Recombinant Human IFN-alpha 21/IFNA21 Protein, CF

Recombinant Human IFN-alpha 21/IFNA21 Protein (Catalog # 11159-IF) demonstrates anti-viral activity in HeLa human cervical epithelial carcinoma cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is 1.00-30.0 pg/mL.

2 μg/lane of Recombinant Human IFN-alpha 21/IFNA21 Protein (Catalog # 11159-IF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 18-22 kDa, under reducing conditions.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IFN-alpha 21/IFNA21 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 1.00-30.0 pg/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human IFN-alpha 21/IFNA21 protein
  Cys24-Glu189
• Accession #: P01568.2
• 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: 18-22 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 21/IFNA21 Protein, CF

• IFNA21
• IFN-alpha 21
• IFNalpha F
• IFN-alpha F
• IFN-alpha-21
• IFN-alphaI
• interferon alpha-21
• Interferon alpha-F
• interferon, alpha 21
• LeIF F
• leukocyte interferon protein
• MGC126687
• MGC126689

Background

Interferons (IFN) are a family of cytokines with potent antiviral, anti-proliferative 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). There is not a mouse homolog for IFNA21, but mature human IFNA21 is identical to chimpanzee IFNA21. 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, with IFNA21 displaying intermediate activity inducing interferon stimulating genes (8). Further, human IFNA21 has shown weak anti-viral activity against viruses such as metapneumovirus (9).

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. Moll, H.P. et al. (2011) Cytokine. 53:52.
9. George, J. and Mattapallil, J.J. (2018) Frontiers in immunology 9:299.

Bioinformatics

• Uniprot:
  • P01568.2()