Recombinant Human CD25/IL-2R alpha Fc Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. 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. |
Source |
Human embryonic kidney cell, HEK293-derived human CD25/IL-2R alpha protein Human CD25/IL-2R alpha (Glu22-Cys213) Accession # P01589.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | |
|
Accession # |
|
N-terminal Sequence |
Glu22 |
Structure / Form |
Disulfide-linked homodimer, biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
50 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. |
SDS-PAGE |
69-77 kDa, under reducing conditions |
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 PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD25/IL-2R alpha Fc Avi-tag Protein, CF
Background
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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