recombinant murine il 22 protein (R&D Systems)
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recombinant murine il 22 protein
Recombinant Murine Il 22 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+mouse+il+22/Recombinant+Mouse+IL-22+Protein/pmc12955021-42-0-10
Average 94 stars, based on 42 article reviews
Recombinant Murine Il 22 Protein, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/recombinant+mouse+il+22/Recombinant+Mouse+IL-22+Protein/pmc12955021-42-0-10
Average 94 stars, based on 42 article reviews
recombinant murine il 22 protein - by Bioz Stars,
2026-10
94/100 stars
Images
1) Product Images from "Low-dose 5-hydroxymethylfurfural mitigates radiation -induced intestinal toxicity via HIF2α-driven IL22/STAT3 signaling enhancement"
Article Title: Low-dose 5-hydroxymethylfurfural mitigates radiation -induced intestinal toxicity via HIF2α-driven IL22/STAT3 signaling enhancement
Journal: Journal of Translational Medicine
doi: 10.1186/s12967-026-07757-3
Figure Legend Snippet: Low-dose 5-HMF sensitizes intestinal crypts to IL-22‒STAT3 signaling and enhances organoid growth. ( A , B ) organoid formation assay. Crypts isolated from control or low-dose 5-HMF-treated mice were cultured with recombinant murine IL-22 (rmIL22; 50 ng/mL) for 3 days. Representative time-lapse images ( A ) and quantification of the organoid surface area (μm 2 ) from day 1 to day 3 after cultivation ( B ) are shown. ( C ) comparison of organoid growth stimulated by rmIL22 and CHIR99021 (3 μM), a Wnt/β-catenin agonist. Representative images of MTT-stained organoids. ( D ) MTT viability analysis (% positive, n = 6 wells/group). ( E , F ) immunoblot analysis ( E ) and quantification ( F ) of STAT3 phosphorylation (Tyr705) in organoids treated with or without rmIL22 (50 ng/mL, 48 h). The data are presented as the mean±SD. Statistical significance compared with the regular diet group. * p < 0.05, ** p < 0.01 and NS, no significant difference
Techniques Used: Tube Formation Assay, Isolation, Control, Cell Culture, Recombinant, Comparison, Staining, Western Blot, Phospho-proteomics
Figure Legend Snippet: 5-HMF upregulates IL-22 receptor expression through HIF-dependent transcriptional activation. ( A , B ) expression of IL-22 receptor subunits in intestinal crypts. ( A ) mRNA and ( B ) protein levels of IL22R1 and IL10R2 in mice treated with vehicle, low-dose (50 mg/kg), or high-dose (100 mg/kg) 5-HMF. ( C ) Bioinformatics analysis of the IL22R1 promoter region. The schematic illustrates the positions of four putative hypoxia response elements (HREs; consensus core sequence) within the murine IL22R1 locus. Supporting evidence from publicly available human ChIP-seq data (GEO database) is shown below. The track labeled “Batch4_CHROM1_LOVO_EPAS1_RABBIT” visualizes HIF-2α (encoded by EPAS1) binding sites on chromosome 1 in the LOVO human colon epithelial cell line (experimental batch 4; rabbit antibody). The prominent peak (red box) indicates significant enrichment of HIF-2α binding within the upstream regulatory region of the human IL22R1 gene, supporting its status as a direct transcriptional target under HIF-mediated regulation. ( D ) mouse IL22R1 promoter scheme showing distal (−1525~-1449 bp) and proximal (+36 ~ +74 bp) HERs identified by sequence analysis. ( E ) dual-luciferase reporter assay in HEK-293 cells with an IL22R1 promoter-luciferase construct containing a wild-type sequence (−2000 wt) or mutations of distal or/and proximal HERs with transactivation by HIF-1, HIF-2, or GFP-control plasmids ( n = 3 transfections/group). Asterisks (*) indicate the comparison of HIF1 or HIF2 to their respective GFP controls. ** p < 0.01, * p < 0.001 and NS, no significant difference. The cross (†) indicates a comparison of the transactivation of the wild-type sequence to the sequences mutated by HIF1 (†) or by HIF2 (†). † p < 0.05. All the error bars represent the means±sds
Techniques Used: Expressing, Activation Assay, Sequencing, ChIP-sequencing, Labeling, Binding Assay, Luciferase, Reporter Assay, Construct, Control, Transfection, Comparison
Figure Legend Snippet: HIF-2α is required for 5-HMF-induced IL22R1 expression and the functional potentiation of IL-22 signaling. ( A , B ) HIF-2α inhibition abolishes 5-HMF-induced upregulation of IL22R1 at the protein level in intestinal crypts from mice treated with low-dose 5-HMF with or without the HIF-2α inhibitor PT-2385. ( C ) MTT-stained organoids were isolated from the mice in this study and cultured in medium in the presence or absence of rmIL22 and/or PT-2385 ( n = 3, 3 replicates/group). ( D ) quantification of the organoid surface area (μm 2 ×10 3 ) and MTT viability analysis (% positive, n = 6 wells/group). Statistical significance compared with the control group. * p < 0.05, ** p < 0.01, * p < 0.001 and NS, no significant difference. ( E ) schematic model summarizing the proposed mechanism by which low-dose 5-HMF mitigates radiation-induced intestinal injury. 5-HMF inhibits prolyl hydroxylase domain (PHD) enzyme activity, leading to the selective stabilization of HIF-2α in intestinal crypt cells. HIF-2α translocates to the nucleus and binds to hypoxia‒response elements (HREs) in the promoter of IL22R1, where it is upregulated. Increased IL22R1 surface expression enhances responsiveness to IL-22, leading to activation of the STAT3 signaling pathway. This promotes the proliferation and survival of intestinal stem cells (ISCs), facilitating epithelial regeneration and ultimately protecting against radiation-induced intestinal damage
Techniques Used: Expressing, Functional Assay, Inhibition, Staining, Isolation, Cell Culture, Control, Activity Assay, Activation Assay
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