Recombinant Human CD25/IL-2R alpha Fc Avi-tag Protein, CF
Recombinant Human CD25/IL-2R alpha Fc Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
When Recombinant Human IL-2 (Catalog # 202-IL) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human CD25/IL-2R alpha Fc Chimera Avi-tag (Catalog # AVI1020) binds with an ED50 of 50-450 ng/mL.
Human CD25/IL-2R alpha (Glu22-Cys213) Accession # P01589.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag |
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.
AVI1020
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
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.
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Scientific Data
When Recombinant Human IL-2 (202-IL) is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant Human CD25/IL-2R alpha Fc Chimera Avi-tag (Catalog # AVI1020) binds with an ED50 of 50-450 ng/mL.
2 μg/lane of Biotinylated Recombinant Human CD25/IL-2R alpha Fc Chimera Avi-tag (Catlog # AVI1020) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 69-77 kDa and 140- 154 kDa, respectively.
Reconstitution Calculator
Background: CD25/IL-2R alpha
IL-2 receptor alpha (IL-2R alpha), also known as CD25, is a 55 kDa type I membrane glycoprotein that belongs to the family of cytokine receptors that utilize the common gamma chain subunit (gamma c). Human IL-2R alpha cDNA encodes a 213 amino acid (aa) precursor with a 21 aa signal peptide and a 192 aa extracellular region. The ECD of Human IL-2R alpha shares a 59% amino acid sequence identity with the ECD of mouse and rat IL-2R alpha, respectively. IL‑2R alpha is primarily expressed on activated T cells and on regulatory T cells (Treg) (1-3). IL-2R beta (CD122) and gamma c (IL-2R gamma /CD132) dimerize to form a constitutively expressed intermediate affinity IL-2 receptor (4, 5). By itself, IL-2R alpha binds IL-2 with low affinity. IL-2R alpha makes no contacts with IL-2R beta or gamma c, and only minor changes are observed in the IL-2 structure in response to receptor binding. These findings support the principal role of IL-2R alpha to deliver IL-2 to the signaling complex and act as regulator of signal transduction (6, 7). A soluble form of IL‑2R alpha can be generated by proteolytic cleavage of the cell surface receptor, rendering the T cell unresponsive to IL-2 (8, 9). Increased serum levels of soluble IL‑2R alpha are found in some cancers and immune disorders (10). IL-2R alpha is required for activation induced cell death (AICD) of naive T cells, a mechanism responsible for deleting autoreactive T cell clones (11, 12). IL-2R alpha is also required for the development of CD4+CD25+ Treg which suppresses autoreactive CD4+ T cells, thereby contributing to peripheral T cell homeostasis (11-13).
- Minami, Y. et al. (1993) Annu. Rev. Immunol. 11:245.
- Kovanen, P.E. and Leonard, W.J. (2004) Immunol. Rev. 202:67.
- Bluestone, J.A. and Tang, Q. (2005) Curr. Opin. Immunol. 17:638.
- Hatakeyama, M. et al. (1989) Science 244:551.
- Takeshita, T. et al. (1992) Science 257:379.
- Stauber, D. et al. (2006) Proc. Natl. Acad. Sci. U. S. A. 103:2788.
- Wang, X. et al. (2005) Science 310:1159.
- Wagner, D.K. et al. (1986) J. Immunol. 137:592.
- Schulz, O. et al. (1998) J. Exp. Med. 187:271.
- Witkowska, A.M. (2005) Mediat. Inflamm. 2005:121.
- Willerford, D.M. et al. (1995) Immunity 3:521.
- Van Parijs, L. et al. (1997) J. Immunol. 158:3738.
- Almeida, A.R.M. et al. (2002) J. Immunol. 169:4850.
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