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 ...read more
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 ...read more
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
>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.
Publications
Read Publication using 11018-IF in the following applications:
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).
Pestka, S. et al. (1987) Annu. Rev. Biochem. 56:727.
Goeddel, D.V. et al. (1980) Nature 287:411.
Matsumiya, T. et al. (2007) J. Immunol. 179:4542.
Schreiber, G. and J. Piehler (2015) Trends Immunol. 36:139.
Wittling, M.C. et al. (2021) Front Immunol. 11:605673.
van Pesch, V. et al. (2004) J. Virol. 78:8219.
James, C.M. et al. (2007) Vaccine. 25(10):1856.
Slutzki, M. et al. (2006) J Mol Biol. 360:1019.
Yanai, Y. et al. (2002) Cancer Letter 185:173.
Yanai, Y. et al. (2001) J. Interferon Cytokine Res 21:1129.
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