Recombinant Mouse IFN-alpha/beta R2 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Mouse IFN‑ alpha / beta R2 Fc Chimera is immobilized at 2 μg/mL, it binds to Recombinant Mouse IFN-alpha / beta R1 (Catalog # 3039-AB) in the presence of Recombinant Mouse Limitin/IFN-zeta (Catalog # 597-LM). The concentration of rmIFN‑ alpha / beta R1 that produces 50% of the optimal binding response was found to be approximately 1-4 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse IFN-alpha/beta R2 protein
Mouse IFN-alpha / beta R2 (Met1-Ala239) with a substitution Lys160Asn Accession # NP_001103968 |
IEGRMD |
Human IgG1 (Pro100-Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Ser22 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Ifnar2 |
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 kDa (monomer). 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 |
80-95 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 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 Mouse IFN-alpha/beta R2 Fc Chimera Protein, CF
Background
IFN‑ alpha / beta R2, also known as IFNAR2, is a 100 kDa glycoprotein member of the class II cytokine receptor family. Proteins from this family form heterodimeric receptor complexes that transduce signals from the type I and II interferon, Tissue factor, IL‑10, and IL‑28/IFN‑ lambda families of cytokines (1‑3). 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 high‑affinity 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 (4, 5). Mature mouse IFN‑ alpha / beta R2 consists of a 221 aa extracellular domain (ECD) with two fibronectin type III repeats, a 21 aa transmembrane segment, and a 250 aa cytoplasmic domain. Alternate splicing generates an approximately 45 kDa secreted isoform that corresponds to the ECD (6, 7). Human 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 (8). 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 (9, 10). Complexes of the soluble receptor with IFN‑ alpha or IFN‑ beta can also exert agonistic activity in cells that lack IFN‑ alpha / beta R2 (10). 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 (11). Within the ECD, mouse IFN‑ alpha / beta R2 shares 46% and 67% aa sequence identity with human and rat 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.
- de Weerd, N.A. et al. (2007) J. Biol. Chem. 282:20053.
- Lamken, P. et al. (2004) J. Mol. Biol. 341:303.
- Arduini, R.M. et al. (1999) Protein Sci. 8:1867.
- Owczarek, C.M. et al. (1997) J. Biol. Chem. 272:23865.
- Hardy, M.P. et al. (2002) Biochem. J. 356:355.
- Saleh, A.Z.M. et al. (2004) Oncogene 23:7076.
- McKenna, S.D. et al. (2004) J. Interferon Cytokine Res. 24:119.
- Hardy, M.P. et al. (2001) Blood 97:473.
- Tyler, D.R. et al. (2007) Mol. Immunol. 44:1864.
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