IRF-1 (D5E4) XP® Rabbit mAb #8478
- WB
- IP
- IHC
- IF
- F
- C&R
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 45-48 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
- IF-Immunofluorescence
- F-Flow Cytometry
- C&R-CUT & RUN
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| IHC Leica Bond | 1:50 |
| Immunohistochemistry (Paraffin) | 1:100 |
| Immunofluorescence (Immunocytochemistry) | 1:200 |
| Flow Cytometry (Fixed/Permeabilized) | 1:50 |
| CUT&RUN | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
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 stimulation with IFN or 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 suggests 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 USA 104, 17028-33.
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