itpr2 antibody Search Results


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Biorbyt anti itpr2
a and b Lrmp interacted with IP3R proteins, including <t>ITPR2,</t> as determined by co-IP followed by LC-MS/MS assays in MEFs. a Lrmp-interacting proteins (label with red) mapped in “Chemo-sensing pathway” in KEGG. b Counts of Lrmp and IP3Rs detected by co-IP followed by LC-MS/MS assays in MEFs. c Lrmp-ITPR2 interaction was confirmed by co-IP assays followed by Western-blot assays in MEFs transfected with vectors expressing Lrmp-Flag and ITPR2-HA, respectively. d The binding region of Lrmp for ITPR2 was determined by co-IP followed by Western-blot assays in H1299 cells transfected with vectors expressing different Lrmp-Flag fragments and ITPR2-HA, respectively. Upper panel: schematic representation of vectors expressing full-length (FL) or serial deletion mutants of Lrmp-Flag. e The Lrmp-IPTR2 interaction was examined by PLA assays in WT and Lrmp−/− small intestinal tissues. Red: PLA signals of the Lrmp-ITPR2 interaction; green: Dclk1; DAPI: nucleus. f – h Ca 2+ flux in response to Ionomycin (2 µM) treatment in WT, p53−/− and Lrmp−/− MEFs with or without transfection of either FL- or ΔM-Lrmp-Flag vectors. f Average traces of Ca 2+ responses. g Relative Fluo-4 fluorescence obtained from Ca 2+ transients at peak (48 s). h Representative fluorescence images. The Fluo-4 fluorescence intensity before Ionomycin treatment was calculated as 1. In f , each curve represents an average of at least 90 cells. Curves of each cell are shown in Fig S . *** p < 0.001; ** p < 0.01; NS: non-significant, two-tailed Student’s t -test.
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Alomone Labs αkv1 2
a and b Lrmp interacted with IP3R proteins, including <t>ITPR2,</t> as determined by co-IP followed by LC-MS/MS assays in MEFs. a Lrmp-interacting proteins (label with red) mapped in “Chemo-sensing pathway” in KEGG. b Counts of Lrmp and IP3Rs detected by co-IP followed by LC-MS/MS assays in MEFs. c Lrmp-ITPR2 interaction was confirmed by co-IP assays followed by Western-blot assays in MEFs transfected with vectors expressing Lrmp-Flag and ITPR2-HA, respectively. d The binding region of Lrmp for ITPR2 was determined by co-IP followed by Western-blot assays in H1299 cells transfected with vectors expressing different Lrmp-Flag fragments and ITPR2-HA, respectively. Upper panel: schematic representation of vectors expressing full-length (FL) or serial deletion mutants of Lrmp-Flag. e The Lrmp-IPTR2 interaction was examined by PLA assays in WT and Lrmp−/− small intestinal tissues. Red: PLA signals of the Lrmp-ITPR2 interaction; green: Dclk1; DAPI: nucleus. f – h Ca 2+ flux in response to Ionomycin (2 µM) treatment in WT, p53−/− and Lrmp−/− MEFs with or without transfection of either FL- or ΔM-Lrmp-Flag vectors. f Average traces of Ca 2+ responses. g Relative Fluo-4 fluorescence obtained from Ca 2+ transients at peak (48 s). h Representative fluorescence images. The Fluo-4 fluorescence intensity before Ionomycin treatment was calculated as 1. In f , each curve represents an average of at least 90 cells. Curves of each cell are shown in Fig S . *** p < 0.001; ** p < 0.01; NS: non-significant, two-tailed Student’s t -test.
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Image Search Results


a and b Lrmp interacted with IP3R proteins, including ITPR2, as determined by co-IP followed by LC-MS/MS assays in MEFs. a Lrmp-interacting proteins (label with red) mapped in “Chemo-sensing pathway” in KEGG. b Counts of Lrmp and IP3Rs detected by co-IP followed by LC-MS/MS assays in MEFs. c Lrmp-ITPR2 interaction was confirmed by co-IP assays followed by Western-blot assays in MEFs transfected with vectors expressing Lrmp-Flag and ITPR2-HA, respectively. d The binding region of Lrmp for ITPR2 was determined by co-IP followed by Western-blot assays in H1299 cells transfected with vectors expressing different Lrmp-Flag fragments and ITPR2-HA, respectively. Upper panel: schematic representation of vectors expressing full-length (FL) or serial deletion mutants of Lrmp-Flag. e The Lrmp-IPTR2 interaction was examined by PLA assays in WT and Lrmp−/− small intestinal tissues. Red: PLA signals of the Lrmp-ITPR2 interaction; green: Dclk1; DAPI: nucleus. f – h Ca 2+ flux in response to Ionomycin (2 µM) treatment in WT, p53−/− and Lrmp−/− MEFs with or without transfection of either FL- or ΔM-Lrmp-Flag vectors. f Average traces of Ca 2+ responses. g Relative Fluo-4 fluorescence obtained from Ca 2+ transients at peak (48 s). h Representative fluorescence images. The Fluo-4 fluorescence intensity before Ionomycin treatment was calculated as 1. In f , each curve represents an average of at least 90 cells. Curves of each cell are shown in Fig S . *** p < 0.001; ** p < 0.01; NS: non-significant, two-tailed Student’s t -test.

Journal: Nature Communications

Article Title: Tumor suppressor p53 regulates intestinal type 2 immunity

doi: 10.1038/s41467-021-23587-x

Figure Lengend Snippet: a and b Lrmp interacted with IP3R proteins, including ITPR2, as determined by co-IP followed by LC-MS/MS assays in MEFs. a Lrmp-interacting proteins (label with red) mapped in “Chemo-sensing pathway” in KEGG. b Counts of Lrmp and IP3Rs detected by co-IP followed by LC-MS/MS assays in MEFs. c Lrmp-ITPR2 interaction was confirmed by co-IP assays followed by Western-blot assays in MEFs transfected with vectors expressing Lrmp-Flag and ITPR2-HA, respectively. d The binding region of Lrmp for ITPR2 was determined by co-IP followed by Western-blot assays in H1299 cells transfected with vectors expressing different Lrmp-Flag fragments and ITPR2-HA, respectively. Upper panel: schematic representation of vectors expressing full-length (FL) or serial deletion mutants of Lrmp-Flag. e The Lrmp-IPTR2 interaction was examined by PLA assays in WT and Lrmp−/− small intestinal tissues. Red: PLA signals of the Lrmp-ITPR2 interaction; green: Dclk1; DAPI: nucleus. f – h Ca 2+ flux in response to Ionomycin (2 µM) treatment in WT, p53−/− and Lrmp−/− MEFs with or without transfection of either FL- or ΔM-Lrmp-Flag vectors. f Average traces of Ca 2+ responses. g Relative Fluo-4 fluorescence obtained from Ca 2+ transients at peak (48 s). h Representative fluorescence images. The Fluo-4 fluorescence intensity before Ionomycin treatment was calculated as 1. In f , each curve represents an average of at least 90 cells. Curves of each cell are shown in Fig S . *** p < 0.001; ** p < 0.01; NS: non-significant, two-tailed Student’s t -test.

Article Snippet: In brief, tissue sections were incubated with anti-Lrmp (Biorbyt, orb166443, 1:50 dilution) and anti-ITPR2 (Novus, NB100-2466, 1:50 dilution) antibodies together with Duolink secondary antibodies.

Techniques: Co-Immunoprecipitation Assay, Liquid Chromatography with Mass Spectroscopy, Western Blot, Transfection, Expressing, Binding Assay, Fluorescence, Two Tailed Test