IFNAR2 Antibody (YA9168)
(Synonyms: IFNABR, IFNARB, IFNAR2, Interferon alpha/beta receptor 2, IFN-R-2, IFN-alpha binding protein, IFN-alpha/beta receptor 2, Interferon alpha binding protein, Type I interferon receptor 2)Based on 1 Customer Validation
IFNAR2 Antibody (YA9168) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to IFNAR2.
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Host:
Mouse
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Isotype:
IgG
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Application:
WB, ICC/IF, IF-Tissue, IP, ELISA
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Reactivity :
human
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Formulation:
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% sodium azide.
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Conjugation:
Non-conjugated
Applications
| Application |
WB
WB: Western Blot
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ICC/IF
ICC/IF: Immunocytochemistry/
Immunofluorescence |
IF-Tissue
IF-Tissue: Immunofluorescence-Tissue
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IP
IP: Immunoprecipitation
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ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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|---|---|---|---|---|---|
| Dilution Ratio | 1:100-1000 | 1:50-500 | 1:50-500 | 1-2μg per 100-500μg Total protein | 1:30-3000 |
Product Details
IFNAR2 Antibody (YA9168) is a Mouse-derived and non-conjugated IgG2b monoclonal antibody, targeting to IFNAR2.
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Host Mouse
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Species Reactivityhuman
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Calculated Molecular Weight Predicted band size: 110 kDa
OMIM: 610424
A synthesized peptide derived from human IFNAR2.
Endogenous
Affinity purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS(pH7.4) containing 0.1% gelatin and < 0.1% sodium azide.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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Storage & Stability
Stored at 2-8°C for 1 year, do not freeze.
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Shipping
Shipping with blue ice.
Background
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Function
IFNAR2 is a Together with IFNAR1, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa). 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. 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. The activated kinases phosphorylate specific tyrosine residues on the intracellular domains of IFNAR1 and IFNAR2, forming docking sites for the STAT transcription factors (STAT1, STAT2 and STAT). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes[1][2][3][4][5][6][7][8][9][10][11][12][13][14][15].
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Subcellular Localization
Cell membrane
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Expression
Tissue_Specificity: Isoform 3 is detected in the urine (at protein level). Expressed in blood cells. Expressed in lymphoblastoid and fibrosarcoma cell lines. -
Isoforms & Post-Translational Modification
IFNAR2 has 3 isoforms, P48551-1: amino acid length is 515, molecular weight is 57759 Da (predicted); P48551-2: amino acid length is 331, molecular weight is 37393 Da (predicted); P48551-3: amino acid length is 239, molecular weight is 27384 Da (predicted).
Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-337 or Tyr-512 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types -
Subunit
Heterodimer with IFNAR1; forming the receptor for type I interferon.
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SwissProt ID
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Synonyms
IFNABR, IFNARB, IFNAR2, Interferon alpha/beta receptor 2, IFN-R-2, IFN-alpha binding protein, IFN-alpha/beta receptor 2, Interferon alpha binding protein, Type I interferon receptor 2
Documentation
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Data Sheet (261 KB)
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SDS (252 KB)
- English - EN (252 KB)
- Français - FR (252 KB)
- Deutsch - DE (252 KB)
- Norwegian - NO (252 KB)
- Español - ES (252 KB)
- Swedish - SV (252 KB)
- Italian - IT (252 KB)
- Korean - KR (252 KB)
- Portuguese - PT (252 KB)
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User Guide for Antibodies (1077 KB)
[1]. Russell-Harde D, et al. Formation of a uniquely stable type I interferon receptor complex by interferon beta is dependent upon particular interactions between interferon beta and its receptor and independent of tyrosine phosphorylation. Biochem Biophys Res Commun. 1999 Feb 16;255(2):539-44. [Content Brief]
[2]. Piehler J, et al. Mutational and structural analysis of the binding interface between type I interferons and their receptor Ifnar2. J Mol Biol. 1999 Nov 19;294(1):223-37. [Content Brief]
[3]. Thomas C, et al. Structural linkage between ligand discrimination and receptor activation by type I interferons. Cell. 2011 Aug 19;146(4):621-32. [Content Brief]
[4]. Duncan CJ, et al. Human IFNAR2 deficiency: Lessons for antiviral immunity. Sci Transl Med. 2015 Sep 30;7(307):307ra154. [Content Brief]
[5]. Arimoto KI, et al. STAT2 is an essential adaptor in USP18-mediated suppression of type I interferon signaling. Nat Struct Mol Biol. 2017 Mar;24(3):279-289. [Content Brief]
[6]. Zhang Q, et al. Inborn errors of type I IFN immunity in patients with life-threatening COVID-19. Science. 2020 Oct 23;370(6515):. [Content Brief]
[7]. Domanski P, et al. Cloning and expression of a long form of the beta subunit of the interferon alpha beta receptor that is required for signaling. J Biol Chem. 1995 Sep 15;270(37):21606-11. [Content Brief]
[8]. Novick D, et al. Soluble and membrane-anchored forms of the human IFN-alpha/beta receptor. J Leukoc Biol. 1995 May;57(5):712-8. [Content Brief]
[9]. Novick D, et al. The human interferon alpha/beta receptor: characterization and molecular cloning. Cell. 1994 May 6;77(3):391-400. [Content Brief]
[10]. Platanias LC, et al. Differences in interferon alpha and beta signaling. Interferon beta selectively induces the interaction of the alpha and betaL subunits of the type I interferon receptor. J Biol Chem. 1996 Sep 27;271(39):23630-3. [Content Brief]
[11]. Croze E, et al. The human type I interferon receptor. Identification of the interferon beta-specific receptor-associated phosphoprotein. J Biol Chem. 1996 Dec 27;271(52):33165-8. [Content Brief]
[12]. Kumaran J, et al. A structural basis for interferon-alpha-receptor interactions. FASEB J. 2007 Oct;21(12):3288-96. [Content Brief]
[13]. Wagner TC, et al. Interferon signaling is dependent on specific tyrosines located within the intracellular domain of IFNAR2c. Expression of IFNAR2c tyrosine mutants in U5A cells. J Biol Chem. 2002 Jan 11;277(2):1493-9. [Content Brief]
[14]. Velichko S, et al. STAT3 activation by type I interferons is dependent on specific tyrosines located in the cytoplasmic domain of interferon receptor chain 2c. Activation of multiple STATS proceeds through the redundant usage of two tyrosine residues. J Biol Chem. 2002 Sep 20;277(38):35635-41. [Content Brief]
[15]. Li X, et al. Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling. Mol Cell Biol. 1997 Apr;17(4):2048-56. [Content Brief]