Recombinant Human IFN-alpha B2/IFNA8 Protein, CF

Recombinant Human IFN-alpha B2/IFNA8 Protein (Catalog # 11018-IF) demonstrates anti-viral activity in HeLa human cervical epithelial carcinoma cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is 1.20-12.0 pg/mL

2 μg/lane of Recombinant Human IFN-alpha B2/IFNA8 Protein (Catalog # 11018-IF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 23-27 kDa.

• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IFN-alpha B2/IFNA8 Protein, CF Summary

• Details of Functionality: Measured in anti-viral assays using HeLa human cervical epithelial carcinoma cells infected with encephalomyocarditis (EMC) virus. Meager, A. (1987) in Lymphokines and Interferons, a Practical Approach. Clemens, M.J. et al. (eds): IRL Press. 129. The ED₅₀ for this effect is 1.20-12.0 pg/mL.
• Source: Human embryonic kidney cell, HEK293-derived IFN-alpha B2/IFNA8 protein
  Cys24-Glu189
• Accession #: P32881.1
• N-terminal Sequence: Cys24
• 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:
  • Bioactivity
• Theoretical MW: 19 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: 23-27 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 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 Human IFN-alpha B2/IFNA8 Protein, CF

• IFNA8
• IFN-alpha 8
• IFNalpha B2
• IFN-alpha B2
• IFN-alpha-8
• IFN-alphaB
• interferon alpha type 201
• interferon alpha-8
• Interferon alpha-B
• interferon alpha-B'
• Interferon alpha-B2
• interferon, alpha 8
• LeIF B

Background

Interferons (IFN) are a family of cytokines with potent antiviral, antiproliferative and immunomodulatory properties, classified based on their binding specificity to cell surface receptors (1). Human IFNA2 was originally cloned in the early ‘80s and now more than a dozen closely related IFN alpha subtypes have been identified in both the human and mouse genome, each sharing about 80% amino acid (aa) sequence homology (2-4). Structurally, type I IFNs belong to the class of five helical-bundle cytokines, with the IFNA subtypes containing 2 conserved disulfide bonds (5). The extracellular domain (ECD) of mature human IFNA8, also known as IFN‑alpha B2, shares 60% aa sequence identity with mouse homolog. The type I IFNs bind to the interferon alpha receptor (IFNAR), which consists of two subunits: IFNAR1 (alpha-subunit) and IFNAR2 (beta -subunit) (6, 7). Individual IFNA subtypes are known to display unique efficacies to viral protection, and IFNA8 is the most potent IFNA, judging by both antiviral and antiproliferative activities (8). The reason for this higher potency is unstructured tail region of IFNA8 that gains structure during complex formation and might explain the differences in activity between IFNAs (8). IFNA8 has been shown to exhibit antiproliferative and cytotoxic effects on renal cancer cell (RCC) lines and chronic myelogenous leukemia (CML)-derived cell lines (9, 10).

1. Pestka, S. et al. (1987) Annu. Rev. Biochem. 56:727.
2. Goeddel, D.V. et al. (1980) Nature 287:411.
3. Matsumiya, T. et al. (2007) J. Immunol. 179:4542.
4. Schreiber, G. and J. Piehler (2015) Trends Immunol. 36:139.
5. Wittling, M.C. et al. (2021) Front Immunol. 11:605673.
6. van Pesch, V. et al. (2004) J. Virol. 78:8219.
7. James, C.M. et al. (2007) Vaccine. 25(10):1856.
8. Slutzki, M. et al. (2006) J Mol Biol. 360:1019.
9. Yanai, Y. et al. (2002) Cancer Letter 185:173.
10. Yanai, Y. et al. (2001) J. Interferon Cytokine Res 21:1129.

Bioinformatics

• Uniprot:
  • P32881.1()