Recombinant Human Interferon alpha/beta receptor 1 protein
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Recombinant Human Interferon alpha/beta receptor 1 protein is a Human Fragment protein, in the 28 to 436 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
IFNAR, IFNAR1, Interferon alpha/beta receptor 1, IFN-R-1, IFN-alpha/beta receptor 1, Cytokine receptor class-II member 1, Cytokine receptor family 2 member 1, Type I interferon receptor 1, CRF2-1
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
IFNAR1 partners with interferon alpha receptor 2 (IFNAR2) to form a functional receptor complex. This complex binds interferons alpha and beta triggering signal transduction cascades vital for antiviral defense. Through this interaction IFNAR1 facilitates cellular immune responses including the activation of antiviral genes and modulation of cell proliferation. IFNAR1's role extends beyond immediate immune response influencing processes like cell differentiation and apoptosis.
Pathways
IFNAR1 is a participant in the JAK-STAT signaling pathway a significant pathway for transmitting cytokine signals. Upon interferon binding it activates the associated Janus kinases (JAKs) which in turn phosphorylate signal transducers and activators of transcription (STATs) specifically STAT1 and STAT2. This chain of events results in the transcription of interferon-stimulated genes that provide antiviral defenses and promote immune regulation. IFNAR1's engagement in these pathways makes it an integral part of immune system communication.
Specifications
Form
Lyophilized
General info
Function
Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed : 10049744, PubMed : 14532120, PubMed : 15337770, PubMed : 2153461, PubMed : 21854986, PubMed : 24075985, PubMed : 31270247, PubMed : 33252644, PubMed : 35442418, PubMed : 7813427). Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response (PubMed : 10049744, PubMed : 21854986, PubMed : 7665574). Mechanistically, type I interferon-binding brings the IFNAR1 and IFNAR2 subunits into close proximity with one another, driving their associated Janus kinases (JAKs) (TYK2 bound to IFNAR1 and JAK1 bound to IFNAR2) to cross-phosphorylate one another (PubMed : 21854986, PubMed : 32972995, PubMed : 7665574, PubMed : 7813427). The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (PubMed : 21854986, PubMed : 32972995, PubMed : 7526154, PubMed : 7665574, PubMed : 7813427). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (PubMed : 19561067, PubMed : 21854986, PubMed : 32972995, PubMed : 7665574, PubMed : 7813427, PubMed : 9121453). Can also act independently of IFNAR2 : form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity).
Sequence similarities
Belongs to the type II cytokine receptor family.
Post-translational modifications
Ubiquitinated, leading to its internalization and degradation (PubMed:14532120, PubMed:15337770). Polyubiquitinated via 'Lys-48'-linked and 'Lys-63'-linked ubiquitin chains, leading to receptor internalization and lysosomal degradation (PubMed:18056411). The 'Lys-63'-linked ubiquitin chains are cleaved off by the BRISC complex (PubMed:24075985).. Phosphorylated on tyrosine residues in response to interferon-binding: phosphorylation by TYK2 tyrosine kinase creates docking sites for STAT proteins (PubMed:10049744, PubMed:7526154). Phosphorylated on serine residues in response to interferon binding; this promotes interaction with FBXW11 and ubiquitination (PubMed:14532120, PubMed:15337770, PubMed:24075985).. Palmitoylation at Cys-463 is required for the activation of STAT1 and STAT2.
Subcellular localisation
Late endosome
Target data
Product promise
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