|Tested species reactivity||Human, Mouse, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Synthetic phosphopeptide derived from human IRF-3 around the phosphorylation site of Serine 385|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS, pH 7.2|
|Contains||0.05% sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:200|
|Western Blot (WB)||1:500-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
This antibody detects endogenous protein at a molecular weight of 47 and 55 kDa.
Purity is >95% by SDS-PAGE.
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.