Our Anti-Interferon-α Receptor, Type I, Subunit I (Ser535,539) rabbit polyclonal phosphospecific primary antibody from PhosphoSolutions is produced in-house. It detects human Interferon-α Receptor, Type I, Subunit I (Ser535,539) and is antigen affinity purified from pooled serum. It is great for use in WB.
Primary Antibody
Human
Bovine, Canine, Non-Human Primate, Mouse, Rat, Sheep
WB
Rabbit
Antigen Affinity Purified from Pooled Serum
IFNAR1
110-130 kDa

Western blot of immunoprecipitates from HEK 293 cells transfected with 1) Mock, 2) IFNAR1 WT, and 3) IFNAR1 S535A and S539A mutants. Specific immunolabeling of the ~110 kDa to ~130 kDa IFNAR1 WT (2) is shown in the first blot, as the immunolabeling is absent in IFNAR1 Ser535 and Ser539 mutants (3). The specific immunolabeling is blocked by the phosphopeptide (+) used as the antigen in the second blot.
Product Specific References for Applications and Species
Western Blot: Human | ||
PMID | Dilution | Publication |
21865166 | not listed | Zheng, H., et al. 2011. Tyrosine phosphorylation of protein kinase D2 mediates ligand-inducible elimination of the Type 1 interferon receptor. Journal of Biological Chemistry, 286(41), pp.35733-35741. |
21695243 | not listed | Qian, J., et al. 2011. Pathogen recognition receptor signaling accelerates phosphorylation-dependent degradation of IFNAR1. PLoS Pathog, 7(6), p.e1002065. |
21540188 | not listed | Bhattacharya, S., et al. 2011. Role of p38 protein kinase in the ligand-independent ubiquitination and down-regulation of the IFNAR1 chain of type I interferon receptor. Journal of Biological Chemistry, 286(25), pp.22069-22076. |
19948722 | not listed | Bhattacharya, S., et al. 2010. Inducible priming phosphorylation promotes ligand-independent degradation of the IFNAR1 chain of type I interferon receptor. J Biol Chem. 285(4):2318-25. |
19805514 | not listed | Liu, J., et al. 2009. Mammalian casein kinase 1α and its leishmanial ortholog regulate stability of IFNAR1 and type I interferon signaling. Molecular and cellular biology, 29(24), pp.6401-6412. |
15337770 | not listed | Kumar, K.G., et al. 2004. Phosphorylation and Specific Ubiquitin Acceptor Sites Are Required for Ubiquitination and Degradation of the IFNAR1 Subunit of Type I Interferon Receptor. J. Biol. Chem., Nov 2004; 279: 46614 - 46620. |
Western Blot: Human | ||
PMID | Dilution | Publication |
21695243 | not listed | Qian, J., et al. 2011. Pathogen recognition receptor signaling accelerates phosphorylation-dependent degradation of IFNAR1. PLoS Pathog, 7(6), p.e1002065. |
21540188 | not listed | Bhattacharya, S., et al. 2011. Role of p38 protein kinase in the ligand-independent ubiquitination and down-regulation of the IFNAR1 chain of type I interferon receptor. Journal of Biological Chemistry, 286(25), pp.22069-22076. |
19805514 | not listed | Liu, J., et al. 2009. Mammalian casein kinase 1α and its leishmanial ortholog regulate stability of IFNAR1 and type I interferon signaling. Molecular and cellular biology, 29(24), pp.6401-6412. |
Product Specific Protocols
- Western Blot Protocol: Download