Recombinant Human IFN-alpha/beta R2 Fc Chimera Protein, CF
Recombinant Human IFN-alpha/beta R2 Fc Chimera Protein, CF Summary
Product Specifications
| Human IFN-alpha / beta R2 (Ile27-Lys243) Accession # P48551 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
4015-AB
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 500 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Recombinant Human IFN-alpha/beta R2 Fc Chimera (Catalog # 4015-AB) inhibits the anti-viral activity of Recombinant Human IFN-beta (Catalog # 8499-IF). The ED50 for this effect is 0.1-0.6 μg/mL.
Reconstitution Calculator
Background: IFN-alpha/beta R2
IFN-alpha / beta R2, also known as IFNAR2, is a 100 kDa glycoprotein in the class II cytokine receptor family. These proteins form heterodimeric receptor complexes that transduce signals from the interferon, IL-10, and IL-28 families of cytokines (1, 2). IFN-alpha / beta R2, in association with IFN-alpha / beta R1, is required for mediating the antiviral, antiproliferative, and apoptotic effects of the type I interferons IFN-alpha and IFN-beta. IFN-alpha / beta R2 is the principal ligand binding subunit of the receptor. Ligand binding is stabilized by the subsequent association with IFN-alpha / beta R1, resulting in the formation of a signaling ternary receptor complex (3, 4). Mature human IFN-alpha / beta R2 consists of a 217 amino acid (aa) extracellular domain (ECD) with two fibronectin type III repeats, a 21 aa transmembrane segment, and a 251 aa cytoplasmic domain. Alternate splicing generates a secreted isoform that corresponds to the ECD and a 50 kDa transmembrane isoform with a substituted and truncated cytoplasmic region (5, 6). The short isoform is impaired in its ability to activate signaling molecules and functions as a dominant negative receptor subunit (7 - 9). IFN-alpha / beta R2 is also subject to presenilin-dependent intramembrane proteolysis, resulting in the liberation of nearly the entire ECD as well as the cytoplasmic domain which migrates to the nucleus and can inhibit gene transcription (10). High concentrations of soluble IFN-alpha / beta R2 bind and neutralize IFN-alpha and IFN-beta, while lower concentrations prolong the antiviral activity of circulating IFN-beta but not IFN-alpha (11). Human but not mouse IFN-alpha / beta R2 constitutively associates with STAT4, which may account for species specific differences observed in type I interferon responses (12). Within the ECD, human IFN-alpha / beta R2 shares 63%, 60%, and 48% aa sequence identity with bovine, mouse, and ovine IFN-alpha / beta R2, respectively.
- Langer, J.A. et al. (2004) Cytokine Growth Factor Rev. 15:33.
- Pestka, S. et al. (2004) Immunol. Rev. 202:8.
- Lamken, P. et al. (2004) J. Mol. Biol. 341:303.
- Arduini, R.M. et al. (1999) Prot. Sci. 8:1867.
- Lutfalla, G. et al. (1995) EMBO J. 14:5100.
- Novick, D. et al. (1995) J. Leukocyte Biol. 57:712.
- Pfeffer, L.M. et al. (1997) J. Biol. Chem. 272:11002.
- Gazziola, C. et al. (2005) Int. J. Oncol. 26:129.
- Kotenko, S.V. and S. Pestka (2000) Oncogene 19:2557.
- Saleh, A.Z.M. et al. (2004) Oncogene 23:7076.
- McKenna, S.D. et al. (2004) J. Interferon Cytokine Res. 24:119.
- Tyler, D.R. et al. (2007) Mol. Immunol. 44:1864.
Citations for Recombinant Human IFN-alpha/beta R2 Fc Chimera Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Human Interferon-ε and interferon-? exhibit low potency and low affinity for cell surface IFNAR and the poxvirus antagonist B18R
Authors: BD Harris, J Schreiter, M Chevrier, JL Jordan, MR Walter
J. Biol. Chem., 2018-08-31;0(0):.
Species: Human
Sample Types: Protein, Whole Cells
Applications: Bioassay -
Systems-based analysis of RIG-I-dependent signalling identifies KHSRP as an inhibitor of RIG-I receptor activation
Authors: S Soonthornv, A Rodriguez-, Y Zhou, F Galvez, NJ Huffmaster, S Tripathi, VR Balasubram, A Inoue, E de Castro, H Moulton, DA Stein, MT Sánchez-Ap, PD De Jesus, Q Nguyen, R König, NJ Krogan, A García-Sas, SM Yoh, SK Chanda
Nat Microbiol, 2017-03-01;2(0):17022.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Novaferon, a novel recombinant protein produced by DNA-shuffling of IFN-alpha, shows antitumor effect in vitro and in vivo.
Authors: Li M, Rao C, Pei D, Wang L, Li Y, Gao K, Wang M, Wang J
Cancer Cell Int, 2014-01-27;14(1):8.
Applications: Surface Plasmon Resonance
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