Recombinant Human Universal Type I IFN Protein, CF Summary
Accession # P01563.1
Accession # CAA23799.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in PBS.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Recombinant Human Universal Type I IFN (Catalog # 11020-IF) demonstrates anti-viral activity in HeLa human cervical epithelial carcinoma cells infected with encephalomyocarditis (EMC) virus. The ED50 for this effect is 6.00‑60.0 pg/mL
2 μg/lane of Recombinant Human Universal Type I IFN Protein (Catalog # 11020-IF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 16-22 kDa.
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 universal Type I IFN is a hybrid of the N-terminal residues of IFNA-2A and C-terminal residues of IFNA-1B. 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 IFNA1 exhibits low potency, determined by both antiviral and antiproliferative activities (8). Conversely, hybrid IFNA molecules, similar to universal Type I IFN, exhibit high specific activity across multiple species (9, 10). These molecules were developed to help study the biology of the IFN system in various animal species (11). Human IFNA1 was the first IFNA to be purified and has been tested as a treatment for various diseases (12-14).
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- George, J. and Mattapallil, J.J. (2018) Front Immunol. 9:299.
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