Anti-Interferon-α Receptor, Type I, Subunit I (Ser535,539) Antibody

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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.

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.
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.
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.

Human
WB
Rabbit

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Data Sheet
Trial Size Trial Size Pooled Serum Pooled Serum

SKU: p170-5359

Volume: 100 µL
Price:
$430.00

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.

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