Reactivity | FeSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | 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 0.02-0.12 ng/mL. |
Source | E. coli-derived feline IL-2 protein Ala21-Thr154 (Cys146Ser), with and without an N-terminal Met |
Accession # | |
N-terminal Sequence | Met & Ala21 |
Protein/Peptide Type | Recombinant Proteins |
Gene | IL2 |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note | <0.01 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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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. |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Sodium Acetate. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Interleukin-2 (IL-2) is a secreted, single chain alpha ‑helical polypeptide that has potent stimulatory activity for antigen-activated T cells. The feline IL-2 gene encodes a 154 amino acid (aa) precursor protein with a 20 aa signal peptide plus a 134 aa mature segment. There are suggestions that the mature protein may be O-glycosylated. At the aa sequence level, mature feline IL-2 is 78%, 82%, 60%, 64%, 62%, 75%, 62%, and 76% identical to mature human, canine, mouse, rat, cotton rat, porcine, goat, and equine 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 biological activity of IL-2 is mediated by IL-2 receptor complexes consisting of three distinct subunits ( alpha , beta , gamma ) in two combinations. The high‑affinity signaling IL-2 receptor complex is a heterotrimer of the IL-2 receptor alpha , beta , gamma subunits. The intermediate signaling complex is a heterodimer of the IL-2 R beta and gamma subunits. The non-ligand binding gamma subunit, referred to as the common gamma subunit ( gamma c), is also a subunit of the receptor complexes of IL-4, IL-7, IL-9 and IL-15. Functionally, IL-2 is best known for its autocrine and paracrine activity on T cells. On naïve CD8+ T cells, high IL-2 levels can induce cell proliferation with a bias towards cytotoxicity. In the presence of low levels of IL-2, CD8+ T cells preferentially undergo apoptosis with a bias towards cytokine secretion. IL-2 also seems to play a central role in the expansion and maintenance of CD4+ CD25+ regulatory T cells. This indicates IL-2 may be a key cytokine in the natural suppression of autoimmunity (1 - 9).
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