Recombinant Human IL-21R His-tag Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-21 Protein
(Catalog #
8879-IL) is immobilized at 1.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human IL-21R His-tag Avi-tag (Catalog # AVI9247) that produces 50% of the optimal binding response is 40.0-240 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human IL-21R protein Human IL-21R (Cys20-Pro236) Accession # Q9HBE5.1 | 6-His tag | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Cys20 |
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 |
26 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 |
51-59 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 100 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-21R His-tag Avi-tag Protein, CF
Background
Interleukin-21 Receptor (IL-21 R )is a type I transmembrane glycoprotein within the class I cytokine receptor family (1). IL-21 R associates with the common gamma chain ( gamma
c) which is also a component of the receptors for IL-2, IL-4, IL-7, IL-9, and IL-15 (2, 3). Mature human IL-21 R consists of a 213 amino acid (aa) extracellular domain (ECD) with 4 conserved cysteine residues, a fibronectin type III domain, and a WSxWS motif, followed by a 21 aa transmembrane domain and a 285 aa cytoplasmic domain with a Box 1 motif, a kinase domain, and several sites for tyrosine phosphorylation (4, 5). Within the ECD, human IL-21 R shares 69% aa identity with mouse and rat IL-21 R, respectively. IL-21 R is expressed mainly on B cells (highest on mature, activated, follicular and germinal center B cells), NK cells, and activated T cells, but is also found on dendritic cells, alternatively activated macrophages, intestinal lamina propria fibroblasts and epithelial cells, and keratinocytes (1, 4, 5). Both IL-21 and IL-4 are necessary for efficient B cell IgG1 production and normal germinal center architecture (6). B cell IL-21 R engagement induces Blimp-1 (which mediates plasma cell differentiation) and is important for memory responses (7, 8). IL-21 R engagement enhances NK cell mediated cytotoxic activity and IFN-gamma production (4, 9), control of viral infection and tumor growth by CD8
+ T cells (10), development of regulatory T cells (11), IL-23 responsiveness of encephalitogenic Th17 cells (12), but suppresses the accumulation of IL-17 secreting gamma δ T cells in the airway (13). IL-21 R expression is often upregulated in allergic skin inflammation, systemic lupus erythematosus and diffuse large B cell lymphoma (DLBCL) (14, 15). Our Avi-tag Biotinylated human IL-21R 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.
- Tangye, S.G. (2015) Curr. Opin. Immunol. 34:107.
- Asao, H. et al. (2001) J. Immunol. 167:1.
- Habib, T. et al. (2002) Biochemistry 41:8725.
- Parrish-Novak, et al. (2000) Nature 408:57.
- Ozaki, K. et al. (2000) Proc. Natl. Acad. Sci. USA 97:11439.
- Ozaki, K. et al. (2002) Science 298:1630.
- Rankin, A.L. et al. (2011) J. Immunol. 186:667.
- King, I.L. et al. (2010) J. Immunol. 185:6138.
- Kasaian, M.T. et al. (2002) Immunity 16:559.
- Frohlich, A. et al. (2009 Science 324:1576.
- Tortola, L. et al. (2010) Blood 116:5200.
- Lee, Y. et al. (2015) J. Clin. Invest. 125:4011.
- Moser, E.K. et al. (2015) PLoS One 10:e0120169.
- Jin, H. et al. (2009) J. Clin. Invest. 119:47.
- Sarosiek, K.A. et al. (2010) Blood 115:570.
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