Recombinant Human IL-15R alpha Fc Chimera Avi-tag, CF

Biotinylated
Catalog # Availability Size / Price Qty
AVI7194-050
Biotinylated Recombinant Human IL-15R alpha Fc Chimera Avi-tag Protein Binding Activity.
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Recombinant Human IL-15R alpha Fc Chimera Avi-tag, CF Summary

Learn more about Avi-tag Biotinylated Proteins

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
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 IL-15R alpha Fc Chimera Avi-tag (Catalog # AVI7194) is immobilized at 0.5 µg/mL (100 µL/well), Recombinant Human IL-15  (Catalog # 247-ILB) binds with an ED50 of 0.02-0.16 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL-15R alpha protein
Human IL-15R alpha
(Ile31-Thr205)
Accession # Q13261.1
IEGRMD
Human IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Analysis
Ile31
Structure / Form
Disulfide-linked homodimer, biotinylated via Avi-tag
Predicted Molecular Mass
47 kDa
SDS-PAGE
70-80 kDa, under reducing conditions

Product Datasheets

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AVI7194

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

AVI7194

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 400 μg/mL in PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.

Scientific Data

Binding Activity View Larger

When Biotinylated Recombinant Human IL-15R alpha Fc Chimera Avi-tag (Catalog # AVI7194) is immobilized at 0.5 µg/mL (100 µL/well), Recombinant Human IL-15 (247-ILB) binds with an ED50 of 0.02-0.16 ng/mL.

SDS-PAGE View Larger

2 μg/lane of Biotinylated Recombinant Human IL-15R alpha Fc Chimera Avi-tag (Catalog # AVI7194) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 70-80 kDa and 140-160 kDa, respectively.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: IL-15R alpha

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.

References
  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.
Long Name
Interleukin 15 Receptor alpha
Entrez Gene IDs
3601 (Human); 16169 (Mouse); 102121571 (Cynomolgus Monkey)
Alternate Names
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

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