B6;129S1-Il1rap^tm1Roml/J

Stock number: 003284
Product name: IL-1R AcP KO
Research areas: Cancer Research, Immunology, Inflammation and Autoimmunity Research

Description

IL-1RAcP-null (Il1rap knock-out) mice exhibit loss of IL-1 receptor mediated signal transduction. These mice may be useful in studying the role of IL-1 cytokine signaling in immune responses such as IL-33 receptor complexes and oncogenic signaling pathways (e.g., AML, CML).

Detailed description

Il1rap encodes interleukin 1 receptor accessory protein (IL-1RAcP) which is a component of the interleukin-1 receptor complex, and is involved in interleukin-1 signalling. IL-1RAcP-null mice are viable and fertile. They exhibit loss of IL-1 receptor-mediated signal transduction. Treatment of these mutant mice with IL-1 Alpha or IL-1 Beta results in no detectable increase in IL-6 levels in serum and fails to induce increased expression of E-selectin mRNA. Homozygous mice are viable with normal breeding.

Development

A targeting vector was designed to replace a genomic fragment containing exons D1 and part of D2A (the exons that encode the first Ig domain and part of the second Ig domain) of the interleukin 1 receptor accessory protein gene (Il1rap) on chromosome 16 with a neomycin resistance cassette. The construct was electroporated into 129S1/Sv-Oca2⁺ Tyr⁺ Kitl⁺-derived W9.5 embryonic stem (ES) cells. Mice are reported to be on a mixed C57BL/6;129S1 genetic background.

Allele

Symbol: Il1rap^tm1Roml
Name: targeted mutation 1, Mark A Labow
MGI accession ID: MGI:1934017
Generation method: Targeted
Attributes: Null/Knockout
Marker symbol: Il1rap
Marker name: interleukin 1 receptor accessory protein
Chromosome: 16
Strain of origin: 129S1/Sv-Oca2⁺ Tyr⁺ Kitl⁺
Molecular note: A neomycin resistance cassette replaced a genomic fragment containing exons D1 and part of D2A. These exons encode the first Ig domain and part of the second Ig domain. Northern blot analysis revealed that a truncated mRNA was produced from this allele, but equilibrium binding studies demonstrated that no protein was present on the cell surface of primary mouse embryo fibroblasts (PMEFs) derived from homozygous mice.