Recombinant Human IFNAR2 Protein (C-Fc)

Beta LifeScience SKU/CAT #: BL-2334NP
BL-2334NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
BL-2334NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Recombinant Human IFNAR2 Protein (C-Fc)

Beta LifeScience SKU/CAT #: BL-2334NP
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Product Overview

Description Recombinant Human Interferon Alpha/Beta Receptor 2 is produced by our Mammalian expression system and the target gene encoding Ile27-Lys243 is expressed with a human IgG1 Fc tag at the C-terminus.
Accession P48551
Synonym Interferon Alpha/Beta Receptor 2; IFN-R-2; IFN-Alpha Binding Protein; IFN-Alpha/Beta Receptor 2; Interferon Alpha Binding Protein; Type I Interferon Receptor 2; IFNAR2; IFNABR; IFNARB
Gene Background Interferon α/β Receptor 2 (IFN-α/β R2) is a single-pass type I membrane protein which belongs to the type II cytokine receptor family. It complexes with IFN-α/β R1 to form the signaling receptor complex for the family of α and β IFN subtypes. By alternative splicing, IFN-α/β R2 can exist as a secreted soluble protein or as a type I membrane protein. IFN-α/β R2 is the principal ligand binding subunit of the receptor. Ligand binding is stabilized by the subsequent association with IFN-α/β R1, resulting in the formation of a signaling ternary receptor complex. IFNAR2 was detected in most lymphocytes, monocytes, and granulocytes, although IFNAR2 expression was higher in the monocytes and granulocytes than in the lymphocytes. Among the lymphocyte subsets, IFNAR2 showed high expression in natural killer (NK) cells and low expression in T lymphocytes. Isoform 1 and isoform 3 of IFNAR2 are directly involved in signal transduction due to their interaction with the TYR kinase, JAK1. Isoform 1 also interacts with the transcriptional factors, STAT1 and STAT2. Both forms are potent inhibitors of type I IFN activity.
Molecular Mass 51.8 KDa
Apmol Mass 67-75 KDa, reducing conditions
Formulation Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity Not tested
Reconstitution Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage For Research Use Only

Target Details

Target Function Associates with IFNAR1 to form the plasma membrane receptor in the type I interferon signaling pathway. Directly involved in signal transduction through its association with the TYR kinase JAK1. Involved in interferon-mediated STAT1, STAT2 and STAT3 activation.; Potent inhibitor of type I IFN receptor activity.
Subcellular Location [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; [Isoform 3]: Secreted.
Protein Families Type II cytokine receptor family
Database References
Associated Diseases Immunodeficiency 45 (IMD45)
Tissue Specificity Isoform 3 is detected in the urine (at protein level). Expressed in blood cells. Expressed in lymphoblastoid and fibrosarcoma cell lines.

Gene Functions References

  1. The findings underline the roles of UL36USP-IFNAR2 interaction in counteracting the type I IFN-mediated signaling pathway and reveal a novel evasion mechanism of antiviral innate immunity by HSV-1. PMID: 29997210
  2. Report lowered serum IFNAR2 levels in multiple sclerosis patients are elevated on treatment with interferon-beta. PMID: 27613121
  3. this study shows that the surface expression levels of the common IFN-alpha/beta receptor subunit 2 are significantly higher on plasmacytoid dendritic cells from females in comparison to males PMID: 27891600
  4. A very small percentage of the pancreatic tumors showed strong expression of the IFNAR-2c. PMID: 25072284
  5. Lack of expression of functional IFNAR2 does not seem to be the major cause of interferon resistance in hepatitis C virus patients receiving standard interferon therapy. PMID: 26176069
  6. The effects of two functional polymorphisms, type I interferon receptor 2 gene (IFNAR2)-F8S and interleukin-10 receptor subunit beta gene (IL10RB)-K47E, on chronic hepatitis B virus (HBV) infection, were investigated. PMID: 23745570
  7. IFNAR2 overexpression was observed in various histological types of lung cancer, and appears to be associated with lung cancers that behave aggressively. PMID: 22236545
  8. In this study we have characterized the Stat2-IFNaR2 interaction and examined its role in IFNalpha signaling PMID: 11786546
  9. STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c PMID: 12105218
  10. Expression and signaling activity of interferon alpha/beta receptors modulates dendritic cell (DC) responsiveness during terminal maturation and differentiation of monocyte-derived DCs. PMID: 12218119
  11. Subunit 2 of the interferon alpha receptor (IFNaR2) is bound more avidly to Stat2 than is phosphorylated IFNaR1. PMID: 12220192
  12. Administration as a complex with sIFNAR-2 may provide a method of enhancing the delivery and effectiveness of type I interferons in Burkitt lymphoma in scid mice. PMID: 14980076
  13. IFNaR2, a subunit of the type I IFN receptor, is proteolytically cleaved in a regulated manner. PMID: 15286706
  14. Dynamics of the IFNAR2 extracellular domain binding site reveal highly flexible loop segments and a malleable binding surface interacting with the IFN ligand supported by a more rigid scaffold which stabilizes the binding site conformation. PMID: 15287740
  15. A dynamic model for the IFN-alpha/receptor complex predicts that IFNAR2 and IFNAR1 are probably anchored in close proximity on the cell surface and that upon IFN binding, the complex assumes a closed form, resulting in activation of intracellular kinases. PMID: 15449939
  16. IFNaR2 intracellular domain transcriptional modulation is dependent upon the carboxyl-terminal transactivation domain of Stat2. PMID: 15717316
  17. Rapid inhibition of MAPK signaling and anti-proliferation effect via JAK/STAT signaling by interferon-alpha in hepatocellular carcinoma cell lines. PMID: 16054712
  18. Oveexpression of IFNAR2 is associated with hepatocellular carcinoma PMID: 16106266
  19. Hepatic IFNAR2c mRNA expression appears to correlate inversely with the fibrosis stage and age in hepatitis C infection. PMID: 16518956
  20. Monocyte-derived dendritic cells can modulate their sensitivity to two IFN subtypes by differential regulation of the IFNAR subunits. PMID: 16624932
  21. IFNAR2 cytoplasmic domain serves to link STAT4 to the IFNAR as a pre-assembled complex that facilitates cytokine-driven STAT4 activation. PMID: 17095088
  22. binding of IFN-alpha8 rather than binding of IFN-alpha2 to IFNAR-2 leads to activation and subsequent antiproliferative activity despite the same antiviral activity in renal cell carcinoma PMID: 17572016
  23. The intensity and distribution of IFNAR-2 may predict the response to therapy with IFN-alpha and IFN-beta in pancreatic cancer. PMID: 17667505
  24. High IFNAR2 is associated with renal cell carcinoma metastasis PMID: 17697365
  25. Results demonstrated that FNAR2-extracellular domain interact differentially with two individual IFN-alphas, suggesting the mutual interaction between multiple IFN-alpha subtypes during the competition for binding to the receptor. PMID: 18027911
  26. The data suggest that liberation of the IFNaR2-ICD by regulated proteolysis could trigger a novel mechanism for moving the transcription factor Stat2 to the nucleus. PMID: 18456457
  27. The Stat3-activating Tyk2 V678F mutant does not up-regulate signaling through the type I interferon receptor but confers ligand hypersensitivity to a homodimeric receptor PMID: 18456658
  28. Findings show that interferon-alpha/beta receptor (IFNAR)-2 isoforms are important regulators of the responsiveness to endogenous and systemically administered interferon beta (IFNbeta). PMID: 18971450
  29. Results suggest that zinc, especially polaprezinc, enhances the expression of type 1 interferon 2 receptor in U937 cells, thereby inducing production of the anti-viral protein 2'-5'OAS. PMID: 19362011
  30. Ep-CAM is a potentially useful marker for resistance to INFalpha/5-FU therapy, especially in IFNAR2-positive cases. PMID: 19401692
  31. The IFNAR2-8SS genotype was associated with HBeAg negative patients; IFNAR2-8F allele was associated with the risk to high viral loads; the IFNAR2-8FF genotype predisposed to higher MxA gene induction and correlated with sustained IFN response. PMID: 19714778


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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