Recombinant Human IL-2 Biotinylated Protein Summary
Product Specifications
Ala21-Thr153, with an N-terminal Met
Analysis
Product Datasheets
Carrier Free
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.
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.
BT202
Formulation | Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
Reconstitution | Reconstitute at 250 μg/mL in 4 mM HCl. |
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.
|
BT202/CF
Formulation | Lyophilized from a 0.2 μm filtered solution in HCl with Trehalose. |
Reconstitution | Reconstitute at 250 μg/mL in 4 mM HCl. |
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.
|
Scientific Data
When Recombinant Human IL-2 Ra 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).
Reconstitution Calculator
Background: IL-2
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).
- Ma, A. et al. (2006) Annu. Rev. Immunol. 24:657.
- Gaffen, S.L. and K.D. Liu (2004) Cytokine 28:109.
- Taniguchi, T. et al. (1983) Nature 302:305.
- Mosmann, T.R. et al. (1987) J. Immunol. 138:1813.
- Liparoto, S.F. et al. (2002) Biochemistry 41:2543.
- Wang, X. et al. (2005) Science 310:1159.
- Bodnar, A. et al. (2008) Immunol. Lett. 116:117.
- Jaleco, S. et al. (2003) J. Immunol. 171:61.
- Malek, T.R. (2003) J. Leukoc. Biol. 74:961.
- Laurence, A. et al. (2007) Immunity 26:371.
- Kryczek, I. et al. (2007) J. Immunol. 178:6730.
- Afzali, B. et al. (2007) Clin. Exp. Immunol. 148:32.
- Fehervari, Z. et al. (2006) Trends Immunol. 27:109.
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