Recommended Dilution: WB: 1:1000 IHC: 1:1000 Quality Control: Western blots performed on each lot.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Liquid
Buffer
100 μL in 10 mM HEPES ( pH 7.5), 150 mM NaCl, 100 μg per ml BSA and 50 % glycerol.
Lagerung
-20 °C
Bhattacharya, HuangFu, Liu, Veeranki, Baker, Koumenis, Diehl, Fuchs: "Inducible priming phosphorylation promotes ligand-independent degradation of the IFNAR1 chain of type I interferon receptor." in: The Journal of biological chemistry, Vol. 285, Issue 4, pp. 2318-25, (2010) (PubMed).
Kumar, Krolewski, Fuchs: "Phosphorylation and specific ubiquitin acceptor sites are required for ubiquitination and degradation of the IFNAR1 subunit of type I interferon receptor." in: The Journal of biological chemistry, Vol. 279, Issue 45, pp. 46614-20, (2004) (PubMed).
Interferons are widely used therapeutic agents because of their anti tumor and antiviral effects and because of their modulatory effects on the immune system (Biron, 2001, Kirkwood, 2002). These cytokines produce their effects by binding to the Type 1 Interferon-a Receptor (IFNAR1). Down regulation of this receptor plays a key role in determining the magnitude and duration of cytokine signaling. This down regulation is thought to be influenced by phosphorylation of Serine 535 and 539 in the IFNAR1 (Kumar et al., 2003). Anti-Phospho Ser535,539 IFNAR1 Western blot of immunoprecipitates from HEK 293 cells transfected with 1. Mock, 2. IFNAR1 WT, and 3. IFNAR1 S535A and S539A mutants showing specific immunolabeling of the ~110k to ~130k IFNAR1 WT. The immunolabeling is absent in IFNAR1 Ser535 and Ser539 mutants (Control). The immunolabeling is blocked by the phosphopeptide (Phos) used as the antigen but not by the corresponding dephosphopeptide (Dephos).