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Recombinant Human IL-2 R beta Fc Chimera Avi-tag Protein, CF

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When Biotinylated Recombinant Human IL-2 R beta Fc Chimera Avi-tag (Catalog # AVI10919) is immobilized at 0.25 µg/mL (100 µL/well), Recombinant Human IL-15 (247-ILB) binds with an ED50 of 0.50-4.00 ng/mL.
2 μg/lane of Biotinylated Recombinant Human IL-2 R beta Fc Chimera Avi-tag Protein (Catalog # AVI10919) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Format
Carrier-Free

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Recombinant Human IL-2 R beta Fc Chimera Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Biotinylated Recombinant Human IL-2 R beta Fc Chimera Avi-tag (Catalog # AVI10919) is immobilized at 0.25 µg/mL (100 µL/well), Recombinant Human IL-15 (Catalog # 247-ILB) binds with an ED50 of 0.50-4.00 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human IL-2 R beta protein
Human IL-2 R beta
(Ala27-Asp239)
Accession # P14784.1
IEGRMDHuman IgG1
(Pro100-Lys330)
Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Ala27
Structure / Form
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

Theoretical MW
53 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
60-70 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 IL-2 R beta Fc Chimera Avi-tag Protein, CF

  • CD122 antigen
  • CD122
  • high affinity IL-2 receptor beta subunit
  • High affinity IL-2 receptor subunit beta
  • IL-15 R beta
  • IL-2 R beta
  • IL-2 receptor subunit beta
  • IL2R beta
  • IL-2R subunit beta
  • IL2RB
  • IL-2Rb
  • interleukin 15 receptor, beta
  • interleukin 2 receptor, beta
  • interleukin-2 receptor subunit beta
  • P70-75
  • p75

Background

Interleukin-2 receptor subunit beta (IL-2 RB), also known as high affinity IL-2 receptor subunit beta, interleukin-15 receptor subunit beta, p70-75 (p75), and CD122, is a member of the cytokine receptor superfamily that plays a role in T cell-mediated immune responses (1, 3). Human IL-2 RB consists of an extracellular domain (ECD) containing a fibronectin type III domain and a WSXWS motif, a type I transmembrane domain, and a cytoplasmic tail. Within the ECD, mature human IL-2 RB shares 58% and 61% amino acid sequence identity with mouse and rat IL-2 RB, respectively. A soluble IL-2 RB (sIL-2 RB) has been identified in the culture supernatants of a human lymphoid cell line, YT, that displays IL-2 RB (5). Functional IL-2 receptors can exist in two affinity states on cell surfaces: the high affinity complex consisting of heterotrimers of the alpha, beta, and gamma chains and the intermediate affinity complex comprising heterodimers of the beta and gamma chains (2, 3). Individual beta chains and alpha chains exhibit low affinity IL-2 binding and the gamma chain alone does not bind IL-2. In addition to their involvement in IL-2 mediated signal transduction, both the beta chain and gamma chain have been shown to be required for IL-15 mediated signaling (4). At present, the function of IL-2 sR beta is unclear. Recombinant human sIL-2RB binds IL-2 with low affinity and is not an effective IL-2 antagonist on cells displaying the high or intermediate affinity IL-2 signaling receptors. Nevertheless, sIL-2 RB binds IL-15 with sufficient affinity to neutralize IL-15 biological activities. Our Avi-tag Biotinylated Recombinant Human IL‑2 RB 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.
  1. Jia, Z. et al. (2019) Int. Immunpharmacol. 74:105716.
  2. Zhou, X. et al. (2019) Fish & Shellfish Immunol. 93:641.
  3. Zhang, Z. et al. (2019) J. Exp. Med. 216:1311.
  4. Fernandez, I. et al. (2019) J. Exp. Med. 216:1255.
  5. Honda, M. et al. (1990) J. Immunol. 145:4131.

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