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il-1 α (p026_09); recombinant human il-1alpha/il-1f1  (R&D Systems)


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    R&D Systems il-1 α (p026_09); recombinant human il-1alpha/il-1f1
    Il 1 α (P026 09); Recombinant Human Il 1alpha/Il 1f1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/il-1 α (p026_09); recombinant human il-1alpha/il-1f1/product/R&D Systems
    Average 90 stars, based on 1 article reviews
    il-1 α (p026_09); recombinant human il-1alpha/il-1f1 - by Bioz Stars, 2026-03
    90/100 stars

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    ASCT2 drives the proinflammatory SASP via <t>IL-1</t> α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 <t>α</t> <t>protein</t> was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.
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    ASCT2 drives the proinflammatory SASP via <t>IL-1</t> α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 <t>α</t> <t>protein</t> was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.
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    ASCT2 drives the proinflammatory SASP via <t>IL-1</t> α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 <t>α</t> <t>protein</t> was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.
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    ASCT2 drives the proinflammatory SASP via <t>IL-1</t> α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 <t>α</t> <t>protein</t> was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.
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    ASCT2 drives the proinflammatory SASP via <t>IL-1</t> α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 <t>α</t> <t>protein</t> was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.
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    ASCT2 drives the proinflammatory SASP via <t>IL-1</t> α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 <t>α</t> <t>protein</t> was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.
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    ASCT2 drives the proinflammatory SASP via <t>IL-1</t> α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 <t>α</t> <t>protein</t> was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.
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    ASCT2 drives the proinflammatory SASP via IL-1 α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.

    Journal: Acta Pharmaceutica Sinica. B

    Article Title: Inhibition of ASCT2 induces hepatic stellate cell senescence with modified proinflammatory secretome through an IL-1 α /NF- κ B feedback pathway to inhibit liver fibrosis

    doi: 10.1016/j.apsb.2022.03.014

    Figure Lengend Snippet: ASCT2 drives the proinflammatory SASP via IL-1 α /NF- κ B feedback loop through interacting with precursor IL-1 α at Lys82 of senescent HSCs. (A) Protein of p31–IL-1 α and p16–IL-1 α was measured by Western blot analysis with 4-OHT ( n = 3 per group). (B) Detection of intracellular IL-1 α by ELISA with 4-OHT ( n = 3 per group). (C) mRNAs of proinflammatory SASP including IL1A , IL1B , IL6 and IL8 were measured by qPCR ( n = 5 per group). (D) Co-IP of ASCT2 with IL-1 α in LX2 cells, as detected by Western blot analysis ( n = 3 per group). (E) Schematic of fragments of IL-1 α that were fused to GST (top) and were transfection into 293T cells. Binding of ASCT2 to GST-IL-1 α proteins was detected by Western blot (bottom, n = 3 per group). FL: full length; F1: domain 1–112; F2: domain 112–271; F3: NLS domain (80–88) deletion; F4: K82N mutation. (F) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and IL1R1 signaling cascade indicators were analyzed by Western blotting ( n = 3 per group). (G) rIL-1 α protein was added to senescent (ASCT2 depletion or etoposide treatment) LX2 cells, and NF- κ B protein was measured in nuclear and cytoplasmic lysates by Western blot ( n = 3 per group). (H) Relative luciferase measurement of NF- κ B in indicated cells ( n = 5–6 per group). (I) ASCT2 depletion-senescent LX2 cells were treated with rIL-1 α protein and addressed in NF- κ B inhibitor PDTC, and the analysis of mRNAs of proinflammatory SASP IL1A , IL1B , IL6 and IL8 by qPCR ( n = 5–6 per group). Bars indicate mean ± SEM; ∗ P < 0.05, ∗∗ P < 0.01; ns, no significance.

    Article Snippet: Recombinant human IL-1 α protein (200-LA, protein for addition of IL-1 α ) was purchased from Bio-Techne (R&D Systems, Shanghai, China), the concentration used is 20 ng/mL in vitro .

    Techniques: Western Blot, Enzyme-linked Immunosorbent Assay, Co-Immunoprecipitation Assay, Transfection, Binding Assay, Mutagenesis, Luciferase