|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:100|
|Western Blot (WB)||1:500-1:1000|
|Tested Species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic phosphopeptide derived from human IRF-3 around the phosphorylation site of Ser385 (G-A-SP-S-L)|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.4, with 50% glycerol, 150mM NaCl|
|Contains||0.02% sodium azide|
IRF-3 can inhibit cell growth and plays a critical role in controlling the expression of genes in the innate immune response. In unstimulated cells, IRF-3 is present in the cytoplasm. Viral infection results in phosphorylation of IRF-3 and leads to its translocation to the nucleus where it activates promoters containing IRF-3-binding sites. Phosphorylation of IRF-3 occurs at a cluster of C-terminal Ser and Thr residues (between 385 and 405), leading to its association with the p300/CBP coactivator protein that promotes DNA binding and transcriptional activity. During infection, IRF-3 is likely activated through a pathway that includes activation of Toll-like receptors and a kinase complex that includes IKK epsilon and TBK1. IRF-3 is phosphorylated at Ser396 following viral infection, expression of viral nucleocapsid, and double-stranded RNA treatment. These events likely play a role in activation of IRF-3.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Interferon regulatory factor 3; IRF-3; IRF3
Gene Aliases: C920001K05Rik; IIAE7; IRF-3; IRF3
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