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Recombinant Human IFN-alpha I/IFN17 Protein, CF

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Recombinant Human IFN-alpha1 Protein (Catalog # 11082-IF) demonstrates anti-viral activity in HeLa human cervical epithelial carcinoma cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is ...read more
2 μg/lane of Recombinant Human IFN‑ alpha 1 Protein (Catalog # 11082-IF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IFN-alpha I/IFN17 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 1.00-20.0 pg/mL.
Source
Human embryonic kidney cell, HEK293-derived human IFN-alpha I protein
Cys24-Asp189
Accession #
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 I/IFN17 Protein, CF

  • IFNA
  • IFNA17
  • IFNalpha I
  • IFN-alpha I
  • IFN-alpha-17
  • IFN-alphaI
  • INFA
  • interferon alpha-17
  • Interferon alpha-88
  • Interferon alpha-I'
  • Interferon alpha-T
  • interferon alpha-WA
  • interferon, alpha 17
  • LeIF I
  • LEIF2C1

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). There is not a mouse homolog for IFNA17, but mature human IFNA17 shares 58% aa sequence identity with chimpanzee IFNA17. 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 (8). IFNA17 has been shown to be potent against HIV-1 activity (9). Human IFNA17 is the only IFNA subtype identified with antiviral activity but a reduced ability to activate NK cells (10). A mutation in IFNA17, Ile184Arg, is associated with an increased risk for cervical cancer (11).
  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. Lavender, K.J. et al. (2016) J Virol. 90:6001.
  10. Ortaldo, J.R. et al. (1984) PNAS 81:4926.
  11. Kim, J.W. et al. (2003) Cancer Lett. 189:183.

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