>Interferon (IFN) Family Proteins
Interferon (IFN) was first discovered in 1957 by Alick Isaacs and Jean Lindenmann from their initial studies in viral interference. Over the years, various studies about IFN were performed, elucidating its anti-viral activity. It was only until 1980 when IFN could be produced in a large-scale for research use, where pioneering recombinant DNA technology was utilized. IFN proteins were discovered to have both anti-tumor and immunomodulatory functions along with its inherent anti-viral activity, classifying them as a subset of cytokines.
The IFN protein family is organized into three types according to its corresponding receptor: type I, type II and type III; each of which are produced in different cellular locations. IFN-α and IFN-β are the most prominent members of type I IFNs and are mainly produced by pathogenesis-associated molecular patterns (PAMPs). PAMPs are induced by stimulation of Toll-like receptors (TLR) or cytoplasmic pattern recognition receptors located on the cell membrane. Type II IFNs have only one type, IFN-γ, which are produced by a variety of cells in the immune system. This includes innate lymphoid-like cell populations such as innate lymphocytes (ILC) and natural killer (NK) cells, as well as adaptive immune cells consisting of helper T cells 1 (Th1) and CD8 cytotoxic T lymphocytes (CTL). Type III IFNs are mainly produced by epithelial cells in non-hematopoietic cells, where viruses can mediate type III interferon expression in different cell types. However, since these IFNs were discovered in 2003, the exact mechanism of its production is still unknown and is the subject of various academic studies.
The corresponding signaling pathways of the three types of IFNs are also different, where each bind to different compositions of heterodimeric receptor complexes. Intracellular signaling is conducted through the Janus kinase/signal transducer and acts as an activator of transcription (JAK/STAT) pathways.
The main transduction pathways of the IFN signaling
Mechanism of action of a drug targeting IFN (Anifrolumab)
Due to the widespread effects of the IFN regulatory pathways, IFN is often associated with the progression of tumor diseases. In vitro studies have shown that IFN can inhibit tumor cell growth by up-regulating the cell cycle and also induce apoptosis by binding to tumor necrosis factor-related apoptosis-inducing ligands. However, in vivo studies have shown that deletion of the type I or type II interferon signaling pathway accelerates tumorigenesis and progression.
The correlation of both type I and II IFN responses to oncogenic properties has highlighted it as a significant pathway for targeted cancer drug resistance. This was observed from the resulting tumor cells after cancer therapy expressing intact or partially intact IFN signaling. As a result, a resistance to viral replication is developed, preventing targeted therapeutics from exerting its normal anti-tumor effects. To combat this, targeted therapies inhibiting JAK/STAT signaling by IFN can be a therapeutic modality to overcome resistance to therapeutic agents.
To assist with your research into the IFN protein family, ACROBiosystems provides a comprehensive catalog of high-quality IFNs to meet your needs in drug discovery, functional evaluation, quality control.
|Molecule||Cat. No.||Species||Product Description||Preorder/Order|
|IFN-alpha 1||IFA-H52H9||Human||Human IFN-alpha 1 Protein, His Tag|
|IFA-H5258||Human IFN-alpha 1 Protein, Fc Tag (MALS verified)|
|IFA-M52H3||Mouse||Mouse IFN-alpha 1 Protein, His Tag|
|IFN-alpha 2b||IFB-H5253||Human||Human IFN-alpha 2b (K46R) Protein, Fc Tag (MALS verified)|
|IFN-gamma||IFG-H4211||Human||Human IFN-gamma / IFNG Protein, premium grade|
|IFN-BM411||Biotinylated Monoclonal Anti-IFNγ antibody, Human IgG1 (13E6H4)|
|IFN-M412||Monoclonal Anti-IFNγ antibody, Human IgG1 (8C5F8)|
|IFN-M414||Monoclonal Anti-IFNγ antibody, Human IgG1 (13E6H6)|
|IFN-M411||Monoclonal Anti-IFNγ antibody, Human IgG1 (13E6H4)|
|IFN-BS138||Mouse||Biotinylated Monoclonal Anti-IFNγ antibody, Mouse IgG1 (13E6H6) (MALS verified)|
|IFN-S120||Monoclonal Anti-IFNγ antibody, Mouse IgG2a (8C5F8) (SPR verified)|
|IFN-S138||Monoclonal Anti-IFNγ antibody, Mouse IgG1 (13E6H4)|
|IFN-alpha/beta R1||IF1-H5253||Human||Human IFN-alpha / beta R1 Protein, Fc Tag|
|IF1-H5225||Human IFN-alpha / beta R1 Protein, His Tag (MALS verified)|
|IF1-M5225||Mouse||Mouse IFN-alpha / beta R1 Protein, His Tag|
|IFN-alpha/beta R2||IF2-H5224||Human||Human IFN-alpha/beta R2 Protein, His Tag (MALS verified)|
|IF2-H5255||Human IFN-alpha / beta R2 Protein, Fc Tag|
|IF2-M5225||Mouse||Mouse IFN-alpha / beta R2 Protein, His Tag|
|IFA-R52H1||Rat||Rat IFN-alpha/beta R2 Protein, His Tag|
|IFN-gamma R1||IF1-H5223||Human||Human IFN-gamma R1 / IFNGR1 Protein, His Tag|
|IF1-H5254||Human IFN-gamma R1 / IFNGR1 Protein, Fc Tag|
Human IFN-alpha 1 (Cat. No. IFA-H5258), Fc Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
The purity of Human IFN-alpha 1, Fc Tag (Cat. No. IFA-H5258) is more than 90% and the molecular weight of this protein is around 90-118 kDa verified by SEC-MALS.
Immobilized ActiveMax® Human IFN-gamma, Tag Free (Cat. No. IFG-H4211) at 5 μg/mL (100 μL/well) can bind Human IFN-gamma R1, His Tag (Cat. No. IF1-H5223) with a linear range of 0.01-0.313 μg/mL.
Loaded Human IFN-alpha 1, His Tag (Cat. No. IFA-H52H9) on HIS1K Biosensor, can bind Human IFNAR1, Fc Tag (Cat. No. IF1-H5253) with an affinity constant of 0.191 μM as determined in BLI assay (ForteBio Octet Red96e).
1. Li Q, Tan F, Wang Y, et al. The gamble between oncolytic virus therapy and IFN[J]. Frontiers in Immunology, 2022, 13.https://doi.org/10.3389/fimmu.2022.971674.
2. Zhang X, Zou M, Liang Y, et al. Arctigenin inhibits abnormal germinal center reactions and attenuates murine lupus by inhibiting IFN-I pathway[J]. European Journal of Pharmacology, 2022, 919: 174808.https://doi.org/10.1016/j.ejphar.2022.174808.
3. Barrat F J, Crow M K, Ivashkiv L B. Interferon target-gene expression and epigenomic signatures in health and disease[J]. Nature immunology, 2019, 20(12): 1574-1583.https://doi.org/10.1038/s41590-019-0466-2.
4. Felten R, Scher F, Sagez F, et al. Spotlight on anifrolumab and its potential for the treatment of moderate-to-severe systemic lupus erythematosus: evidence to date[J]. Drug design, development and therapy, 2019, 13: 1535.https://doi.org/10.2147/DDDT.S170969.
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