Recombinant Human IL-2 Biotinylated Protein

When Recombinant Human IL‑2 R alpha Fc Chimera (Catalog # 1020‑RL) is coated at 1 μg/mL, Recombinant Biotinylated Human IL‑2 (Catalog # BT202) binds with an ED50 of 4‑24 ng/mL.

When Recombinant Human IL‑2 R alpha Fc Chimera (Catalog # 1020‑RL) is coated at 1 μg/mL, Recombinant Biotinylated Human IL‑2 (Catalog # BT202) binds with an ED50 of 4‑24 ng/mL.

In a functional flow cytometry test, Recombinant Human IL-2 Biotinylated protein (Catalog # BT202, 500 ng/mL) binds to HEK293 human embryonic kidney cell line transfected with recombinant human CD25/IL-2R alpha (black dotted line). Binding is completely blocked (orange histogram) by 0.5 μg/mL of Mouse Anti-Human CD25/IL-2R alpha Monoclonal Antibody (Catalog # MAB1020). Mouse IgG2A Isotype Control (Catalog # MAB003) at 0.5 μg/mL was used as a control (blue line). Ligand binding was detected by staining cells with APC-conjugated Streptavidin (Catalog # F0050).

• Reactivity: Hu
• Applications: Bioactivity

Recombinant Human IL-2 Biotinylated Protein Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human IL‑2 R alpha Fc Chimera (Catalog # 1020-RL) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human IL‑2 binds with an ED₅₀ of 4-24 ng/mL. Measured in a cell proliferation assay using CTLL‑2 mouse cytotoxic T cells. Gearing, A.J.H. and C.B. Bird (1987) in Lymphokines and Interferons, A Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 295. The ED₅₀ for this effect is 0.05-0.25 ng/mL.
• Source: E. coli-derived human IL-2 protein
  Ala21-Thr153, with an N-terminal Met
• Accession #: P60568
• N-terminal Sequence: Met
• Structure / Form: Biotinylated protein via amines
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
  • Bioactivity2
• Theoretical MW: 15 kDa (unlabeled).
  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: 13 kDa, 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 HCl with BSA as a carrier protein.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 250 μg/mL in 4 mM HCl.

Notes

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

Alternate Names for Recombinant Human IL-2 Biotinylated Protein

• Aldesleukin
• IL2
• IL-2
• IL-2lymphokine
• interleukin 2
• interleukin-2
• involved in regulation of T-cell clonal expansion
• Proleukin
• T cell growth factor
• T-cell growth factor
• TCGF

Background

Interleukin-2 (IL-2) is a O-glycosylated, four alpha -helix bundle cytokine that has potent stimulatory activity for antigen-activated T cells. It is expressed by CD4⁺ and CD8⁺ T cells, gamma δ T cells, B cells, dendritic cells, and eosinophils (1-3). Mature human IL-2 shares 56% and 66% aa sequence identity with mouse and rat IL-2, respectively. Human and mouse IL-2 exhibit cross-species activity (4). The receptor for IL-2 consists of three subunits that are present on the cell surface in varying preformed complexes (5-7). The 55 kDa IL-2 R alpha is specific for IL-2 and binds with low affinity. The 75 kDa IL-2 R beta , which is also a component of the IL-15 receptor, binds IL-2 with intermediate affinity. The 64 kDa common gamma chain gamma c/IL-2 R gamma , which is shared with the receptors for IL-4, -7, -9, -15, and -21, does not independently interact with IL-2. Upon ligand binding, signal transduction is performed by both IL-2 R beta and gamma c. IL-2 is best known for its autocrine and paracrine activity on T cells. It drives resting T cells to proliferate and induces IL-2 and IL-2 R alpha synthesis (1, 2). It contributes to T cell homeostasis by promoting the Fas-induced death of naïve CD4⁺ T cells but not activated CD4⁺ memory lymphocytes (8). IL-2 plays a central role in the expansion and maintenance of regulatory T cells, although it inhibits the development of Th17 polarized cells (9-11). Thus, IL-2 may be a key cytokine in the natural suppression of autoimmunity (12, 13).

1. Ma, A. et al. (2006) Annu. Rev. Immunol. 24:657.
2. Gaffen, S.L. and K.D. Liu (2004) Cytokine 28:109.
3. Taniguchi, T. et al. (1983) Nature 302:305.
4. Mosmann, T.R. et al. (1987) J. Immunol. 138:1813.
5. Liparoto, S.F. et al. (2002) Biochemistry 41:2543.
6. Wang, X. et al. (2005) Science 310:1159.
7. Bodnar, A. et al. (2008) Immunol. Lett. 116:117.
8. Jaleco, S. et al. (2003) J. Immunol. 171:61.
9. Malek, T.R. (2003) J. Leukoc. Biol. 74:961.
10. Laurence, A. et al. (2007) Immunity 26:371.
11. Kryczek, I. et al. (2007) J. Immunol. 178:6730.
12. Afzali, B. et al. (2007) Clin. Exp. Immunol. 148:32.
13. Fehervari, Z. et al. (2006) Trends Immunol. 27:109.

Show all background references

Bioinformatics

• Uniprot:
  • P60568()