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recombinant human rh cxcl11  (R&D Systems)


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    R&D Systems recombinant human rh cxcl11
    Recombinant Human Rh Cxcl11, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/recombinant+human+cxcl11/Recombinant+Human+CXCL11%2FI-TAC+Protein%2C+CF/pm40341878-423-14-17
    Average 94 stars, based on 7 article reviews
    recombinant human rh cxcl11 - by Bioz Stars, 2026-09
    94/100 stars

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    Recombinant:

    Article Title: Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation.
    Article Snippet: Interactions between chemokines and enzymes are vital in immunoregulation.. Structural protein citrullination by peptidylarginine deiminase (PAD) has been associated with autoimmunity.. In this report, we identified a novel naturally occurring posttranslational modification of chemokines, that is, the deimination of arginine at position 5 into citrulline of CXC chemokine ligand 10 (CXCL10) by rabbit PAD and human PAD2.

    Article Title: Amino acid sequences directed against chemokines and polypeptides comprising the same for the treatment of chemokine-related diseases and disorders
    Article Snippet: The cocktail was a mix of recombinant human CCL2/MCP1 (Mucin stalk Chimera) carrier free (R&D Systems, Minneapolis, Minn., US; cat nr: 979-MC/CF), recombinant human CCL3/MIP1 alpha carrier free (R&D Systems; cat nr: 270-LD/CF), recombinant human CCL5/RANTES (Mucin stalk Chimera) carrier free (R&D Systems; cat nr: 978-RN/CF), recombinant human CXCL11/I-TAC carrier free (R&D Systems; cat nr: 672-IT/CF), and recombinant human CXCL12/SDF1alpha carrier free (R&D Systems; cat nr: 350-NS/CF;)). .. The cocktail was a mix of recombinant human CCL2/MCP1 (Mucin stalk Chimera) carrier free (R&D Systems, Minneapolis, Minn., US; cat nr: 979-MC/CF), recombinant human CCL3/MIP1 alpha carrier free (R&D Systems; cat nr: 270-LD/CF), recombinant human CCL5/RANTES (Mucin stalk Chimera) carrier free (R&D Systems; cat nr: 978-RN/CF), recombinant human CXCL11/I-TAC carrier free (R&D Systems; cat nr: 672-IT/CF), and recombinant human CXCL12/SDF1alpha carrier free (R&D Systems; cat nr: 350-NS/CF;)). ..

    Article Title: Colon carcinoma cells induce CXCL11-dependent migration of CXCR3-expressing cytotoxic T lymphocytes in organotypic culture.
    Article Snippet: Adoptive immunotherapy of cancer patients with cytolytic T lymphocytes (CTL) has been hampered by the inability of the CTL to home into tumors in vivo.. Chemokines can attract T lymphocytes to the tumor site, as demonstrated in animal models, but the role of chemokines in T-lymphocyte trafficking toward human tumor cells is relatively unexplored.. In the present study, the role of chemokines and their receptors in the migration of a colon carcinoma (CC) patient’s CTL toward autologous tumor cells has been studied in a novel three-dimensional organotypic CC culture.

    Article Title: SDF-1α induces differential trafficking of CXCR4-CXCR7 involving cyclophilin A, CXCR7 ubiquitination and promotes platelet survival.
    Article Snippet: Platelet-derived SDF-1 (CXCL12) mediates inflammatory and regenerative mechanisms.. The present study characterizes the effect of SDF-1 ligation in platelets.. SDF-1 (0–100 M) dose and time dependently caused internalization of its receptor CXCR4 (28.9 1.6 vs. 16.1 1.9 in SDF-1 -treated platelets), coupled to the surface externalization of CXCR7 (65.5 8 vs. 162.8 27.6 following SDF-1 treatment), both in vitro and in vivo.

    Article Title: Colon carcinoma cells induce CXCL11-dependent migration of CXCR3-expressing cytotoxic T lymphocytes in organotypic culture
    Article Snippet: Reagents The following monoclonal antibodies (mAbs) were used: HLA-class I-specific mAb W6/32 and HLA-class II-specific mAb B33.1 and D1.B6 (obtained from Dr B. Perussia, Thomas Jefferson University, and Dr G. Trinchieri, The Wistar Institute); mAb Nok-1 to Fas ligand (PharMingen, Los Angeles, CA, USA); mAb CH-11 to CD95 and anti-CD11a mAb (Immunotech, Westbrook, ME, USA); fluoresceinated or phycoerythrin-labeled anti-CD:4, 8, 25, 29, 40, 40L, 44, 49a, 49b, 80, and 54 (PharMingen, Los Angeles, CA, USA); anti-CXCL-11 mAb; anti-human CCR:1, 2, 3, 5, 6, 7, 9, and CXCR:1, 2, 3, 4, 5, and 6 mAbs (R&D Systems, Minneapolis, MN, USA); anti-human CCR:4, 8, and 10 mAbs (Imgenex, San Diego, CA, USA); anti-CCR11 and -CX3CR1 polyclonal Abs (Abcam, Cambridge, MA, USA); fluoresceinated goat anti-mouse IgG (Molecular Probes, Eugene, OR, USA). .. Recombinant human CXCL11 was purchased from R&D Systems (Minneapolis, MN, USA). .. Generation of anti-CC CTL lines CTL020 cells were obtained from co-culture of PBMC (obtained 7 months after surgery; 10 5 cells/well of 96-well round-bottom microtiter plates) of CC patient 020 with irradiated (30,000 rads, Cs source) autologous CC cells WC020 (10 5 cells/well) in T-cell medium containing RPMI 1640 medium, 10% human AB serum (Gemini, Calabasas, CA, USA), 10 mM HEPES (Sigma-Aldrich, St Louis, MO, USA), l -arginine (116 mg/l), l -asparagine (36 mg/l), l -glutamine (216 mg/l; all from GIBCO-Invitrogen, Carlsbad, CA, USA) and 2-mercaptoethanol (5 × 10 −5 M; Sigma, Aldrict, St Louis, MO, USA), in a humidified 5% CO 2 incubator.

    Article Title: Macrophage Migration Inhibitory Factor Limits Activation-Induced Apoptosis of Platelets via CXCR7-Dependent Akt Signaling
    Article Snippet: .. These findings link the proinflammatory role of MIF with an antithrombotic effect and suggest targeting the MIF-CXCR7 interaction may be a potential strategy to control inflammation. at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from 1 Supplemental Material Materials: Recombinant murine/human/feline SDF-1α/CXCL12, recombinant human CXCL11/I-TAC (rhCXCL11), recombinant murine CXCL11/I-TAC (rmCXCL11) recombinant human MIF (rhMIF), recombinant murine MIF (rmMIF), mouse monoclonal anti-human CXCR4-PE, rat anti-mouse CXCR4-FITC, mouse anti- human/mouse CXCR7-PE, rat monoclonal anti-mouse CXCR4-unconjugated, mouse monoclonal anti-human CXCR4-unconjugated, mouse monoclonal anti-human CXCR7-unconjugated, mouse anti human CXCR2-unconjugated antibodies were procured from R&D systems. .. Rabbit polyclonal CD74-FITC, rabbit polyclonal MIF- FITC and rabbit polyclonal CXCL11-FITC were from Biorbyt, rabbit polyclonal antibody to CXCR7/GPR159 (N-term) was from Acris Antibodies, mouse monoclonal anti-MIF and rabbit anti-human CXCL11 were from Abcam, rabbit monoclonal p42/44MAPK (Erk1/2) and rabbit monoclonal phospho p42/44 MAPK (Erk1/2), rabbit monoclonal-PI3K and rabbit monoclonal-phospho-PI3K, rabbit monoclonal-Akt and rabbit monoclonal-phospho-Akt, rabbit monoclonal-phospho-BAD, rabbit monoclonal- cleaved active caspase 3-Alexa Fluor-488 conjugated antibodies were purchased from Cell Signaling Technology.

    Article Title: In vitro migration of cytotoxic T lymphocyte derived from a colon carcinoma patient is dependent on CCL2 and CCR2
    Article Snippet: The following monoclonal antibodies (mAb) were used: mAb Nok-1 to Fas ligand (BD-PharMingen, San Diego, CA); mAb CH-11 to CD95 and anti-CD11a mAb (Immunotech, Westbrook, ME); fluoresceinated (FITC) or phycoerythrin (PE) -conjugated anti-CD:4, 8, 25, 29, 40, 40L, 44, 49a, 49b, 54 and 80; anti-CXCL-11 mAb; anti-human CCR:1, 2, 3, 5, 6, 7 and 9 mAb; anti- CXCR:1, 2, 3, 4, 5 and 6 mAb (R&D Systems, Minneapolis, MN); anti-human CCR:4, 8, and 10 mAb (Imgenex, San Diego, CA); anti-CCR11 and -CX3CR1 polyclonal Ab (Abcam, Cambridge, MA); FITC conjugated goat anti-mouse IgG (Invitrogen, Carlsbad, CA). .. Recombinant human CXCL11 was purchased from R&D Systems. .. mRNA was extracted from CRC cells (5 × 10 6 ) using Fast Track 2.0 mRNA isolation kit (Invitrogen).

    Article Title: Tumor Cell-Intrinsic Circular RNA CircFNDC3B Attenuates CD8+ T Cells Infiltration in Non-Small Cell Lung Cancer
    Article Snippet: .. When indicated, anti-CXCL11 (R&D Systems, MAB672, 1μg/ml), anti-CXCL10 (R&D Systems, MAB266, 1μg/ml), recombinant human CXCL11 (R&D Systems, 672-IT, 50ng/ml), recombinant human CXCL10 (R&D Systems, 266-IP, 50ng/ml) were added to the lower chamber. .. The chambers were incubated at 37°C, 5% CO2 for 4 h. Transmigrated cells in the lower chambers were collected and stained with anti-human CD8 mAbs (Biolegend, 980908).

    Control:

    Article Title: Macrophage Migration Inhibitory Factor Limits Activation-Induced Apoptosis of Platelets via CXCR7-Dependent Akt Signaling
    Article Snippet: .. These findings link the proinflammatory role of MIF with an antithrombotic effect and suggest targeting the MIF-CXCR7 interaction may be a potential strategy to control inflammation. at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from at New York University/ Medical Center--New York on October 15, 2014http://circres.ahajournals.org/Downloaded from 1 Supplemental Material Materials: Recombinant murine/human/feline SDF-1α/CXCL12, recombinant human CXCL11/I-TAC (rhCXCL11), recombinant murine CXCL11/I-TAC (rmCXCL11) recombinant human MIF (rhMIF), recombinant murine MIF (rmMIF), mouse monoclonal anti-human CXCR4-PE, rat anti-mouse CXCR4-FITC, mouse anti- human/mouse CXCR7-PE, rat monoclonal anti-mouse CXCR4-unconjugated, mouse monoclonal anti-human CXCR4-unconjugated, mouse monoclonal anti-human CXCR7-unconjugated, mouse anti human CXCR2-unconjugated antibodies were procured from R&D systems. .. Rabbit polyclonal CD74-FITC, rabbit polyclonal MIF- FITC and rabbit polyclonal CXCL11-FITC were from Biorbyt, rabbit polyclonal antibody to CXCR7/GPR159 (N-term) was from Acris Antibodies, mouse monoclonal anti-MIF and rabbit anti-human CXCL11 were from Abcam, rabbit monoclonal p42/44MAPK (Erk1/2) and rabbit monoclonal phospho p42/44 MAPK (Erk1/2), rabbit monoclonal-PI3K and rabbit monoclonal-phospho-PI3K, rabbit monoclonal-Akt and rabbit monoclonal-phospho-Akt, rabbit monoclonal-phospho-BAD, rabbit monoclonal- cleaved active caspase 3-Alexa Fluor-488 conjugated antibodies were purchased from Cell Signaling Technology.



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    VUF16840 inhibits constitutive as well as agonist induced β -arrestin2 recruitment to ACKR3. (A) Transiently transfected HEK293T cells, expressing hACKR3-SmBiT and β -arrestin2-LgBiT, were stimulated with increasing concentrations CXCL12 or (B) VUF16840. Subsequently, β -arrestin2 recruitment to hACKR3 was detected by NanoBiT complementation. (C) Transfected HEK293T cells were stimulated for 30 minutes with increasing concentrations CXCL12 or VUF16840 and β -arrestin2 recruitment to the hACKR3 was detected by NanoBiT complementation. (D) Transfected HEK293T cells were stimulated with increasing concentrations VUF15485 , VUF16840, <t>CXCL11</t> or CXCL12, and β -arrestin2 recruitment to hACKR3 was detected by BRET. (E) β -Arrestin2 recruitment to the ACKR3 was measured after stimulation with 100 nM of VUF15485 , CXCL11 or CXCL12 in the presence of increasing concentrations VUF16840. (F) Transfected HEK293T cells were stimulated with increasing concentrations VUF16840 in the presence or absence of 100 nM CXCL12 and β -arrestin2 recruitment to the hCXCR4 was detected by biolumescence resonance energy transfer. Depicted data is normalized as fold-basal and represents the mean ± SD of n experiments with triplicate measurements per experiment. Panel A–C and F depicts the average of 3 experiments; for panel D and E, the number of experiments differed per condition and is summarized in .
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    Fig. 7. FABP5 downregulation in DSCs repressed <t>CXCL11/CXCR3</t> signaling between DSCs and HTR-8/Svneo cells. (A) KEGG pathway analysis of DEGs identified by RNA-seq in FABP5-knockdown primary DSC. (B) Gene Set Enrichment Analysis (GSEA) of chemokine signaling pathways in FABP5-silenced DSCs. (C) FPKM values of CXCL11 expression in control and FABP5-knockdown groups. (D) RT-qPCR, (E, F) Western blot, and (G) ELISA quantification of CXCL11 expression in DSCs transfected with FABP5-targeting or NC siRNAs. (H) RT-qPCR and (I, J) Western blot analyses of CXCR3 expression in HTR-8/Svneo cells treated with CS from FABP5-deficient or control DSCs. Statistical significance: *P < 0.05, **P < 0.01.
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    Fig. 7. FABP5 downregulation in DSCs repressed <t>CXCL11/CXCR3</t> signaling between DSCs and HTR-8/Svneo cells. (A) KEGG pathway analysis of DEGs identified by RNA-seq in FABP5-knockdown primary DSC. (B) Gene Set Enrichment Analysis (GSEA) of chemokine signaling pathways in FABP5-silenced DSCs. (C) FPKM values of CXCL11 expression in control and FABP5-knockdown groups. (D) RT-qPCR, (E, F) Western blot, and (G) ELISA quantification of CXCL11 expression in DSCs transfected with FABP5-targeting or NC siRNAs. (H) RT-qPCR and (I, J) Western blot analyses of CXCR3 expression in HTR-8/Svneo cells treated with CS from FABP5-deficient or control DSCs. Statistical significance: *P < 0.05, **P < 0.01.
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    Fig. 4 Cytokine analysis of CM from M0, M1, and M2 macrophages. A Comparative analysis of cytokine secretion in CM from naïve and polarized macrophage-CM. Each cytokine was detected in duplicate. Target cytokines are indicated using square frames with numbers. B CXCL9, <t>CXCL11,</t> and PTX3 proteins (indicated by arrows in a panel) were highly detected in M1-CM compared to M0- and M2-CM. C Quantification shows the mean signal intensity
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    Image Search Results


    VUF16840 inhibits constitutive as well as agonist induced β -arrestin2 recruitment to ACKR3. (A) Transiently transfected HEK293T cells, expressing hACKR3-SmBiT and β -arrestin2-LgBiT, were stimulated with increasing concentrations CXCL12 or (B) VUF16840. Subsequently, β -arrestin2 recruitment to hACKR3 was detected by NanoBiT complementation. (C) Transfected HEK293T cells were stimulated for 30 minutes with increasing concentrations CXCL12 or VUF16840 and β -arrestin2 recruitment to the hACKR3 was detected by NanoBiT complementation. (D) Transfected HEK293T cells were stimulated with increasing concentrations VUF15485 , VUF16840, CXCL11 or CXCL12, and β -arrestin2 recruitment to hACKR3 was detected by BRET. (E) β -Arrestin2 recruitment to the ACKR3 was measured after stimulation with 100 nM of VUF15485 , CXCL11 or CXCL12 in the presence of increasing concentrations VUF16840. (F) Transfected HEK293T cells were stimulated with increasing concentrations VUF16840 in the presence or absence of 100 nM CXCL12 and β -arrestin2 recruitment to the hCXCR4 was detected by biolumescence resonance energy transfer. Depicted data is normalized as fold-basal and represents the mean ± SD of n experiments with triplicate measurements per experiment. Panel A–C and F depicts the average of 3 experiments; for panel D and E, the number of experiments differed per condition and is summarized in .

    Journal: Molecular Pharmacology

    Article Title: Inhibition of constitutive activity of the atypical chemokine receptor 3 by the small-molecule inverse agonist VUF16840

    doi: 10.1016/j.molpha.2025.100085

    Figure Lengend Snippet: VUF16840 inhibits constitutive as well as agonist induced β -arrestin2 recruitment to ACKR3. (A) Transiently transfected HEK293T cells, expressing hACKR3-SmBiT and β -arrestin2-LgBiT, were stimulated with increasing concentrations CXCL12 or (B) VUF16840. Subsequently, β -arrestin2 recruitment to hACKR3 was detected by NanoBiT complementation. (C) Transfected HEK293T cells were stimulated for 30 minutes with increasing concentrations CXCL12 or VUF16840 and β -arrestin2 recruitment to the hACKR3 was detected by NanoBiT complementation. (D) Transfected HEK293T cells were stimulated with increasing concentrations VUF15485 , VUF16840, CXCL11 or CXCL12, and β -arrestin2 recruitment to hACKR3 was detected by BRET. (E) β -Arrestin2 recruitment to the ACKR3 was measured after stimulation with 100 nM of VUF15485 , CXCL11 or CXCL12 in the presence of increasing concentrations VUF16840. (F) Transfected HEK293T cells were stimulated with increasing concentrations VUF16840 in the presence or absence of 100 nM CXCL12 and β -arrestin2 recruitment to the hCXCR4 was detected by biolumescence resonance energy transfer. Depicted data is normalized as fold-basal and represents the mean ± SD of n experiments with triplicate measurements per experiment. Panel A–C and F depicts the average of 3 experiments; for panel D and E, the number of experiments differed per condition and is summarized in .

    Article Snippet: Human recombinant CXCL11 (#CN-13), CXCL12 (#CN-11), and fluorescently labeled CXCL12-A647 (#CAF-11) were purchased from Almac or Protein Foundry.

    Techniques: Transfection, Expressing, Förster Resonance Energy Transfer

    VUF16840 noncompetitively inhibits agonist-induced β -arrestin2 recruitment to hACKR3. (A) Transiently transfected HEK293T cells, expressing hACKR3-SmBiT and β -arrestin2-LgBiT were stimulated with increasing concentrations of (A) CXCL11 or (B) CXCL12 following a 60 minutes pretreatment with buffer or various concentrations of the inverse agonist VUF16840. Next, the β -arrestin2 recruitment to the hACKR3 was detected by NLuc complementation. Depicted data are the mean ± SD of 3 experiments.

    Journal: Molecular Pharmacology

    Article Title: Inhibition of constitutive activity of the atypical chemokine receptor 3 by the small-molecule inverse agonist VUF16840

    doi: 10.1016/j.molpha.2025.100085

    Figure Lengend Snippet: VUF16840 noncompetitively inhibits agonist-induced β -arrestin2 recruitment to hACKR3. (A) Transiently transfected HEK293T cells, expressing hACKR3-SmBiT and β -arrestin2-LgBiT were stimulated with increasing concentrations of (A) CXCL11 or (B) CXCL12 following a 60 minutes pretreatment with buffer or various concentrations of the inverse agonist VUF16840. Next, the β -arrestin2 recruitment to the hACKR3 was detected by NLuc complementation. Depicted data are the mean ± SD of 3 experiments.

    Article Snippet: Human recombinant CXCL11 (#CN-13), CXCL12 (#CN-11), and fluorescently labeled CXCL12-A647 (#CAF-11) were purchased from Almac or Protein Foundry.

    Techniques: Transfection, Expressing

    Fig. 7. FABP5 downregulation in DSCs repressed CXCL11/CXCR3 signaling between DSCs and HTR-8/Svneo cells. (A) KEGG pathway analysis of DEGs identified by RNA-seq in FABP5-knockdown primary DSC. (B) Gene Set Enrichment Analysis (GSEA) of chemokine signaling pathways in FABP5-silenced DSCs. (C) FPKM values of CXCL11 expression in control and FABP5-knockdown groups. (D) RT-qPCR, (E, F) Western blot, and (G) ELISA quantification of CXCL11 expression in DSCs transfected with FABP5-targeting or NC siRNAs. (H) RT-qPCR and (I, J) Western blot analyses of CXCR3 expression in HTR-8/Svneo cells treated with CS from FABP5-deficient or control DSCs. Statistical significance: *P < 0.05, **P < 0.01.

    Journal: Free radical biology & medicine

    Article Title: Oxidative stress-induced decreased expression of FABP5 leads to mitochondrial damage and survival disorder of decidual stromal cells in women with recurrent spontaneous abortion.

    doi: 10.1016/j.freeradbiomed.2025.06.003

    Figure Lengend Snippet: Fig. 7. FABP5 downregulation in DSCs repressed CXCL11/CXCR3 signaling between DSCs and HTR-8/Svneo cells. (A) KEGG pathway analysis of DEGs identified by RNA-seq in FABP5-knockdown primary DSC. (B) Gene Set Enrichment Analysis (GSEA) of chemokine signaling pathways in FABP5-silenced DSCs. (C) FPKM values of CXCL11 expression in control and FABP5-knockdown groups. (D) RT-qPCR, (E, F) Western blot, and (G) ELISA quantification of CXCL11 expression in DSCs transfected with FABP5-targeting or NC siRNAs. (H) RT-qPCR and (I, J) Western blot analyses of CXCR3 expression in HTR-8/Svneo cells treated with CS from FABP5-deficient or control DSCs. Statistical significance: *P < 0.05, **P < 0.01.

    Article Snippet: The concentration of CXCL11 in the CS was measured using a human CXCL11 ELISA kit (Boster, Beijing, China; CAT# EK0737) following the manufacturer’s instructions.

    Techniques: RNA Sequencing, Knockdown, Protein-Protein interactions, Expressing, Control, Quantitative RT-PCR, Western Blot, Enzyme-linked Immunosorbent Assay, Transfection

    Fig. 4 Cytokine analysis of CM from M0, M1, and M2 macrophages. A Comparative analysis of cytokine secretion in CM from naïve and polarized macrophage-CM. Each cytokine was detected in duplicate. Target cytokines are indicated using square frames with numbers. B CXCL9, CXCL11, and PTX3 proteins (indicated by arrows in a panel) were highly detected in M1-CM compared to M0- and M2-CM. C Quantification shows the mean signal intensity

    Journal: Cell & bioscience

    Article Title: CXCL11 reprograms M2-biased macrophage polarization to alleviate pulmonary fibrosis in mice.

    doi: 10.1186/s13578-024-01320-7

    Figure Lengend Snippet: Fig. 4 Cytokine analysis of CM from M0, M1, and M2 macrophages. A Comparative analysis of cytokine secretion in CM from naïve and polarized macrophage-CM. Each cytokine was detected in duplicate. Target cytokines are indicated using square frames with numbers. B CXCL9, CXCL11, and PTX3 proteins (indicated by arrows in a panel) were highly detected in M1-CM compared to M0- and M2-CM. C Quantification shows the mean signal intensity

    Article Snippet: For recombinant human CXCL11 (R&D SYSTEMS, Minneapolis, Minnesota, USA) treatment, the mice with fibrosis induction received an IV injection of CXCL11 (2 μg/mouse) on days 10, 12, 13, and 15 after BLM administration.

    Techniques:

    Fig. 5 M1 macrophage-derived CXCL11 promotes M2 to M1 phenotype polarization mediated through the p65, ERK1/2, and AKT pathway in vitro. A A schematic diagram illustrating the experimental procedures to examine the effect of CXCL11 on macrophage polarity. B Real-time RT-PCR analyzed the relative mRNA levels of M1 (iNos and Socs3)- and M2 (Arg1 and Mrc1)-related factors. C Western blotting for phosphorylation of p65, ERK1/2, AKT and COX2, iNOS, ARG1, and CD206 protein in BMDM after CXCL11 treatment. α-Tubulin was used as a loading control. D, E The graph shows the relative intensity of phosphorylation of p65, ERK1/2, and AKT (D) and COX2, iNOS, ARG1, and CD206 (E). F A schematic diagram illustrating the experimental procedures to examine the pathway of CXCL11 on macrophage polarity. G Western blotting for phosphorylation of p65, ERK1/2, AKT and COX2, iNOS, ARG1, and CD206 protein in BMDM after CXCL11 treatment with inhibitors. α-Tubulin was used as a loading control. H, I The graph shows the relative intensity of phosphorylation of p65, ERK1/2, and AKT (H) and COX2, iNOS, ARG1, and CD206 (I)

    Journal: Cell & bioscience

    Article Title: CXCL11 reprograms M2-biased macrophage polarization to alleviate pulmonary fibrosis in mice.

    doi: 10.1186/s13578-024-01320-7

    Figure Lengend Snippet: Fig. 5 M1 macrophage-derived CXCL11 promotes M2 to M1 phenotype polarization mediated through the p65, ERK1/2, and AKT pathway in vitro. A A schematic diagram illustrating the experimental procedures to examine the effect of CXCL11 on macrophage polarity. B Real-time RT-PCR analyzed the relative mRNA levels of M1 (iNos and Socs3)- and M2 (Arg1 and Mrc1)-related factors. C Western blotting for phosphorylation of p65, ERK1/2, AKT and COX2, iNOS, ARG1, and CD206 protein in BMDM after CXCL11 treatment. α-Tubulin was used as a loading control. D, E The graph shows the relative intensity of phosphorylation of p65, ERK1/2, and AKT (D) and COX2, iNOS, ARG1, and CD206 (E). F A schematic diagram illustrating the experimental procedures to examine the pathway of CXCL11 on macrophage polarity. G Western blotting for phosphorylation of p65, ERK1/2, AKT and COX2, iNOS, ARG1, and CD206 protein in BMDM after CXCL11 treatment with inhibitors. α-Tubulin was used as a loading control. H, I The graph shows the relative intensity of phosphorylation of p65, ERK1/2, and AKT (H) and COX2, iNOS, ARG1, and CD206 (I)

    Article Snippet: For recombinant human CXCL11 (R&D SYSTEMS, Minneapolis, Minnesota, USA) treatment, the mice with fibrosis induction received an IV injection of CXCL11 (2 μg/mouse) on days 10, 12, 13, and 15 after BLM administration.

    Techniques: Derivative Assay, In Vitro, Quantitative RT-PCR, Western Blot, Phospho-proteomics, Control

    Fig. 7 A schematic illustration of M1 macrophage-derived CXCL11 in BLM-induced PF in mice. M1 macrophage-derived CXCL11 to modulate M1 macrophage polarization for reverting the fibrogenic process in mice with PF

    Journal: Cell & bioscience

    Article Title: CXCL11 reprograms M2-biased macrophage polarization to alleviate pulmonary fibrosis in mice.

    doi: 10.1186/s13578-024-01320-7

    Figure Lengend Snippet: Fig. 7 A schematic illustration of M1 macrophage-derived CXCL11 in BLM-induced PF in mice. M1 macrophage-derived CXCL11 to modulate M1 macrophage polarization for reverting the fibrogenic process in mice with PF

    Article Snippet: For recombinant human CXCL11 (R&D SYSTEMS, Minneapolis, Minnesota, USA) treatment, the mice with fibrosis induction received an IV injection of CXCL11 (2 μg/mouse) on days 10, 12, 13, and 15 after BLM administration.

    Techniques: Derivative Assay