Human SIGIRR Antibody

Detection of SIGIRR by Western Blot The expression of the cell surface of the SIGIRR is downregulated in CF cells. (A,B) Cell surface expression of the SIGIRR in (A) C38 and IB3-1, (B) NHBE and DHBE-CF (non-CF vs. CF) airway epithelial cells were assessed by biotinylation assay, followed by immunoblotting using anti-SIGIRR, calreticulin (CRT) and Sp1 antibodies. Protein bands in (A) were scanned, and relative band intensities were normalized to the beta -actin band. The graphs represent the average relative band intensity with S.D. from four independent experiments. * p < 0.05; Student’s t-test (n = 3). (C) Flow cytometry for the SIGIRR was performed using C38 and IB3-1 cells. Surface expressions of the SIGIRR were indicated by a fluorescence shift compared to the isotype control antibody (dotted line). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of SIGIRR by Western Blot The expression of the cell surface of the SIGIRR is downregulated in CF cells. (A,B) Cell surface expression of the SIGIRR in (A) C38 and IB3-1, (B) NHBE and DHBE-CF (non-CF vs. CF) airway epithelial cells were assessed by biotinylation assay, followed by immunoblotting using anti-SIGIRR, calreticulin (CRT) and Sp1 antibodies. Protein bands in (A) were scanned, and relative band intensities were normalized to the beta -actin band. The graphs represent the average relative band intensity with S.D. from four independent experiments. * p < 0.05; Student’s t-test (n = 3). (C) Flow cytometry for the SIGIRR was performed using C38 and IB3-1 cells. Surface expressions of the SIGIRR were indicated by a fluorescence shift compared to the isotype control antibody (dotted line). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of SIGIRR by Western Blot Suppression of IL-8 production by IL-37b is dependent on the cell surface-expressed WT-SIGIRR, leading to the attenuation of JNK phosphorylation. (A,B) C38 and IB3-1 cells were stimulated with 1 μg/mL flagellin or 20 μg/mL poly(I:C) 2 h after treatment with the indicated concentrations of a precursor or Val46 IL-37b. After 24 h, released IL-8 in the condition media was measured by ELISA. (C) NHBE and DHBE-CF cells were stimulated with 0.5 μg/mL poly(I:C) 2 h after treatment with 10 ng/mL of a precursor or Val46 IL-37b. After 24 h, released IL-8 in the condition media was measured by ELISA. (D) C38 and IB3-1 cells and (E) NHBE and DHBE-CF cells were stimulated with poly(I:C) (D, 20 μg/mL; E, 1 μg/mL) 2 h after treatment with a 10 ng/mL precursor of IL-37b. After the indicated period of the poly(I:C) treatment, the total cell lysates were subjected to immunoblotting using antibodies against the phospho-active form of MAPKs, IRF3, and I kappa B alpha. (F,G) pcDNA or delta 8-SIGIRR-transfected C38 cells and (H and I) pcDNA or the WT-SIGIRR-transfected IB3-1 cells were stimulated with 20 μg/mL poly(I:C) 2 h after treatment with the indicated concentrations of the precursor of IL-37b. After 24 h, released IL-8 in the condition media was measured by ELISA. Exogenously expressed delta 8 and the WT-SIGIRR were assessed by immunoblotting with the anti-SIGIRR. For the immunoblotting experiments (D–F,H), beta -actin was used as a loading control. (A–C,G,I) Results represent the mean ± S.D. * p < 0.05, ** p < 0.01, *** p < 0.001 versus poly(I:C)-treated cells; ANOVA with Dunnett’s test (n = 3). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of SIGIRR by Flow Cytometry The expression of the cell surface of the SIGIRR is downregulated in CF cells. (A,B) Cell surface expression of the SIGIRR in (A) C38 and IB3-1, (B) NHBE and DHBE-CF (non-CF vs. CF) airway epithelial cells were assessed by biotinylation assay, followed by immunoblotting using anti-SIGIRR, calreticulin (CRT) and Sp1 antibodies. Protein bands in (A) were scanned, and relative band intensities were normalized to the beta -actin band. The graphs represent the average relative band intensity with S.D. from four independent experiments. * p < 0.05; Student’s t-test (n = 3). (C) Flow cytometry for the SIGIRR was performed using C38 and IB3-1 cells. Surface expressions of the SIGIRR were indicated by a fluorescence shift compared to the isotype control antibody (dotted line). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of SIGIRR by Western Blot Suppression of IL-8 production by IL-37b is dependent on the cell surface-expressed WT-SIGIRR, leading to the attenuation of JNK phosphorylation. (A,B) C38 and IB3-1 cells were stimulated with 1 μg/mL flagellin or 20 μg/mL poly(I:C) 2 h after treatment with the indicated concentrations of a precursor or Val46 IL-37b. After 24 h, released IL-8 in the condition media was measured by ELISA. (C) NHBE and DHBE-CF cells were stimulated with 0.5 μg/mL poly(I:C) 2 h after treatment with 10 ng/mL of a precursor or Val46 IL-37b. After 24 h, released IL-8 in the condition media was measured by ELISA. (D) C38 and IB3-1 cells and (E) NHBE and DHBE-CF cells were stimulated with poly(I:C) (D, 20 μg/mL; E, 1 μg/mL) 2 h after treatment with a 10 ng/mL precursor of IL-37b. After the indicated period of the poly(I:C) treatment, the total cell lysates were subjected to immunoblotting using antibodies against the phospho-active form of MAPKs, IRF3, and I kappa B alpha. (F,G) pcDNA or delta 8-SIGIRR-transfected C38 cells and (H and I) pcDNA or the WT-SIGIRR-transfected IB3-1 cells were stimulated with 20 μg/mL poly(I:C) 2 h after treatment with the indicated concentrations of the precursor of IL-37b. After 24 h, released IL-8 in the condition media was measured by ELISA. Exogenously expressed delta 8 and the WT-SIGIRR were assessed by immunoblotting with the anti-SIGIRR. For the immunoblotting experiments (D–F,H), beta -actin was used as a loading control. (A–C,G,I) Results represent the mean ± S.D. * p < 0.05, ** p < 0.01, *** p < 0.001 versus poly(I:C)-treated cells; ANOVA with Dunnett’s test (n = 3). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of SIGIRR by Flow Cytometry The expression of the cell surface of the SIGIRR is downregulated in CF cells. (A,B) Cell surface expression of the SIGIRR in (A) C38 and IB3-1, (B) NHBE and DHBE-CF (non-CF vs. CF) airway epithelial cells were assessed by biotinylation assay, followed by immunoblotting using anti-SIGIRR, calreticulin (CRT) and Sp1 antibodies. Protein bands in (A) were scanned, and relative band intensities were normalized to the beta -actin band. The graphs represent the average relative band intensity with S.D. from four independent experiments. * p < 0.05; Student’s t-test (n = 3). (C) Flow cytometry for the SIGIRR was performed using C38 and IB3-1 cells. Surface expressions of the SIGIRR were indicated by a fluorescence shift compared to the isotype control antibody (dotted line). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of SIGIRR by Western Blot The expression of the cell surface of the SIGIRR is downregulated in CF cells. (A,B) Cell surface expression of the SIGIRR in (A) C38 and IB3-1, (B) NHBE and DHBE-CF (non-CF vs. CF) airway epithelial cells were assessed by biotinylation assay, followed by immunoblotting using anti-SIGIRR, calreticulin (CRT) and Sp1 antibodies. Protein bands in (A) were scanned, and relative band intensities were normalized to the beta -actin band. The graphs represent the average relative band intensity with S.D. from four independent experiments. * p < 0.05; Student’s t-test (n = 3). (C) Flow cytometry for the SIGIRR was performed using C38 and IB3-1 cells. Surface expressions of the SIGIRR were indicated by a fluorescence shift compared to the isotype control antibody (dotted line). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.

Detection of SIGIRR by Western Blot The expression of the cell surface of the SIGIRR is downregulated in CF cells. (A,B) Cell surface expression of the SIGIRR in (A) C38 and IB3-1, (B) NHBE and DHBE-CF (non-CF vs. CF) airway epithelial cells were assessed by biotinylation assay, followed by immunoblotting using anti-SIGIRR, calreticulin (CRT) and Sp1 antibodies. Protein bands in (A) were scanned, and relative band intensities were normalized to the beta -actin band. The graphs represent the average relative band intensity with S.D. from four independent experiments. * p < 0.05; Student’s t-test (n = 3). (C) Flow cytometry for the SIGIRR was performed using C38 and IB3-1 cells. Surface expressions of the SIGIRR were indicated by a fluorescence shift compared to the isotype control antibody (dotted line). Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35887095), licensed under a CC-BY license. Not internally tested by R&D Systems.