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stat5 inhibitor stat5 (MedChemExpress)

Name: stat5 inhibitor stat5
Brand: MedChemExpress
Rating: 94 (39 reviews)

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MedChemExpress stat5 inhibitor stat5

ELF5 regulate casein synthesis in GMECs. (A, B) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, phosphorylated JAK2 and <t>STAT5</t> after transfection with pcDNA3.1-ELF5 or pcDNA3.1-NC for 48 h. (C, D) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, p-JAK2, and p-STAT5 after transfection with siRNA-ELF5 or siRNA-NC (100 nM) for 48 h. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. * p<0.05, ** p<0.01. siRNA, small interfering ribonucleic acid; NC, negative control; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Stat5 Inhibitor Stat5, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 39 article reviews

stat5 inhibitor stat5 - by Bioz Stars, 2026-02

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1) Product Images from "ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway"

Article Title: ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway

Journal: Animal Bioscience

doi: 10.5713/ab.25.0181

ELF5 regulate casein synthesis in GMECs. (A, B) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, phosphorylated JAK2 and STAT5 after transfection with pcDNA3.1-ELF5 or pcDNA3.1-NC for 48 h. (C, D) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, p-JAK2, and p-STAT5 after transfection with siRNA-ELF5 or siRNA-NC (100 nM) for 48 h. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. * p<0.05, ** p<0.01. siRNA, small interfering ribonucleic acid; NC, negative control; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Figure Legend Snippet: ELF5 regulate casein synthesis in GMECs. (A, B) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, phosphorylated JAK2 and STAT5 after transfection with pcDNA3.1-ELF5 or pcDNA3.1-NC for 48 h. (C, D) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, p-JAK2, and p-STAT5 after transfection with siRNA-ELF5 or siRNA-NC (100 nM) for 48 h. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. * p<0.05, ** p<0.01. siRNA, small interfering ribonucleic acid; NC, negative control; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Techniques Used: Expressing, Transfection, Quantitative Proteomics, Negative Control

The protein abundance of caseins after JAK2 and STAT5 inhibition in GMECs. (A) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, and phosphorylated JAK2 and STAT5 after JAK2 inhibitor Tyrphosting AG490 (30 μM) treatment for 48 h. (B) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, and p-STAT5 after STAT5 inhibitor STAT5-IN-1 (50 μM) treatment for 48 h. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. ** p<0.01. GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Figure Legend Snippet: The protein abundance of caseins after JAK2 and STAT5 inhibition in GMECs. (A) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, and phosphorylated JAK2 and STAT5 after JAK2 inhibitor Tyrphosting AG490 (30 μM) treatment for 48 h. (B) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, and p-STAT5 after STAT5 inhibitor STAT5-IN-1 (50 μM) treatment for 48 h. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. ** p<0.01. GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Techniques Used: Quantitative Proteomics, Inhibition, Expressing

ELF5 mediates casein synthesis by STAT5 activity in GMECs. (A) Cells were treated with STAT5-IN-1 (50 μM) or DMSO, followed by pcDNA3.1-ELF5 or pcDNA3.1-NC transfection for 48 h. (B) Cells were treated with STAT5-IN-1 (50 μM) or DMSO, followed by siRNA-ELF5 or siRNA-NC (100 nM) transfection for 48 h. The protein abundances of αS1-casein, αS2-casein, β-casein, κ-casein, and p-STAT5 were detected. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-STAT5 was normalized to total STAT5. Values are presented as mean±SEM. a–d Different lowercase letters represent significant differences (* p<0.05). siRNA, small interfering ribonucleic acid; NC, negative control; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Figure Legend Snippet: ELF5 mediates casein synthesis by STAT5 activity in GMECs. (A) Cells were treated with STAT5-IN-1 (50 μM) or DMSO, followed by pcDNA3.1-ELF5 or pcDNA3.1-NC transfection for 48 h. (B) Cells were treated with STAT5-IN-1 (50 μM) or DMSO, followed by siRNA-ELF5 or siRNA-NC (100 nM) transfection for 48 h. The protein abundances of αS1-casein, αS2-casein, β-casein, κ-casein, and p-STAT5 were detected. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-STAT5 was normalized to total STAT5. Values are presented as mean±SEM. a–d Different lowercase letters represent significant differences (* p<0.05). siRNA, small interfering ribonucleic acid; NC, negative control; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Techniques Used: Activity Assay, Transfection, Quantitative Proteomics, Negative Control

ELF5 mediates casein synthesis by JAK2 and STAT5 activity in GMECs. (A) Cells were treated with Tyrphosting AG490 (30 μM) or DMSO, followed by pcDNA3.1-ELF5 or pcDNA3.1-NC transfection for 48 h. (B) Cells were treated with Tyrphosting AG490 (30 μM) or DMSO, followed by siRNA-ELF5 or siRNA-NC (100 nM) transfection for 48 h. The protein abundances of αS1-casein, αS2-casein, β-casein, κ-casein, p-JAK2, and p-STAT5 were detected. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. a–d Different lowercase letters represent significant differences (* p<0.05). NC, negative control; siRNA, small interfering ribonucleic acid; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Figure Legend Snippet: ELF5 mediates casein synthesis by JAK2 and STAT5 activity in GMECs. (A) Cells were treated with Tyrphosting AG490 (30 μM) or DMSO, followed by pcDNA3.1-ELF5 or pcDNA3.1-NC transfection for 48 h. (B) Cells were treated with Tyrphosting AG490 (30 μM) or DMSO, followed by siRNA-ELF5 or siRNA-NC (100 nM) transfection for 48 h. The protein abundances of αS1-casein, αS2-casein, β-casein, κ-casein, p-JAK2, and p-STAT5 were detected. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. a–d Different lowercase letters represent significant differences (* p<0.05). NC, negative control; siRNA, small interfering ribonucleic acid; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Techniques Used: Activity Assay, Transfection, Quantitative Proteomics, Negative Control

The interaction between ELF5 and STAT5 in GMECs. (A) Cells were transfected with ELF5-MYC and STAT5-FLAG for 48 h. Then, total protein of cells was extracted and incubated with MYC (or FLAG) tag antibody and protein G magnetic beads at 4°C overnight. The protein abundance of ELF5 and STAT5 was detected. (B) The mRNA expression of STAT5a and ELF5 gene was measured after pCMV-STAT5a and pCMV-NC transfection for 48 h. Values are presented as mean±SEM. ** p<0.01. GMECs, goat mammary epithelial cells; NC, negative control; SEM, standard error of the mean.

Figure Legend Snippet: The interaction between ELF5 and STAT5 in GMECs. (A) Cells were transfected with ELF5-MYC and STAT5-FLAG for 48 h. Then, total protein of cells was extracted and incubated with MYC (or FLAG) tag antibody and protein G magnetic beads at 4°C overnight. The protein abundance of ELF5 and STAT5 was detected. (B) The mRNA expression of STAT5a and ELF5 gene was measured after pCMV-STAT5a and pCMV-NC transfection for 48 h. Values are presented as mean±SEM. ** p<0.01. GMECs, goat mammary epithelial cells; NC, negative control; SEM, standard error of the mean.

Techniques Used: Transfection, Incubation, FLAG-tag, Magnetic Beads, Quantitative Proteomics, Expressing, Negative Control

Molecular mechanism of ELF5 promotes casein synthesis by enhancing the activity of JAK2/STAT5 signaling pathway in goat mammary epithelial cells. PRLR stands for prolactin receptor.

Figure Legend Snippet: Molecular mechanism of ELF5 promotes casein synthesis by enhancing the activity of JAK2/STAT5 signaling pathway in goat mammary epithelial cells. PRLR stands for prolactin receptor.

Techniques Used: Activity Assay

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Journal: Animal Bioscience

Article Title: ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway

doi: 10.5713/ab.25.0181

Figure Lengend Snippet: ELF5 regulate casein synthesis in GMECs. (A, B) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, phosphorylated JAK2 and STAT5 after transfection with pcDNA3.1-ELF5 or pcDNA3.1-NC for 48 h. (C, D) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, p-JAK2, and p-STAT5 after transfection with siRNA-ELF5 or siRNA-NC (100 nM) for 48 h. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. * p<0.05, ** p<0.01. siRNA, small interfering ribonucleic acid; NC, negative control; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Article Snippet: For the inhibition of JAK2/STAT5 pathway, JAK2 inhibitor AG490 (30 μM, MedChemExpress) or STAT5 inhibitor STAT5-IN-1 (50 μM, MedChemExpress) were treated with cells.

Techniques: Expressing, Transfection, Quantitative Proteomics, Negative Control

Journal: Animal Bioscience

Article Title: ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway

doi: 10.5713/ab.25.0181

Figure Lengend Snippet: The protein abundance of caseins after JAK2 and STAT5 inhibition in GMECs. (A) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, and phosphorylated JAK2 and STAT5 after JAK2 inhibitor Tyrphosting AG490 (30 μM) treatment for 48 h. (B) The expression of αS1-casein, αS2-casein, β-casein, κ-casein, and p-STAT5 after STAT5 inhibitor STAT5-IN-1 (50 μM) treatment for 48 h. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. ** p<0.01. GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Article Snippet: For the inhibition of JAK2/STAT5 pathway, JAK2 inhibitor AG490 (30 μM, MedChemExpress) or STAT5 inhibitor STAT5-IN-1 (50 μM, MedChemExpress) were treated with cells.

Techniques: Quantitative Proteomics, Inhibition, Expressing

Journal: Animal Bioscience

Article Title: ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway

doi: 10.5713/ab.25.0181

Figure Lengend Snippet: ELF5 mediates casein synthesis by STAT5 activity in GMECs. (A) Cells were treated with STAT5-IN-1 (50 μM) or DMSO, followed by pcDNA3.1-ELF5 or pcDNA3.1-NC transfection for 48 h. (B) Cells were treated with STAT5-IN-1 (50 μM) or DMSO, followed by siRNA-ELF5 or siRNA-NC (100 nM) transfection for 48 h. The protein abundances of αS1-casein, αS2-casein, β-casein, κ-casein, and p-STAT5 were detected. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-STAT5 was normalized to total STAT5. Values are presented as mean±SEM. a–d Different lowercase letters represent significant differences (* p<0.05). siRNA, small interfering ribonucleic acid; NC, negative control; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Article Snippet: For the inhibition of JAK2/STAT5 pathway, JAK2 inhibitor AG490 (30 μM, MedChemExpress) or STAT5 inhibitor STAT5-IN-1 (50 μM, MedChemExpress) were treated with cells.

Techniques: Activity Assay, Transfection, Quantitative Proteomics, Negative Control

Journal: Animal Bioscience

Article Title: ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway

doi: 10.5713/ab.25.0181

Figure Lengend Snippet: ELF5 mediates casein synthesis by JAK2 and STAT5 activity in GMECs. (A) Cells were treated with Tyrphosting AG490 (30 μM) or DMSO, followed by pcDNA3.1-ELF5 or pcDNA3.1-NC transfection for 48 h. (B) Cells were treated with Tyrphosting AG490 (30 μM) or DMSO, followed by siRNA-ELF5 or siRNA-NC (100 nM) transfection for 48 h. The protein abundances of αS1-casein, αS2-casein, β-casein, κ-casein, p-JAK2, and p-STAT5 were detected. The relative protein abundance of αS1-casein, αS2-casein, β-casein, and κ-casein was normalized to β-tubulin. The relative protein abundance of p-JAK2 and p-STAT5 was normalized to total JAK2 and STAT5, respectively. Values are presented as mean±SEM. a–d Different lowercase letters represent significant differences (* p<0.05). NC, negative control; siRNA, small interfering ribonucleic acid; GMECs, goat mammary epithelial cells; SEM, standard error of the mean.

Article Snippet: For the inhibition of JAK2/STAT5 pathway, JAK2 inhibitor AG490 (30 μM, MedChemExpress) or STAT5 inhibitor STAT5-IN-1 (50 μM, MedChemExpress) were treated with cells.

Techniques: Activity Assay, Transfection, Quantitative Proteomics, Negative Control

Journal: Animal Bioscience

Article Title: ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway

doi: 10.5713/ab.25.0181

Figure Lengend Snippet: The interaction between ELF5 and STAT5 in GMECs. (A) Cells were transfected with ELF5-MYC and STAT5-FLAG for 48 h. Then, total protein of cells was extracted and incubated with MYC (or FLAG) tag antibody and protein G magnetic beads at 4°C overnight. The protein abundance of ELF5 and STAT5 was detected. (B) The mRNA expression of STAT5a and ELF5 gene was measured after pCMV-STAT5a and pCMV-NC transfection for 48 h. Values are presented as mean±SEM. ** p<0.01. GMECs, goat mammary epithelial cells; NC, negative control; SEM, standard error of the mean.

Article Snippet: For the inhibition of JAK2/STAT5 pathway, JAK2 inhibitor AG490 (30 μM, MedChemExpress) or STAT5 inhibitor STAT5-IN-1 (50 μM, MedChemExpress) were treated with cells.

Techniques: Transfection, Incubation, FLAG-tag, Magnetic Beads, Quantitative Proteomics, Expressing, Negative Control

Journal: Animal Bioscience

Article Title: ELF5 modulates casein synthesis in goat mammary epithelial cells via JAK2/STAT5 signaling pathway

doi: 10.5713/ab.25.0181

Figure Lengend Snippet: Molecular mechanism of ELF5 promotes casein synthesis by enhancing the activity of JAK2/STAT5 signaling pathway in goat mammary epithelial cells. PRLR stands for prolactin receptor.

Article Snippet: For the inhibition of JAK2/STAT5 pathway, JAK2 inhibitor AG490 (30 μM, MedChemExpress) or STAT5 inhibitor STAT5-IN-1 (50 μM, MedChemExpress) were treated with cells.

Techniques: Activity Assay

a , Schematic representation of the metabolic pathway of IRG1-related metabolites. b, Heatmap indicates the relative levels of itaconate and its related metabolites in CM derived from BP-TAM and control macrophages in the untargeted metabolomic analysis. c, RT-qPCR analysis of IRG1 expression in THP-1-Mφ and 436-TAMs. Data are presented as mean ± s.d.; unpaired Student’s t-test; n = 3. d, Western blot analysis of IRG1 protein expression in THP-1-Mφ and 436-TAMs. e, RT-qPCR analysis of IRG1 expression in BMDMs and BP-TAMs. Data are presented as mean ± s.d.; unpaired Student’s t-test; n = 3. f, Western blot analysis of IRG1 protein expression in BMDMs and BP-TAMs. g, GSEA of RNA-seq data from BMDMs and BP-TAMs. h,i, Western blot analysis of STAT5 and phosphorylated STAT5 (p-STAT5) expression in THP-1-Mφ, 436-TAMs, BMDMs, and BP-TAMs. j, Western blot analysis of IRG1 protein expression in THP-1-Mφ and 436-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. The inhibitors were used at the following concentrations: STAT3-IN-1 (10 μM), STAT5-IN-1 (100 μM), and pyrrolidinedithiocarbamate ammonium (PDTC, 10 μM). k, RT-qPCR analysis of IRG1 mRNA expression in THP-1-Mφ and 436-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. Fold changes and P values in IRG1 mRNA levels in TAMs relative to THP-1-Mφ are shown. The inhibitors were used at the same concentrations as in ( j ). l, Western blot analysis of IRG1 protein expression in BMDMs and BP-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. The inhibitors were used at the same concentrations as in ( j ). m, RT-qPCR analysis of IRG1 mRNA expression in BMDMs and BP-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. Fold changes and P values in IRG1 mRNA levels in TAMs relative to BMDMs are shown. The inhibitors were used at the same concentrations as in ( j ).

Journal: bioRxiv

Article Title: IRG1/itaconate/NRF2/GSH axis in tumor-associated macrophages drives therapy resistance and immune evasion in BRCA1-deficient breast cancer

doi: 10.1101/2025.10.14.682312

Figure Lengend Snippet: a , Schematic representation of the metabolic pathway of IRG1-related metabolites. b, Heatmap indicates the relative levels of itaconate and its related metabolites in CM derived from BP-TAM and control macrophages in the untargeted metabolomic analysis. c, RT-qPCR analysis of IRG1 expression in THP-1-Mφ and 436-TAMs. Data are presented as mean ± s.d.; unpaired Student’s t-test; n = 3. d, Western blot analysis of IRG1 protein expression in THP-1-Mφ and 436-TAMs. e, RT-qPCR analysis of IRG1 expression in BMDMs and BP-TAMs. Data are presented as mean ± s.d.; unpaired Student’s t-test; n = 3. f, Western blot analysis of IRG1 protein expression in BMDMs and BP-TAMs. g, GSEA of RNA-seq data from BMDMs and BP-TAMs. h,i, Western blot analysis of STAT5 and phosphorylated STAT5 (p-STAT5) expression in THP-1-Mφ, 436-TAMs, BMDMs, and BP-TAMs. j, Western blot analysis of IRG1 protein expression in THP-1-Mφ and 436-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. The inhibitors were used at the following concentrations: STAT3-IN-1 (10 μM), STAT5-IN-1 (100 μM), and pyrrolidinedithiocarbamate ammonium (PDTC, 10 μM). k, RT-qPCR analysis of IRG1 mRNA expression in THP-1-Mφ and 436-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. Fold changes and P values in IRG1 mRNA levels in TAMs relative to THP-1-Mφ are shown. The inhibitors were used at the same concentrations as in ( j ). l, Western blot analysis of IRG1 protein expression in BMDMs and BP-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. The inhibitors were used at the same concentrations as in ( j ). m, RT-qPCR analysis of IRG1 mRNA expression in BMDMs and BP-TAMs treated with inhibitors of STAT3, STAT5, and NF-κB. Fold changes and P values in IRG1 mRNA levels in TAMs relative to BMDMs are shown. The inhibitors were used at the same concentrations as in ( j ).

Article Snippet: The following small-molecule compounds, metabolites, inhibitors, and neutralizing antibodies were used in this study: olaparib (HY-10162, MedChemExpress), L-glutathione reduced (GSH; G4251, Sigma-Aldrich, St. Louis, MO, USA), N-acetyl-L-cysteine (NAC; A7250, Sigma-Aldrich), L-(+)-lactic acid (L1750, Sigma-Aldrich), sodium L-lactate (71718, Sigma-Aldrich), itaconic acid (T4837, TargetMol, Wellesley Hills, MA, USA), citraconic acid (C82604, Sigma-Aldrich), 4-octyl itaconate (4-OI; SML2338, Sigma-Aldrich), dimethyl itaconate (DMI; T5377, TargetMol), dimethyl citraconate (DMC; C0346, TCI America, Portland, OR, USA), DL-buthionine-sulfoximine (BSO; 19176, Sigma-Aldrich), sodium oxamate (LDHi; O2751, Sigma-Aldrich), STAT5-IN-1 (S6784, Selleck Chemicals, Houston, TX, USA), STAT3-IN-1 (S0818, Selleck Chemicals), pyrrolidinedithiocarbamate ammonium (PDTC; S3633, Selleck Chemicals), RSL3 (S8155, Selleck Chemicals), Ferrostatin-1 (Fer-1; S7243, Selleck Chemicals), ML385 (T4360, TargetMol), and IRG1-IN-1 (T78525, TargetMol).

Techniques: Derivative Assay, Control, Quantitative RT-PCR, Expressing, Western Blot, RNA Sequencing

STAT5-dependent activation of the IRG1/itaconate pathway in TAMs reprograms mitochondrial metabolism and activates NRF2-driven GSH biosynthesis. The TAM-derived GSH protects tumor cells from ROS-induced DNA damage and ferroptosis, while concurrently suppressing STING-mediated immune activation in both tumor and dendritic cells. Pharmacological inhibition of IRG1 restores tumor sensitivity to PARPi, reactivates anti-tumor immunity, and significantly suppresses tumor growth in BRCA1-deficient preclinical models.

Journal: bioRxiv

Article Title: IRG1/itaconate/NRF2/GSH axis in tumor-associated macrophages drives therapy resistance and immune evasion in BRCA1-deficient breast cancer

doi: 10.1101/2025.10.14.682312

Figure Lengend Snippet: STAT5-dependent activation of the IRG1/itaconate pathway in TAMs reprograms mitochondrial metabolism and activates NRF2-driven GSH biosynthesis. The TAM-derived GSH protects tumor cells from ROS-induced DNA damage and ferroptosis, while concurrently suppressing STING-mediated immune activation in both tumor and dendritic cells. Pharmacological inhibition of IRG1 restores tumor sensitivity to PARPi, reactivates anti-tumor immunity, and significantly suppresses tumor growth in BRCA1-deficient preclinical models.

Techniques: Activation Assay, Derivative Assay, Inhibition

CAG inhibits neutrophil chemoattraction-related NF-κB and STAT signaling pathway activity. (A,B) Molecular simulation diagrams and interaction tables between CAG and the STAT5B receptor; (C–E) ELISA was used to analyze the effects of CAG and STAT5 inhibitor on the expression of TGF-β1, CXCL3, and CCL5 in LLC cells (N = 3). (F–H) qPCR analysis of the effects of CAG and STAT5 inhibitor on the expression of TGF-β1, CXCL3, and CCL5 in LLC cells ( N = 3). Data are presented as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001.

Journal: Frontiers in Medicine

Article Title: The research on cycloastragenol in the treatment of brain metastases from lung cancer: mechanistic exploration of radiotherapy sensitization and amelioration of brain injury

doi: 10.3389/fmed.2025.1616894

Figure Lengend Snippet: CAG inhibits neutrophil chemoattraction-related NF-κB and STAT signaling pathway activity. (A,B) Molecular simulation diagrams and interaction tables between CAG and the STAT5B receptor; (C–E) ELISA was used to analyze the effects of CAG and STAT5 inhibitor on the expression of TGF-β1, CXCL3, and CCL5 in LLC cells (N = 3). (F–H) qPCR analysis of the effects of CAG and STAT5 inhibitor on the expression of TGF-β1, CXCL3, and CCL5 in LLC cells ( N = 3). Data are presented as mean ± SEM. * p < 0.05; ** p < 0.01; *** p < 0.001.

Article Snippet: (1) Cycloastragenol (source leaf), physiological sodium chloride solution (Fengyuan), T-25, T-75 sterile culture bottle, Trypsin (Biosharp), 1% streptomycin (Biosharp), 4% paraformaldehyde (Biosharp), 1 × PBS (Biosharp), DMEM medium (Gibco), 1,640 medium (Gibco), Fetal bovine serum (ExCell), Puromycin (Biosharp) pasteurized straw, 1 mL disposable sterile syringe, 10 mL round-bottomed capped centrifuge tube (Biosharp), 1.5 mL sharp-bottomed centrifuge tube (Biosharp), STAT5 inhibitor (STAT5-IN-1, HY-101853, MCE). (2) Ki67 (Servicebio, GB111141 ), CD31 (Servicebio, GB11063-1), Ly6G (Servicebio, GB11229), Iba-1 (PTG, 26177-1-ap), CD16 (ABCam, ab183685), CD206 (CD206, ab182422) was used for IF. (3) Mouse kits for ELISA: TGF-β1 (ruixinbio RX104768H), CXCL3 (ruixinbio RX101460H), CCL5 (ruixinbio RX105344H). (4) PCR reagent: RNA extract (Xavier, G3013), Chloroform substitute (Xavier, G3014), Isopropanol (Xavier, 80109218), Reverse Transcription Kit (Xavier, G3337). (5) Antibodies required for brain transplantation tumor experiment: InVivoMab anti-mouse Ly6G (BE0075-1.

Techniques: Activity Assay, Enzyme-linked Immunosorbent Assay, Expressing

The signal pathways involved in IL-15-induced innate cytotoxicity of CD38 + HLA-DR + CD8 + T cells. (A) 1 × 10 6 CD8 + T cells from healthy donors were stimulated with IL-15 (20 ng/mL) for 48 h and 72 h, after which phosphorylation of signaling proteins was assessed by flow cytometry for STAT5 ( n = 10), ERK1/2 ( n = 7) and mTOR ( n = 8). Representative dot plots and the summary data show the expression of signaling proteins in CD38 + HLA-DR + CD8 + T cells. (B) The percentage of CD38 + HLA-DR + CD8 + T cells was analyzed after inhibitors treatment ( n = 4). Representative dot plots from a single donor (left) and summary data (right) are presented. (C-G) The percentage NKG2D, FasL, perforin, and Granzyme B in CD38 + HLA-DR + CD8 + T cells were analyzed after inhibitors treatment ( n = 4). (H) CD8 + T cells from healthy donors were pre-treated with STAT5 inhibitor pimozide, MEK inhibitor PD98059, PI3K inhibitor LY294002 or mTOR inhibitor PP242, followed by IL-15 (20 ng/mL) stimulation for the next 72 h. Then, CD8 + T cells were co-cultured with CFSE-labeled K562 cells at a 10:1 E: T ratio and cytotoxicity against K562 cells evaluated ( n = 4). Representative dot plots and the summary data show expression of PI in the gate of CFSE + . (I) Schematic representation of cytokine-mediated crosstalk between T cells and liver cells in liver cirrhosis. The Wilcoxon matched-pairs signed rank test (A) was used for comparisons among groups. The one-way ANOVA (B , C , D-H) was used for comparisons between groups. Control group was indicated treatment only IL-15. ns, not significant, * p < 0.05, ** p < 0.01.

Journal: Scientific Reports

Article Title: IL-15-Activated CD38 + HLA-DR + CD8 + T cells induce liver injury in cirrhosis via JAK/STAT5 and PI3K/mTOR pathways

doi: 10.1038/s41598-025-02693-6

Figure Lengend Snippet: The signal pathways involved in IL-15-induced innate cytotoxicity of CD38 + HLA-DR + CD8 + T cells. (A) 1 × 10 6 CD8 + T cells from healthy donors were stimulated with IL-15 (20 ng/mL) for 48 h and 72 h, after which phosphorylation of signaling proteins was assessed by flow cytometry for STAT5 ( n = 10), ERK1/2 ( n = 7) and mTOR ( n = 8). Representative dot plots and the summary data show the expression of signaling proteins in CD38 + HLA-DR + CD8 + T cells. (B) The percentage of CD38 + HLA-DR + CD8 + T cells was analyzed after inhibitors treatment ( n = 4). Representative dot plots from a single donor (left) and summary data (right) are presented. (C-G) The percentage NKG2D, FasL, perforin, and Granzyme B in CD38 + HLA-DR + CD8 + T cells were analyzed after inhibitors treatment ( n = 4). (H) CD8 + T cells from healthy donors were pre-treated with STAT5 inhibitor pimozide, MEK inhibitor PD98059, PI3K inhibitor LY294002 or mTOR inhibitor PP242, followed by IL-15 (20 ng/mL) stimulation for the next 72 h. Then, CD8 + T cells were co-cultured with CFSE-labeled K562 cells at a 10:1 E: T ratio and cytotoxicity against K562 cells evaluated ( n = 4). Representative dot plots and the summary data show expression of PI in the gate of CFSE + . (I) Schematic representation of cytokine-mediated crosstalk between T cells and liver cells in liver cirrhosis. The Wilcoxon matched-pairs signed rank test (A) was used for comparisons among groups. The one-way ANOVA (B , C , D-H) was used for comparisons between groups. Control group was indicated treatment only IL-15. ns, not significant, * p < 0.05, ** p < 0.01.

Article Snippet: CD8 + T cells (1 × 10 6 ) from healthy donors were pre-treated with STAT5 inhibitor pimozide, PI3K inhibitor LY294002 or mTOR inhibitor PP242, followed by IL-15 (20 ng/mL) (Thermo, MA, USA) stimulation for the next 72 h. All the inhibitors were obtained from MedChemExpress (NJ, USA).

Techniques: Phospho-proteomics, Flow Cytometry, Expressing, Cell Culture, Labeling, Control

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