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Recombinant Human CD25/IL-2R alpha Fc Avi-tag Protein, CF

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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 0.05-45 ...read more
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 ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

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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
IEGRMDHuman 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
  • Bioactivity
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

  • CD25 antigen
  • CD25
  • IDDM10
  • IL-2 R alpha
  • IL-2 receptor subunit alpha
  • IL2R alpha
  • IL-2R subunit alpha
  • IL2R
  • IL2RA
  • IL-2Ra
  • IL-2-RA
  • IL2-RA
  • interleukin 2 receptor, alpha
  • interleukin-2 receptor subunit alpha
  • p55
  • TAC antigen
  • TCGFR

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).
  1. Minami, Y. et al. (1993) Annu. Rev. Immunol. 11:245.
  2. Kovanen, P.E. and Leonard, W.J. (2004) Immunol. Rev. 202:67.
  3. Bluestone, J.A. and Tang, Q. (2005) Curr. Opin. Immunol. 17:638.
  4. Hatakeyama, M. et al. (1989) Science 244:551.
  5. Takeshita, T. et al. (1992) Science 257:379.
  6. Stauber, D. et al. (2006) Proc. Natl. Acad. Sci. U. S. A. 103:2788.
  7. Wang, X. et al. (2005) Science 310:1159.
  8. Wagner, D.K. et al. (1986) J. Immunol. 137:592.
  9. Schulz, O. et al. (1998) J. Exp. Med. 187:271.
  10. Witkowska, A.M. (2005) Mediat. Inflamm. 2005:121.
  11. Willerford, D.M. et al. (1995) Immunity 3:521.
  12. Van Parijs, L. et al. (1997) J. Immunol. 158:3738.
  13. Almeida, A.R.M. et al. (2002) J. Immunol. 169:4850.

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