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Calnexin (CNX), an unglycosylated resident ER transmembrane protein, together with Calreticulin (CRT), plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their monoglucosylated glycans. Calnexin associates with newly synthesized monomeric glycoproteins and only recognizes glycoproteins when they are incompletely folded. Furthermore, Calnexin has been demonstrated to function as a molecular chaperone capable of interacting with polypeptide segments of folding glycoproteins.
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Immunohistochemistry analysis of human placenta tissue stained with Calnexin, pAb at 5µg/ml.
Western blot analysis: Lane 1: MWM, Lane 2: Vero, Lane 3: 3T3, Lane 4: PC-12, Lane 5: HeLa.
Identification of calnexin as a DGAT2 interacting protein by co-immunoprecipitation and mass spectrometry.(A) HEK-293T cells were transfected with either FL-DGAT2 or myc-DGAT2. FL-DGAT2 was immunoprecipitated with anti-FLAG agarose from detergent solubilized material. Immunoprecipitates (IP) were separated by SDS-PAGE and were then probed with anti-DGAT2. (B) Calnexin, but not PDI, was detected in anti-FLAG immunoprecipitates by immunoblotting. HC; heavy chain. (C) Interaction of DGAT2 and calnexin was detected in situ using a proximity ligation assay. COS-7 cells expressing either FL-DGAT2 or Myc-DGAT2 were stained with mouse anti-FLAG and rabbit anti-calnexin antibodies. Interaction signals (red) were detected using a Duolink detection kit. Nuclei were stained with DAPI (blue). Scale bar = 10 μm.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. PLoS One (2019)
Effect of cell-intrinsic antiviral signaling components on dsRNA-induced cell death and IRF1 expression.A A549 cells with functional KO of the indicated genes were mock stimulated with poly(C) or stimulated with 2 ng/ml 5’ppp-dsRNA for 6 h. IRF1 mRNA transcripts were determined by qRT-PCR; fold-induction over mock stimulation is shown. Non-normalized data shown in Fig. S6A + B. B–D Percentage of dead A549 cells with functional KO of the indicated genes relative to total cells counted over time (B, C) or 36 h (D) post dsRNA stimulation. Mock controls (poly[C] stimulation) shown in Fig. S6C + D. E–G A549 cells with functional KO of the indicated genes or administration of the indicated inhibitors were treated with 2 µM DOX or DMSO for 6 h. Levels of IRF1 were determined by western blot. Uncropped images of western blots shown in Fig. S9E–G. Quantification of replicate (n ≥ 3) western blots shown in Fig. S6H + I. A–D Data shown represent the results of at least three biologically independent experiments.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Cooperative effects of RIG-I-like receptor signaling and IRF1 on DNA damage-induced cell death. Cell Death Dis (2022)
Identification of calnexin as a DGAT2 interacting protein by co-immunoprecipitation and mass spectrometry.(A) HEK-293T cells were transfected with either FL-DGAT2 or myc-DGAT2. FL-DGAT2 was immunoprecipitated with anti-FLAG agarose from detergent solubilized material. Immunoprecipitates (IP) were separated by SDS-PAGE and were then probed with anti-DGAT2. (B) Calnexin, but not PDI, was detected in anti-FLAG immunoprecipitates by immunoblotting. HC; heavy chain. (C) Interaction of DGAT2 and calnexin was detected in situ using a proximity ligation assay. COS-7 cells expressing either FL-DGAT2 or Myc-DGAT2 were stained with mouse anti-FLAG and rabbit anti-calnexin antibodies. Interaction signals (red) were detected using a Duolink detection kit. Nuclei were stained with DAPI (blue). Scale bar = 10 μm.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. PLoS One (2019)
Relevance of IRF1 on DNA damage-induced cell death.A A549 cells were treated with 1 µM DOX or DMSO for the indicated durations. IRF1 mRNA transcripts were determined by qRT-PCR. B A549 cells or A549 TP53−/− were treated with 1 µM DOX or DMSO for 10 h. Levels of IRF1 were determined by western blot. Uncropped image of western blot shown in Fig. S9B. Quantification of replicate western blots in Fig. S4A. C A549 cells were mock treated or stimulated with IFN-β or IFN-γ over-night. Levels of IRF1 were determined by western blot. Uncropped image of western blot shown in Fig. S9C. Data with additional DOX-treatment in Fig. S4B. D–G Percentage of dead A549 cells with functional KO or OE of IRF1, or post IFN pre-stimulation relative to total cells counted over time (D–F) or 36 h (G) post DOX or γ-IR (20 Gy) treatment. DMSO controls shown in Fig. S4D, E, G. H Percentage of dead cells upon IFN-γ treatment in absence or presence of γ-IR (20 Gy) at 36 h. I A549 cells were γ-irradiated. After 10 h IRF1 protein levels were determined by western blot. Uncropped image of western blot shown in Fig. S9D. A, D–H Data shown represent the results of at least three biologically independent experiments.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Cooperative effects of RIG-I-like receptor signaling and IRF1 on DNA damage-induced cell death. Cell Death Dis (2022)
KSHV miRNAs and Ago2 are partially localized in the nuclei of latently infected cells.(A) qRT-PCR analysis of mature KSHV miRNA distribution in the cytoplasmic and nuclear fractions of PEL cells. Percentage distribution was calculated by normalizing to expression in whole PEL cells, assuming no loss during fractionation. RNU48 was used as a nuclear control for fractionation. The bar graphs show the mean values (n = 3) ± SEM. p-values: * < 0.05; ** < 0.01; *** < 0.005. (B) Subcellular distribution of Ago2 proteins in PEL cells analyzed using Western blotting. Tubulin was probed as positive control for cytoplasm, Sm and Lamin A/C are positive controls for nuclei and Calnexin is the negative control for Endoplasmic Reticulum (C) Localization of Ago2 in PEL nuclei analyzed using IFA and confocal microscopy. Ago2 is shown in green and DAPI in blue. DAPI is shown at half the original intensity.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: microRNA dependent and independent deregulation of long non-coding RNAs by an oncogenic herpesvirus. PLoS Pathog (2017)
Relevance of IRF1 on DNA damage-induced cell death.A A549 cells were treated with 1 µM DOX or DMSO for the indicated durations. IRF1 mRNA transcripts were determined by qRT-PCR. B A549 cells or A549 TP53−/− were treated with 1 µM DOX or DMSO for 10 h. Levels of IRF1 were determined by western blot. Uncropped image of western blot shown in Fig. S9B. Quantification of replicate western blots in Fig. S4A. C A549 cells were mock treated or stimulated with IFN-β or IFN-γ over-night. Levels of IRF1 were determined by western blot. Uncropped image of western blot shown in Fig. S9C. Data with additional DOX-treatment in Fig. S4B. D–G Percentage of dead A549 cells with functional KO or OE of IRF1, or post IFN pre-stimulation relative to total cells counted over time (D–F) or 36 h (G) post DOX or γ-IR (20 Gy) treatment. DMSO controls shown in Fig. S4D, E, G. H Percentage of dead cells upon IFN-γ treatment in absence or presence of γ-IR (20 Gy) at 36 h. I A549 cells were γ-irradiated. After 10 h IRF1 protein levels were determined by western blot. Uncropped image of western blot shown in Fig. S9D. A, D–H Data shown represent the results of at least three biologically independent experiments.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Cooperative effects of RIG-I-like receptor signaling and IRF1 on DNA damage-induced cell death. Cell Death Dis (2022)
The subcellular localization and stability of DGAT2 is not altered in the absence of calnexin.(A) Immunoblot with anti-calnexin showing the efficient silencing of calnexin in HEK-293T cells with shRNAs (top panel). The control (NT) refers to HEK-293T cells transduced with a non-targeting shRNA. The bottom panel shows non-targeted and calnexin knockdown cells transiently transfected with FL-DGAT2 (2 right lanes). Untransfected cells (Untrans.) are the 2 left lanes. (B) Total cell extracts (TCE), crude mitochondria (Cr. Mito.) and microsomes (Micro.) were separated by SDS-PAGE and immunoblotted with anti-FLAG, anti-PDI and HSP70 antibodies. (C) Non-targeted and calnexin knockdown cells were transfected with FL-DGAT2 and treated with 0.5 mM oleate for 12 h. After fixation and permeabilization, cells were stained with anti-FLAG and BODIPY 493/503 to visualize lipid droplets. Scale bars: 10 μm. (D) 100 μg/mL CHX was added to the culture medium of HEK-293T (non-targeted and calnexin knockdown) cells expressing FL-DGAT2. Cells were harvested 0, 1 and 3 h after the addition of CHX. The amount of FL-DGAT2 and calnexin present after CHX treatment was determined by immunoblotting. (E) Quantification of the data in Fig 6E. Data are the mean of three independent experiments, performed in triplicate.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. PLoS One (2019)
Effect of cell-intrinsic antiviral signaling components on dsRNA-induced cell death and IRF1 expression.A A549 cells with functional KO of the indicated genes were mock stimulated with poly(C) or stimulated with 2 ng/ml 5’ppp-dsRNA for 6 h. IRF1 mRNA transcripts were determined by qRT-PCR; fold-induction over mock stimulation is shown. Non-normalized data shown in Fig. S6A + B. B–D Percentage of dead A549 cells with functional KO of the indicated genes relative to total cells counted over time (B, C) or 36 h (D) post dsRNA stimulation. Mock controls (poly[C] stimulation) shown in Fig. S6C + D. E–G A549 cells with functional KO of the indicated genes or administration of the indicated inhibitors were treated with 2 µM DOX or DMSO for 6 h. Levels of IRF1 were determined by western blot. Uncropped images of western blots shown in Fig. S9E–G. Quantification of replicate (n ≥ 3) western blots shown in Fig. S6H + I. A–D Data shown represent the results of at least three biologically independent experiments.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Cooperative effects of RIG-I-like receptor signaling and IRF1 on DNA damage-induced cell death. Cell Death Dis (2022)
Effect of cell-intrinsic antiviral signaling components on dsRNA-induced cell death and IRF1 expression.A A549 cells with functional KO of the indicated genes were mock stimulated with poly(C) or stimulated with 2 ng/ml 5’ppp-dsRNA for 6 h. IRF1 mRNA transcripts were determined by qRT-PCR; fold-induction over mock stimulation is shown. Non-normalized data shown in Fig. S6A + B. B–D Percentage of dead A549 cells with functional KO of the indicated genes relative to total cells counted over time (B, C) or 36 h (D) post dsRNA stimulation. Mock controls (poly[C] stimulation) shown in Fig. S6C + D. E–G A549 cells with functional KO of the indicated genes or administration of the indicated inhibitors were treated with 2 µM DOX or DMSO for 6 h. Levels of IRF1 were determined by western blot. Uncropped images of western blots shown in Fig. S9E–G. Quantification of replicate (n ≥ 3) western blots shown in Fig. S6H + I. A–D Data shown represent the results of at least three biologically independent experiments.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Cooperative effects of RIG-I-like receptor signaling and IRF1 on DNA damage-induced cell death. Cell Death Dis (2022)
Relevance of IRF1 on DNA damage-induced cell death.A A549 cells were treated with 1 µM DOX or DMSO for the indicated durations. IRF1 mRNA transcripts were determined by qRT-PCR. B A549 cells or A549 TP53−/− were treated with 1 µM DOX or DMSO for 10 h. Levels of IRF1 were determined by western blot. Uncropped image of western blot shown in Fig. S9B. Quantification of replicate western blots in Fig. S4A. C A549 cells were mock treated or stimulated with IFN-β or IFN-γ over-night. Levels of IRF1 were determined by western blot. Uncropped image of western blot shown in Fig. S9C. Data with additional DOX-treatment in Fig. S4B. D–G Percentage of dead A549 cells with functional KO or OE of IRF1, or post IFN pre-stimulation relative to total cells counted over time (D–F) or 36 h (G) post DOX or γ-IR (20 Gy) treatment. DMSO controls shown in Fig. S4D, E, G. H Percentage of dead cells upon IFN-γ treatment in absence or presence of γ-IR (20 Gy) at 36 h. I A549 cells were γ-irradiated. After 10 h IRF1 protein levels were determined by western blot. Uncropped image of western blot shown in Fig. S9D. A, D–H Data shown represent the results of at least three biologically independent experiments.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Cooperative effects of RIG-I-like receptor signaling and IRF1 on DNA damage-induced cell death. Cell Death Dis (2022)
Effect of cell-intrinsic antiviral signaling components on dsRNA-induced cell death and IRF1 expression.A A549 cells with functional KO of the indicated genes were mock stimulated with poly(C) or stimulated with 2 ng/ml 5’ppp-dsRNA for 6 h. IRF1 mRNA transcripts were determined by qRT-PCR; fold-induction over mock stimulation is shown. Non-normalized data shown in Fig. S6A + B. B–D Percentage of dead A549 cells with functional KO of the indicated genes relative to total cells counted over time (B, C) or 36 h (D) post dsRNA stimulation. Mock controls (poly[C] stimulation) shown in Fig. S6C + D. E–G A549 cells with functional KO of the indicated genes or administration of the indicated inhibitors were treated with 2 µM DOX or DMSO for 6 h. Levels of IRF1 were determined by western blot. Uncropped images of western blots shown in Fig. S9E–G. Quantification of replicate (n ≥ 3) western blots shown in Fig. S6H + I. A–D Data shown represent the results of at least three biologically independent experiments.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Cooperative effects of RIG-I-like receptor signaling and IRF1 on DNA damage-induced cell death. Cell Death Dis (2022)
The subcellular localization and stability of DGAT2 is not altered in the absence of calnexin.(A) Immunoblot with anti-calnexin showing the efficient silencing of calnexin in HEK-293T cells with shRNAs (top panel). The control (NT) refers to HEK-293T cells transduced with a non-targeting shRNA. The bottom panel shows non-targeted and calnexin knockdown cells transiently transfected with FL-DGAT2 (2 right lanes). Untransfected cells (Untrans.) are the 2 left lanes. (B) Total cell extracts (TCE), crude mitochondria (Cr. Mito.) and microsomes (Micro.) were separated by SDS-PAGE and immunoblotted with anti-FLAG, anti-PDI and HSP70 antibodies. (C) Non-targeted and calnexin knockdown cells were transfected with FL-DGAT2 and treated with 0.5 mM oleate for 12 h. After fixation and permeabilization, cells were stained with anti-FLAG and BODIPY 493/503 to visualize lipid droplets. Scale bars: 10 μm. (D) 100 μg/mL CHX was added to the culture medium of HEK-293T (non-targeted and calnexin knockdown) cells expressing FL-DGAT2. Cells were harvested 0, 1 and 3 h after the addition of CHX. The amount of FL-DGAT2 and calnexin present after CHX treatment was determined by immunoblotting. (E) Quantification of the data in Fig 6E. Data are the mean of three independent experiments, performed in triplicate.
Image collected and cropped by CiteAb under a CC-BY license from the following publication: Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. PLoS One (2019)
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RUO – Research Use Only |
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Related Products
| Application | ELISA, IHC, WB |
|---|---|
| Host | Goat |
| Species Reactivity | Rabbit |