Recombinant Human IL-15R alpha His-tag Avi-tag Protein, CF

When Recombinant Human IL-15 (247-ILB) is immobilized at 0.1 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-15R alpha His-tag Avi-tag Protein (Catalog # AVI11068) binds with an ED50 of 6.00‑60.0 ng/mL.

2 μg/lane of Biotinylated Recombinant Human IL-15R alpha His-tag Avi-tag Protein (Catalog # AVI11068) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 45-63 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-15R alpha His-tag Avi-tag Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human IL-15 (Catalog # 247-ILB) is immobilized at 0.1 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-15R alpha His-tag Avi-tag (Catalog # AVI11068) binds with an ED₅₀ of 6.00-60.0 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human IL-15R alpha protein
  

  Human IL-15R alpha (Ile31-Thr205) Accession # Q13261.1	6-His tag	Avi-tag
  N-terminus		C-terminus

• Accession #: Q13261.1
• N-terminal Sequence: Ile31
• Structure / Form: Biotinylated via Avi-tag
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 21 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: 45-63 kDa, under reducing conditions.

Packaging, Storage & Formulations

• 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.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human IL-15R alpha His-tag Avi-tag Protein, CF

• CD215 antigen
• CD215
• IL15 R alpha
• IL-15 R alpha
• IL-15 receptor subunit alpha
• IL-15R alpha
• IL15RA
• IL-15Ra
• IL-15R-alpha
• interleukin 15 receptor, alpha
• interleukin-15 receptor subunit alpha
• MGC104179

Background

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.

1. Ma, A. et al. (2006) Annu. Rev. Immunol. 24:657.
2. Di Sabatino, A. et al. (2011) Cytokine Growth Factor Rev. 22:19.
3. Budagian, V. et al. (2006) Cytokine Growth Factor Rev. 17:259.
4. Anderson, D.M. et al. (1995) J. Biol. Chem. 270:29862.
5. Dubois, S. et al. (1999) J. Biol. Chem. 274:26978.
6. Giri, J.G. et al. (1995) EMBO 14:3654.
7. Grabstein, K. et al. (1994) Science 264:965.
8. Giri, J. et al. (1994) EMBO J. 13:2822.
9. Stonier, S.W. and K.S. Schluns (2010) Immunol. Lett. 127:85.
10. Duitman, E.H. et al. (2008) Mol. Cell. Biol. 28:4851.
11. Dubois, S. et al. (2002) Immunity 17:537.
12. Burkett, P.R. et al. (2004) J. Exp. Med. 200:825.
13. Budagian, V. et al. (2004) J. Biol. Chem. 279:42192.
14. Neely, G.G. et al. (2004) J. Immunol. 172:4225.
15. Budagian, V. et al. (2004) J. Biol. Chem. 279:40368.
16. Mortier, E. et al. (2004) J. Immunol. 173:1681.

Bioinformatics

• Uniprot:
  • Q13261.1()