Recombinant Cyno/Rhesus IFN-alpha/beta R2 Fc Protein, CF Summary
Details of Functionality |
Measured by its ability to inhibit Type-I IFN-mediated anti-viral activity. The ED 50 for this effect is 0.500-3.50 μg/mL in the presence of 30 pg/mL of Recombinant Human IFN‑ beta
(Catalog #
8499-IF). |
Source |
Chinese Hamster Ovary cell line, CHO-derived IFN-alpha/beta R2 protein Cyno/Rhesus IFN-alpha R2 (Ile 27-Lys243) Accession # XP_005548871.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
|
Structure / Form |
Disulfide-linked homodimer
|
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 |
51.4 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 |
75 - 95 kDa, 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. |
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 Cyno/Rhesus IFN-alpha/beta R2 Fc Protein, CF
Background
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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