Product Pathways - NF-kappaB Signaling
IRF-1 Antibody #4966
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IP | H M R | Endogenous | 48 | Rabbit |
Applications Key:
W=Western Blotting
IP=Immunoprecipitation
Reactivity Key:
H=Human
M=Mouse
R=Rat
Species cross-reactivity is determined by Western blot.
Specificity / Sensitivity
IRF-1 Antibody detects endogenous levels of IRF-1. The antibody does not cross-react with other family members at physiological levels.
Source / Purification
Polyclonal antibodies are produced by immunizing rabbits with a synthetic peptide (KLH-coupled) corresponding to residues surrounding Ser149 of IRF-1. Antibodies are purified by protein A and peptide affinity chromatography.
Western Blotting
Western blot analysis of extracts from Jurkat (human), C2C12 (mouse), and NBT-II (rat) cells, using IRF-1 Antibody.
Background
Interferon regulatory factors (IRFs) comprise a family of transcription factors that function with the Jak/Stat pathway to regulate interferon (IFN) and IFN-inducible gene expression in response to viral infection (1). IRFs play an important role in the pathogen defense, autoimmunity, lymphocyte development, cell growth and susceptibility to transformation. The IRF family includes nine members: IRF-1, IRF-2, ISGF3γ/p48, IRF-3, IRF-4 (Pip/LSIRF/ICSAT), IRF-5, IRF-6, IRF-7 and IRF-8/ICSBP. All IRF proteins share homology in their amino-terminal DNA binding domains. IRF family members regulate transcription through interactions with proteins that share similar DNA binding motifs, such as IFN-stimulated response elements (ISRE), IFN consensus sequences (ICS) and IFN regulatory elements (IRF-E) (2).
The IRF-1 transcription factor was originally identified as a regulator of virus-inducible enhancer-like elements of the IFN-β gene (3). IRF-1 is widely expressed and upregulated by viral infection or interferon stimulation and other cytokines. IRF-1 is serine-phosphorylated by casein kinase II (CKII ) at two clustered sites, one in the DNA binding domain (amino acids 138-150) and another in the transactivation domain (amino acids 219-231) (4). Mutation analysis of the latter site suggest that these phosphorylation sites help regulate IRF-1 activity. Tyrosine phosphorylation has also been shown to be important in IFN-γ-mediated differentiation of myeloid cell lines (5). C-terminal SUMOylated IRF-1 inhibits apoptosis in tumor cells by repression of its transcriptional activity (6).
- Taniguchi, T. et al. (2001) Annu Rev Immunol 19, 623-55.
- Honda, K. and Taniguchi, T. (2006) Nat Rev Immunol 6, 644-58.
- Fujita, T. et al. (1988) EMBO J 7, 3397-405.
- Lin, R. and Hiscott, J. (1999) Mol Cell Biochem 191, 169-80.
- Kautz, B. et al. (2001) J Biol Chem 276, 37868-78.
- Park, J. et al. (2007) Proc Natl Acad Sci U S A 104, 17028-33.
Application References
Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know!
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This product is for in vitro research use only and is not intended for use in humans or animals. This product is not intended for use as therapeutic or in diagnostic procedures.
