Recombinant Bovine IL-2 Protein, CF

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

Recombinant Bovine IL-2 Protein, CF Summary

• Details of Functionality: Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED₅₀ for this effect is 0.15-0.75 µg/mL.
• Source: E. coli-derived bovine IL-2 protein
  Ala21-Thr155, with an N-terminal Met
• Accession #: P05016
• N-terminal Sequence: Met
• Protein/Peptide Type: Recombinant Proteins
• Gene: IL2
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 15.6 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.

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 Sodium Acetate.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Bovine IL-2 Protein, CF

• 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

Bovine Interleukin-2 (IL-2) is a 15 kDa, alpha -helical, single chain, potentially glycosylated polypeptide that has potent stimulatory activity for antigen-activated T cells (1 - 5). The molecule is synthesized as a 155 amino acid (aa) precursor that contains a 20 aa signal peptide plus a 135 aa mature segment that is possibly O-glycosylated (4, 5). The mature region has multiple alpha -helices and one intrachain disulfide bond. Mature bovine IL-2 is 64%, 60%, 49%, 50%, 72%, 63% and 67% to mature human, canine, mouse, rat, porcine, equine, and feline IL-2, respectively. Mammalian cells known to express IL-2 include CD4⁺ and CD8⁺ T cells, visceral smooth muscle cells, eosinophils, gamma δ T cells, B cells and dendritic cells. The receptor for IL-2 is complex and consists of three distinct subunits in varying combinations (6, 7). Two of these are ligand-binding and are termed IL-2 R alpha and IL-2 R beta . IL-2 R alpha is 55 kDa and binds IL-2 with low affinity. IL-2 R beta is 75 kDa and binds IL-2 with intermediate affinity. Signal transduction is performed by both IL-2 R beta and a 64 kDa common gamma chain ( gamma _c). This signal transducing common gamma chain does not bind IL-2, but does heterodimerize with IL-2 R beta to form a functional IL-2 receptor. The complex heterotrimeric alpha -beta -gamma c receptor may arise from IL-2 binding to preformed R alpha -R beta  complexes (8). Functionally, IL-2 is best known for its autocrine and paracrine activity on T cells. It drives resting T cells into active G1, inducing IL-2 and IL-2 R alpha synthesis and cell proliferation (7). It also promotes Fas-induced death of naïve CD4⁺ T cells, while having minimal effect on activated CD4⁺ memory lymphocytes. Finally, IL-2 seems to play a central role in the expansion and maintenance of CD4⁺ CD25⁺ regulatory T cells. Thus, IL-2 may be a key cytokine in the natural suppression of autoimmunity (9, 10).

1. Smith, K.A. (1992) Curr. Opin. Immunol. 4:271.
2. Smith, K.A. (1988) Science 240:1169.
3. Waldmann, T.A. et al. (2001) Immunity 14:105.
4. Cerretti, D.P. et al. (1986) Proc. Natl. Acad. Sci. USA 83:3223.
5. Reeves, R. et al. (1986) Proc. Natl. Acad. Sci. USA 83:3228.
6. Ellery, J.M. and P.J. Nicholls (2002) Cytokine Growth Factor Rev. 13:27.
7. Nelson, B.H. and D.M. Willerford (1998) Adv. Immunol. 70:1.
8. Liparoto, S.F. et al. (2002) Biochemistry 41:2543.
9. Jaleco, S. et al. (2003) J. Immunol. 171:61.
10. Malek, T.R. (2003) J. Leukoc. Biol. 74:961.

Bioinformatics

• Gene Symbol: IL2
• Uniprot:
  • P05016()