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 ED 50 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 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag | N-terminus | | | C-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
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
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.
- Jia, Z. et al. (2019) Int. Immunpharmacol. 74:105716.
- Zhou, X. et al. (2019) Fish & Shellfish Immunol. 93:641.
- Zhang, Z. et al. (2019) J. Exp. Med. 216:1311.
- Fernandez, I. et al. (2019) J. Exp. Med. 216:1255.
- Honda, M. et al. (1990) J. Immunol. 145:4131.
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