Recombinant Human CD25/IL-2R alpha His 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 His-tag Avi-tag (Catalog
# AVI10305) binds with an ED 50 of 45.0-540 ng/mL. The biotin to protein ratio is greater than 0.7 as determined by the HABA assay. |
Source |
Human embryonic kidney cell, HEK293-derived human CD25/IL-2R alpha protein Human CD25/IL-2R alpha (Glu22-Cys213) Accession # P01589.1 | Avi-tag | 6-His tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Glu22 |
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 |
- Binding Activity
- Bioactivity
|
Theoretical MW |
25 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 |
36-51 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 His 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). Our Avi‑tag Biotinylated IL-2Ra features biotinylation at
a single site contained within the Avi‑tag, a unique 15 amino acid peptide.
Protein orientation will be uniform when bound to streptavidin-coated surface
due to the precise control of biotinylation and the rest of the protein is
unchanged so there is no interference in the protein's bioactivity
- 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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