Recombinant Cyno/Rhesus IFN-alpha/beta R2 Fc Protein, CF
Recombinant Cyno/Rhesus IFN-alpha/beta R2 Fc Protein, CF Summary
Product Specifications
Cyno/Rhesus IFN-alpha R2 (Ile 27-Lys243) Accession # XP_005548871.1 | IEGRMD | Human IgG1 (Pro100-Lys330) |
N-terminus | C-terminus | |
Analysis
Ile 27
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.
10071-AB
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 500 μg/mL in 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
Recombinant Cyno/Rhesus IFN-alpha/beta R2 Fc Chimera (Catalog # 10071-AB) inhibits the anti-viral activity of (Catalog # 8499-IF) The ED50 for this effect is 0.500-3.50 µg/mL.
2 μg/lane of Recombinant Cyno/Rhesus IFN‑ alpha / beta R2 Fc Chimera (Catalog # 10071-AB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 75-95 kDa and 150-190 kDa, respectively.
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). Mature IFN-alpha / beta R2 consists of an extracellular domain (ECD), containing two fibronectin type III repeats, a transmembrane segment, and a cytoplasmic domain. Alternative splicing generates a secreted isoform that corresponds to the ECD as well as a 50 kDa transmembrane isoform with a substituted and truncated cytoplasmic region (3, 4). The short isoform is impaired in its ability to activate signaling molecules and functions as a dominant negative receptor subunit (5-7). The mature ECD of cynomolgus IFN-alpha/ beta R2 shares 93% and 100% amino acid (aa) sequence identity with that of human and rhesus, respectively. 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 (8, 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).
- Langer, J.A. et al. (2004) Cytokine Growth Factor Rev. 15:33.
- Pestka, S. et al. (2004) Immunol. Rev. 202:8.
- 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.
- Lamken, P. et al. (2004) J. Mol. Biol. 341:303.
- Arduini, R.M. et al. (1999) Prot. Sci. 8:1867.
- 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.
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