IFN-alpha/beta R2 Protein, Human (Biotinylated, HEK293, His)

IFN-alpha/beta R2, one of the subunit of IFN-α/β receptor, is a type I IFN receptor. IFN-alpha/beta R2 forms the heterodimeric receptor with IFNAR1, and binds to type I IFNs^[1]. IFN-alpha/beta R2 also interacts with JAK1 and leads to tyrosine phosphorylation of the IFNARs and STAT proteins^[2]. Upon activation by these IFNs, IFNAR1 and IFN-alpha/beta R2 undergo a conformational change to promote a cascade of downstream signaling events, including the phosphorylation of Tyk2 and JAK1, STAT1 and STAT2^[3]. IFN-alpha/beta R2 Protein, Human (Biotinylated, HEK293, His) is a recombinant biotinylated human IFN-alpha/beta R2 (I27-K243) with C-terminal His tag, which is produced in HEK293 cells.

IFN-alpha/beta R2, one of the subunit of IFN-α/β receptor, is a type I IFN receptor. IFN-alpha/beta R2 is expressed on peripheral blood B cells and monocytes, and mediates differentiation and activation of these cells^[4].
IFN-alpha/beta R2 forms the heterodimeric receptor (IFN-α/β receptor) together with IFNAR1. IFNs such as IFN-α/-β can induce association of the IFNAR1 and IFN-alpha/beta R2, which makes JAK1 and TYK2 form a functional signaling unit^[1]. Upon activation by these IFNs, IFNAR1 and IFN-alpha/beta R2 undergo a conformational change to promote a cascade of downstream signaling events. The signaling events includes the phosphorylation of Tyk2 and JAK1, the signal transducers and activators of transcription STAT1 and STAT2, and the formation of the IFN-stimulated gene factor 3 (ISGF3) complex which consists of phosphorylated STAT1 and STAT2 and IRF9^[3]. IFNAR2 is critical for anti-viral immunity^[5].
Human IFN-alpha/beta R2 consists of extracellular domain (I27-K243), helical domain (I244-L264), and cytoplasmic domain (K265-R515). The sequence of amino acids in IFN-alpha/beta R2 differs in different species. Human IFN-alpha/beta R2 shares <50% aa sequence identity with mouse.
IFN-alpha/beta R2 mediates IFN-induced tyrosine phosphorylation of the IFNARs and STAT proteins, and activates the JAK-STAT signaling cascade^[1]

IFN-alpha/beta R2 (human, 3 μg/mL, 4 h) down-regulates the production of IL-17 and IFN-γ in PBMCs^[6].
IFN-alpha/beta R2 (human, 1 ng/mL, 4 h) reduces the cell proliferation rate in PBMCs^[6].

Human

HEK293

C-His

P48551-1 (I27-K243)

3455  [NCBI]

Extracellular Domain

Biotin

ISYDSPDYTDESCTFKISLRNFRSILSWELKNHSIVPTHYTLLYTIMSKPEDLKVVKNCANTTRSFCDLTDEWRSTHEAYVTVLEGFSGNTTLFSCSHNFWLAIDMSFEPPEFEIVGFTNHINVMVKFPSIVEEELQFDLSLVIEEQSEGIVKKHKPEIKGNMSGNFTYIIDKLIPNTNYCVSVYLEHSDEQAVIKSPLKCTLLPPGQESESAESAK

Approximately 43.04 kDa

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.

• [1]. Zanin N, et al. Interferon Receptor Trafficking and Signaling: Journey to the Cross Roads. Front Immunol. 2021 Jan 20;11:615603.  [Content Brief]

  [2]. Shemesh M, et al. IFNAR1 and IFNAR2 play distinct roles in initiating type I interferon-induced JAK-STAT signaling and activating STATs. Sci Signal. 2021 Nov 23;14(710):eabe4627.  [Content Brief]

  [3]. Jun Zou, et al. Chapter 7 - Antiviral Immunity: Origin and Evolution in Vertebrates. The Evolution of the Immune System. 2016,Pages 173-204.

  [4]. Pogue SL, et al. The receptor for type I IFNs is highly expressed on peripheral blood B cells and monocytes and mediates a distinct profile of differentiation and activation of these cells. J Interferon Cytokine Res. 2004 Feb;24(2):131-9.  [Content Brief]

  [5]. Duncan CJ, et al. Human IFNAR2 deficiency: Lessons for antiviral immunity. Sci Transl Med. 2015 Sep 30;7(307):307ra154.  [Content Brief]

  [6]. Hurtado-Guerrero I, et al. Immunomodulatory and Antiproliferative Activities of Recombinant Soluble IFNAR2 without IFN-β Mediation. J Clin Med. 2020 Mar 31;9(4):959.  [Content Brief]