Recombinant Cynomolgus Monkey IFN-alpha/beta R1 Protein, CF Summary
Additional Information |
His-tag |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When
Recombinan Cynomolgus Monkey IFN‑ alpha / beta R1 His-tag protein is immobilized at 10
µg/mL (100 µL/well), Recombinant Human IFN-A2 binds with an ED50 of 1-6 μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived cynomolgus monkey IFN-alpha/beta R1 protein Ala23-Ile439, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ala23 & Gly26 |
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 |
48 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 |
80-100 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 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 Cynomolgus Monkey IFN-alpha/beta R1 Protein, CF
Background
Interferon-alpha/beta receptor 1 (IFN-alpha / beta R1), also known as
IFNAR1, is a member of the class II cytokine receptor family of proteins. These
proteins form heterodimeric receptor complexes that mediate class II cytokine
signals and subunits of the different receptor complexes are shared and serve
multiple functions (1). Mature human IFN-alpha / beta R1 consists of an extracellular
domain (ECD) with three tandem fibronectin type III repeats, a transmembrane
segment, and a cytoplasmic domain (2). Within the ECD, human IFN-alpha / beta R1 shares
47% and 50% amino acid sequence identity with mouse and rat IFN-alpha / beta R1,
respectively. Alternative splicing generates two additional isoforms that lack
the transmembrane segment and either all or a portion of the cytoplasmic domain.
IFN-alpha / beta R1, in association with IFN-alpha / beta R2, is required for propagating
anti-microbial signal transduction triggered by the type 1 interferons such as
IFN-alpha and IFN-beta (3, 4). IFN-alpha / beta R1 interacts very weakly or not at all with
type 1 interferons and does not stably interact with IFN-alpha / beta R2. Ligands
preferentially associate with IFN-alpha / beta R2, and this complex subsequently forms a
stable ternary assembly with IFN-alpha / beta R1 (5-7). IFN-alpha / beta R1 also associates with
IFN-gamma R2 even in the absence of IFN-gamma stimulation (3). IFN-alpha / beta R1 activation
depends on tyrosine phoshorylation as well as palmitoylation of its cytoplasmic
domain (8, 9). Rapid down-regulation of the receptor is accomplished by
ligand‑dependent or -independent pathways (e.g. VEGF R signaling, TLR signaling,
or cellular stress) which induce its serine phosphorylation, ubiquitination,
and degradation (10-13).
- Langer, J.A. et al. (2004) Cytokine Growth Factor Rev. 15:33.
- Uze, G. et al. (1990) Cell 60:225.
- Hwang, S.Y. et al. (1995) Proc. Natl. Acad. Sci. USA 92:11284.
- Takaoka, A. et al. (2000) Science 288:2357.
- Lamken, P. et al. (2004) J. Mol. Biol. 341:303.
- Arduini, R.M. et al. (1999) Prot. Sci. 8:1867.
- Kalie, E. et al. (2008) J. Biol. Chem. 283:32925.
- Platanias, L.C. (2005) Nat. Rev. Immunol. 5:375.
- Claudinon, J. et al. (2009) J. Biol. Chem. 284:24328.
- Zheng, H. et al. (2011) Blood 118:4003.
- Qian, J. et al. (2011) PLoS Pathogens 7:e1002065.
- Bhattacharya, S. et al. (2010) J. Biol. Chem. 285:2318.
- Bhattacharya, S. et al. (2011) J. Biol. Chem. 286:22069.
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