| Cat.No. : |
IL15RA-051H
Optional Service: Optional requirements on this protein
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| Product Overview : |
Biotinylated Recombinant Human IL15RA(Ile31-Thr205) protein, fused to Fc/Avi tag at the C-terminus, was expressed in CHO cells . |
| Description : |
Interleukin 15 Receptor alpha (IL‑15 R alpha ), also known as CD215, is a widely expressed 60-kDa transmembrane glycoprotein that plays an important role in the homeostasis and activation of NK cells and CD8+ memory T cells and participates in the development and function of many other hematopoietic cell types and non‑immune cell types (1‑3). Mature human IL‑15 R alpha consists of a 175 amino acid (aa) extracellular domain (ECD) containing one N‑linked glycosylation site, a 23 aa transmembrane segment, and a 39 aa cytoplasmic tail (4). Within the ECD, human IL‑15 R alpha shares approximately 60% aa sequence identity with mouse and rat IL‑15 R alpha. Alternate splicing of human IL‑15 R alpha generates additional isoforms with variable length deletions in the ECD and/or substitutions in the cytoplasmic domain (4, 5). IL‑15 R alpha binds to Interleukin‑15 with high affinity (6). IL‑15 additionally interacts with lower affinity to a complex of IL‑2 R beta and the common gamma chain ( gamma c) which are also subunits of the IL‑2 receptor complex (7, 8). The use of shared receptor components contributes to the overlapping biological effects of IL‑15 and IL‑2. The dominant mechanism of IL‑15 action is known as transpresentation in which IL‑15/IL‑15 R alpha complexes are expressed on the surface of one cell and interact with complexes of IL‑2 R beta / gamma c on adjacent cells (9). This enables cells to respond to IL‑15 even if they do not express IL‑15 R alpha (10‑12). IL‑15/IL‑15 R alpha complexes can transmit reverse signaling that promotes cellular adhesion, tyrosine phosphorylation of intracellular proteins, and cytokine secretion by the IL‑15/IL‑15 R alpha expressing cells (13, 14). Shed soluble forms of IL‑15 R alpha retain the ability to bind tightly to IL‑15 and can inhibit IL‑15 bioactivity (6, 15, 16). Our Avi-tag Biotinylated Recombinant Human IL‑15 R alpha features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity. |
| Source : |
CHO cells |
| Species : |
Human |
| Tag : |
Fc/Avi |
| Predicted N Terminal : |
Ile31 |
| Form : |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Bio-activity : |
The biotin to protein ratio is greater than 0.7 as determined by the HABA assay.
Measured by its binding ability in a functional ELISA.
When Biotinylated Recombinant Human IL15RA Fc Chimera Avi-tag is immobilized at 0.5 µg/mL (100 µL/well),
Recombinant Human IL15 binds with an ED50 of 0.02-0.16 ng/mL. |
| Molecular Mass : |
70-80 kDa, under reducing conditions |
| Protein length : |
Ile31-Thr205 |
| Endotoxin : |
<0.10 EU per 1 μg of the protein by the LAL method. |
| Purity : |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Applications : |
Binding Activity, Bioactivity |
| Storage : |
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. |
| Reconstitution : |
Reconstitute at 400 μg/mL in PBS. |
| SDS-PAGE : |
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2 μg/lane Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining.
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| Binding Activity : |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.