reducing condition.
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| Amount : | 50 µg |
| Purification : | The purity of the protein is greater than 90% as determined by SDS-PAGE and Coomassie blue staining. |
| Content : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose is added as protectants before lyophilization. |
| Storage condition : | Store at -80°C for 12 months (Avoid repeated freezing and thawing) |
| Alternative Name : | IL5Ra, CD125, IL-5 R alpha |
Expression Host : HEK293
The protein has a predicted molecular mass of 37.0 kDa after removal of the signal peptide.The apparent molecular mass of IL5RA-His is approximately 50-55 kDa due to glycosylation.
The protein encoded by this gene is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is comprised of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL5 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL5. This protein has been found to interact with syndecan binding protein (syntenin), which is required for IL5 mediated activation of the transcription factor SOX4. Several alternatively spliced transcript variants encoding four distinct isoforms have been reported.
The protein has a predicted molecular mass of 37.0 kDa after removal of the signal peptide.The apparent molecular mass of IL5RA-His is approximately 50-55 kDa due to glycosylation.
The protein encoded by this gene is an interleukin 5 specific subunit of a heterodimeric cytokine receptor. The receptor is comprised of a ligand specific alpha subunit and a signal transducing beta subunit shared by the receptors for interleukin 3 (IL3), colony stimulating factor 2 (CSF2/GM-CSF), and interleukin 5 (IL5). The binding of this protein to IL5 depends on the beta subunit. The beta subunit is activated by the ligand binding, and is required for the biological activities of IL5. This protein has been found to interact with syndecan binding protein (syntenin), which is required for IL5 mediated activation of the transcription factor SOX4. Several alternatively spliced transcript variants encoding four distinct isoforms have been reported.
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