IL-2, Bovine, BioAssay(TM) ELISpot Kit (Interleukin 2)

Bovine Interleukin 2 (IL-2) is a 15kD, a-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 20aa signal peptide plus a 135aa mature segment that is possibly O-glycosylated (4, 5). The mature region has multiple a-helices and one intrachain disulfide bond. Mature bovine IL-2 is 64%, 60%, 49%, 50%, 72%, 63%, and 67% identical 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, gd 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 Ra and IL-2 Rb. IL-2Ra is 55kD and binds IL-2 with low affinity. IL-2 Rb is 75kD and binds IL-2 with intermediate affinity. Signal transduction is performed by both IL-2 Rb and a 64kD common gamma chain (gc). This signal transducing common gamma chain does not bind IL-2 but does heterodimerize with IL-2 Rb to form a functional IL-2 receptor. The complex heterotrimeric a-b-gc receptor may arise from IL-2 binding to preformed Ra-Rb 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 Ra synthesis and cell proliferation (7). It also promotes Fas-induced death of na

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SPECIFICATIONS

Catalog Number

145749

Size

1Kit

References

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.\n10. Malek, T.R. et al. (2003) J. Leujoc. Biol. 74:961. 11. Czerkinsky, C.C. et al. (1983) J. Immunol. Methods 65:109. 12. Sedgwick, J.D. and P.G. Holt (1983) J. Immunol. Methods 57:301. 13. Czerkinsky, C.C. et al. (1984) J. Immunol. Methods 72:489. 14. Helms, T. et al. (2000) J. Immunol. 164:3723.