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Mouse Anti-IFNAR1 Recombinant Antibody (MAR1-5A3) (CBMAB-1022-LY)

This product is mouse antibody recognizes mouse IFNAR-1. The antibody MAR1-5A3 immunoassay techniques such as: Blocking, WB.
See all IFNAR1 antibodies
Published Data
Fig. 1 IFNAR1 expression analyzed by flow cytometry on IEC or LPL fractions harvested from wild-type or Ifnar1-/- mice.
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Fig. 2 Immunoprecipitation of 129/SvEv splenic lysates (1 × 10⁸ cells/lane) using 5 μg of individual MAR1 mAb or control Ig plus protein G sepahrose. Protein was visualized with biotin-conjugated MAR1-5A3.
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Fig.1 Hemotoxylin and eosin stained sections of rear ankle joints obtained from animals receiving α-IFNAR1 antibody.
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Summary

Host Animal
Mouse
Specificity
Mouse
Clone
MAR1-5A3
Antibody Isotype
IgG1
Application
Blocking, WB

Basic Information

Specificity
Mouse
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Interferon Alpha And Beta Receptor Subunit 1
Introduction
Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1. Functions in general as heterodimer with IFNAR2. Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves. Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway.
Entrez Gene ID
15975
UniProt ID
P33896
Alternative Names
Ifar; Ifrc; Ifnar; Infar
Function
Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1 (PubMed:2153461, PubMed:7665574, PubMed:10049744, PubMed:14532120, PubMed:15337770, PubMed:21854986).

Functions in general as heterodimer with IFNAR2 (PubMed:7665574, PubMed:10049744, PubMed:21854986).

Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves (PubMed:7665574, PubMed:21854986, PubMed:32972995).

Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity).
Biological Process
Cellular response to interferon-alpha Source: UniProtKB
Cytokine-mediated signaling pathway Source: GO_Central
Positive regulation of cellular respiration Source: ARUK-UCL
Receptor signaling pathway via JAK-STAT Source: ProtInc
Response to lipopolysaccharide Source: UniProtKB
Response to virus Source: ProtInc
Type I interferon signaling pathway Source: UniProtKB
Cellular Location
Isoform 1: Lysosome; Cell membrane; Late endosome. Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes.
Topology
Extracellular: 28-436
Helical: 437-457
Cytoplasmic: 458-557
PTM
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 serine residues in response to interferon binding; this promotes interaction with FBXW11 and ubiquitination (PubMed:14532120, PubMed:15337770, PubMed:24075985). Phosphorylated on tyrosine residues by TYK2 tyrosine kinase (PubMed:7526154). Phosphorylated on tyrosine residues in response to interferon (PubMed:10049744).
Palmitoylation at Cys-463 is required for the activation of STAT1 and STAT2.

Abolhassani, H., Landegren, N., Bastard, P., Materna, M., Modaresi, M., Du, L., ... & Pan-Hammarström, Q. (2022). Inherited IFNAR1 deficiency in a child with both critical COVID-19 pneumonia and multisystem inflammatory syndrome. Journal of Clinical Immunology, 42(3), 471-483.

Khanmohammadi, S., Rezaei, N., Khazaei, M., & Shirkani, A. (2022). A case of autosomal recessive interferon alpha/beta receptor alpha chain (IFNAR1) deficiency with severe COVID-19. Journal of clinical immunology, 1-6.

Bastard, P., Hsiao, K. C., Zhang, Q., Choin, J., Best, E., Chen, J., ... & Casanova, J. L. (2022). A loss-of-function IFNAR1 allele in Polynesia underlies severe viral diseases in homozygotes. Journal of Experimental Medicine, 219(6), e20220028.

Bastard, P., Manry, J., Chen, J., Rosain, J., Seeleuthner, Y., AbuZaitun, O., ... & Zhang, S. Y. (2021). Herpes simplex encephalitis in a patient with a distinctive form of inherited IFNAR1 deficiency. The Journal of clinical investigation, 131(1).

Xu, F., Wang, H., Tian, J., & Xu, H. (2021). Down-regulation of ID2-AS1 alleviates the neuronal injury induced by 1-methy1-4-phenylpyridinium in human neuroblastoma cell line SH-SY5Y cells through regulating miR-199a-5p/IFNAR1/JAK2/STAT1 Axis. Neurochemical Research, 46, 2192-2203.

Shemesh, M., Lochte, S., Piehler, J., & Schreiber, G. (2021). IFNAR1 and IFNAR2 play distinct roles in initiating type I interferon–induced JAK-STAT signaling and activating STATs. Science signaling, 14(710), eabe4627.

Saminathan, M., Singh, K. P., Vineetha, S., Maity, M., Biswas, S. K., Manjunathareddy, G. B., ... & Mertens, P. P. C. (2020). Virological, immunological and pathological findings of transplacentally transmitted bluetongue virus serotype 1 in IFNAR1-blocked mice during early and mid gestation. Scientific Reports, 10(1), 2164.

Tian, J., Kang, H., Huang, J., Li, Z., Pan, Y., Li, Y., ... & Qu, L. (2020). Feline calicivirus strain 2280 p30 antagonizes type I interferon-mediated antiviral innate immunity through directly degrading IFNAR1 mRNA. PLoS Pathogens, 16(10), e1008944.

Hernandez, N., Bucciol, G., Moens, L., Le Pen, J., Shahrooei, M., Goudouris, E., ... & Bossuyt, X. (2019). Inherited IFNAR1 deficiency in otherwise healthy patients with adverse reaction to measles and yellow fever live vaccines. Journal of Experimental Medicine, 216(9), 2057-2070.

Zhang, G., Deweerd, N. A., Stifter, S. A., Liu, L., Zhou, B., Wang, W., ... & Feng, C. G. (2018). A proline deletion in IFNAR1 impairs IFN-signaling and underlies increased resistance to tuberculosis in humans. Nature communications, 9(1), 1-9.

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For research use only. Not intended for any clinical use.

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