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human embryo kidney tissue cells (ATCC)

Name: human embryo kidney tissue cells
Brand: ATCC
Rating: 99 (12297 reviews)

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ATCC human embryo kidney tissue cells
Human Embryo Kidney Tissue Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 12297 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/human embryo kidney tissue cells/product/ATCC
Average 99 stars, based on 12297 article reviews

human embryo kidney tissue cells - by Bioz Stars, 2026-03

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(A) WT, SPCS1 KO HEK293T, SPCS1 KO cells transfected with empty vector or FLAG-tagged SPCS1 were infected with RRV at an MOI of 3, and cells were collected for western blot analysis at 12 hpi using anti-FLAG and SPCS1 antibodies to confirm the protein level of SPCS1. (B) The lysates and supernatants were collected for FFU assays to determine the titers. (C) WT and SPCS1 KO HEK293T cells were infected with RRV, SA11 and UK strains at an MOI of 3. At 12 hpi, all the cell lysates and supernatants were collected for FFU assay to detect the titers. (D) WT and SPCS1 KO Huh7.5 cells were infected with RRV, SA11 and UK strains at an MOI of 3, respectively. At 12 hpi, all the cell lysates and supernatants were collected for FFU assay to detect the titers. (E) WT and SPCS1 KO HEK293T cells were transfected with siRNAs targeted against SPCS2 , SEC11A , SEC11C and a scrambled siRNA at the concentration of 20 nM. At 48 hpi, cells were infected with RRV at an MOI of 3. The cell lysates and supernatants were collected for FFU assay to detect the titers at 12 hpi. The results are the averages of data in three independent experiments and plotted as mean ± SD. Statistical significance was determined using two-way ANOVA with Sidak’s multiple comparisons test (**, P < 0.01; ***, P < 0.001, **** P < 0.0001).

Journal: bioRxiv

Article Title: Signal peptidase complex mediates rotavirus VP7 processing and virion assembly

doi: 10.1101/2025.11.04.686468

Figure Lengend Snippet: (A) WT, SPCS1 KO HEK293T, SPCS1 KO cells transfected with empty vector or FLAG-tagged SPCS1 were infected with RRV at an MOI of 3, and cells were collected for western blot analysis at 12 hpi using anti-FLAG and SPCS1 antibodies to confirm the protein level of SPCS1. (B) The lysates and supernatants were collected for FFU assays to determine the titers. (C) WT and SPCS1 KO HEK293T cells were infected with RRV, SA11 and UK strains at an MOI of 3. At 12 hpi, all the cell lysates and supernatants were collected for FFU assay to detect the titers. (D) WT and SPCS1 KO Huh7.5 cells were infected with RRV, SA11 and UK strains at an MOI of 3, respectively. At 12 hpi, all the cell lysates and supernatants were collected for FFU assay to detect the titers. (E) WT and SPCS1 KO HEK293T cells were transfected with siRNAs targeted against SPCS2 , SEC11A , SEC11C and a scrambled siRNA at the concentration of 20 nM. At 48 hpi, cells were infected with RRV at an MOI of 3. The cell lysates and supernatants were collected for FFU assay to detect the titers at 12 hpi. The results are the averages of data in three independent experiments and plotted as mean ± SD. Statistical significance was determined using two-way ANOVA with Sidak’s multiple comparisons test (**, P < 0.01; ***, P < 0.001, **** P < 0.0001).

Article Snippet: Human embryo kidney HEK293T cells (ATCC CRL-3216), were grown in Dulbecco’s modified Eagle’s medium (DMEM) (catalog number 11965118; Gibco) supplemented with 10% heat-inactivated fetal bovine serum (FBS) (catalog number 267820; Avantor).

Techniques: Transfection, Plasmid Preparation, Infection, Western Blot, Concentration Assay

(A) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3. At 4, 8, 12 hpi, the cells were collected for qRT-PCR analysis of viral mRNA level by detecting NSP5. The NSP5 level was normalized to that of GAPDH. Results are the average of data in triplicates and plotted as mean ± SD. (B) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3. At 4, 8, 12 hpi, the infected cells and mock cells were harvested for western blot analysis of viral protein level by detecting VP6 protein. (C) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3. At 12 hpi, an immunofluorescence assay was performed to detect the viroplasms in the infected cells. Cells were fixed and probed with in-house polyclonal antibody against NSP5; the positive cells were shown as green fluorescence. Nuclei were counterstained with DAPI. Representative data from one of three independent experiments are shown. Scale bar, 50 μm.

Journal: bioRxiv

Article Title: Signal peptidase complex mediates rotavirus VP7 processing and virion assembly

doi: 10.1101/2025.11.04.686468

Figure Lengend Snippet: (A) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3. At 4, 8, 12 hpi, the cells were collected for qRT-PCR analysis of viral mRNA level by detecting NSP5. The NSP5 level was normalized to that of GAPDH. Results are the average of data in triplicates and plotted as mean ± SD. (B) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3. At 4, 8, 12 hpi, the infected cells and mock cells were harvested for western blot analysis of viral protein level by detecting VP6 protein. (C) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3. At 12 hpi, an immunofluorescence assay was performed to detect the viroplasms in the infected cells. Cells were fixed and probed with in-house polyclonal antibody against NSP5; the positive cells were shown as green fluorescence. Nuclei were counterstained with DAPI. Representative data from one of three independent experiments are shown. Scale bar, 50 μm.

Techniques: Infection, Quantitative RT-PCR, Western Blot, Immunofluorescence, Fluorescence

(A) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3 for 12 hours, and the supernatants were subjected to density gradient ultracentrifugation. The TLP layer was extracted following CsCl gradient ultracentrifugation and detected by SDS-PAGE and followed by silver staining. (B) Western blot validation of TLPs from WT and SPCS1 KO HEK293T cells by probing TLP and VP7. (C) Electron micrograph (low magnification) of RRV-infected HEK293T WT cells. ‘V’ indicates the viroplasm. (D) Enlarged view of the area boxed in red in panel (C). Blue arrows indicate TLPs. (E) Electron micrograph (low magnification) of RRV-infected SPCS1 KO cells. ‘V’ indicates the viroplasm. (F) Enlarged view of the area boxed in red in panel (E). Magenta arrows indicate abnormal morphology of TLPs. Scale bars: low magnification, 50 nm; high magnification, 100 nm.

Journal: bioRxiv

Article Title: Signal peptidase complex mediates rotavirus VP7 processing and virion assembly

doi: 10.1101/2025.11.04.686468

Figure Lengend Snippet: (A) WT and SPCS1 KO HEK293T cells were infected with RRV at an MOI of 3 for 12 hours, and the supernatants were subjected to density gradient ultracentrifugation. The TLP layer was extracted following CsCl gradient ultracentrifugation and detected by SDS-PAGE and followed by silver staining. (B) Western blot validation of TLPs from WT and SPCS1 KO HEK293T cells by probing TLP and VP7. (C) Electron micrograph (low magnification) of RRV-infected HEK293T WT cells. ‘V’ indicates the viroplasm. (D) Enlarged view of the area boxed in red in panel (C). Blue arrows indicate TLPs. (E) Electron micrograph (low magnification) of RRV-infected SPCS1 KO cells. ‘V’ indicates the viroplasm. (F) Enlarged view of the area boxed in red in panel (E). Magenta arrows indicate abnormal morphology of TLPs. Scale bars: low magnification, 50 nm; high magnification, 100 nm.

Techniques: Infection, SDS Page, Silver Staining, Western Blot, Biomarker Discovery

(A) Schematic diagram of rotavirus VP7, cleavage site was indicated by an arrow. (B) WT and SPCS1 KO HEK293T cells were transfected with plasmids expressing -EV, - WT VP7, -A50V mutant VP7, -non-structural proteins NSP4, respectively. Those plasmids were all tagged with GFP. At 24 hours post-transfection, cells were harvested for western blot analysis by probing GFP. (C) Quantification of the cleavage ratio of WT and A50V mutant VP7 proteins in WT and SPCS1 KO HEK293T cells. The results are the averages of data in three independent experiments and plotted as mean ± SD. Statistical significance was determined by two-way ANOVA with Sidak’s multiple comparisons test (***, P < 0.001, **** P < 0.0001).

Journal: bioRxiv

Article Title: Signal peptidase complex mediates rotavirus VP7 processing and virion assembly

doi: 10.1101/2025.11.04.686468

Figure Lengend Snippet: (A) Schematic diagram of rotavirus VP7, cleavage site was indicated by an arrow. (B) WT and SPCS1 KO HEK293T cells were transfected with plasmids expressing -EV, - WT VP7, -A50V mutant VP7, -non-structural proteins NSP4, respectively. Those plasmids were all tagged with GFP. At 24 hours post-transfection, cells were harvested for western blot analysis by probing GFP. (C) Quantification of the cleavage ratio of WT and A50V mutant VP7 proteins in WT and SPCS1 KO HEK293T cells. The results are the averages of data in three independent experiments and plotted as mean ± SD. Statistical significance was determined by two-way ANOVA with Sidak’s multiple comparisons test (***, P < 0.001, **** P < 0.0001).

Techniques: Transfection, Expressing, Mutagenesis, Western Blot

(A) Alpha-Fold 3 prediction of VP7 with SPC complex (SPCS1, SPCS2, SPCS3, and SEC11A). (B) The magnification of the interaction site of VP7 and SPCS3 from (A). (C) Co-IP of SPCS1 with VP7 mutants. HEK293 cells were co-transfected with plasmids expressing SPCS1-FLAG with GFP-WT VP7, -E256R mutant VP7, -NSP4 and -EV, respectively. Cell lysates of transfected cells were immunoprecipitated with anti-GFP antibody. The resulting precipitates and whole-cell lysates used for immunoprecipitation were examined by immunoblot using anti-GFP and anti-FLAG antibodies. (D) WT and SPCS1 KO HEK293T cells were infected with rSA11-WT or rSA11-E256R at an MOI of 3. At 12 hpi, all the cell lysates and supernatants were collected for FFU assay to detect the titers. Statistical significance was determined by two-way ANOVA with Sidak’s multiple comparisons test (***, P < 0.001, **** P < 0.0001). (E) Samples were collected from WT HEK293T cells infected with rSA11-VP7-WT and rSA11-VP7-E256R in three independent experiments. The purified PCR products targeting the VP7 gene were subjected to Sanger sequencing, and the results are shown in the chart (right panel). Direct sequencing of VP7 from rSA11-VP7-WT and rSA11-VP7-E256R viruses served as controls. The red box indicates the codon of mutated amino acids.

Journal: bioRxiv

Article Title: Signal peptidase complex mediates rotavirus VP7 processing and virion assembly

doi: 10.1101/2025.11.04.686468

Figure Lengend Snippet: (A) Alpha-Fold 3 prediction of VP7 with SPC complex (SPCS1, SPCS2, SPCS3, and SEC11A). (B) The magnification of the interaction site of VP7 and SPCS3 from (A). (C) Co-IP of SPCS1 with VP7 mutants. HEK293 cells were co-transfected with plasmids expressing SPCS1-FLAG with GFP-WT VP7, -E256R mutant VP7, -NSP4 and -EV, respectively. Cell lysates of transfected cells were immunoprecipitated with anti-GFP antibody. The resulting precipitates and whole-cell lysates used for immunoprecipitation were examined by immunoblot using anti-GFP and anti-FLAG antibodies. (D) WT and SPCS1 KO HEK293T cells were infected with rSA11-WT or rSA11-E256R at an MOI of 3. At 12 hpi, all the cell lysates and supernatants were collected for FFU assay to detect the titers. Statistical significance was determined by two-way ANOVA with Sidak’s multiple comparisons test (***, P < 0.001, **** P < 0.0001). (E) Samples were collected from WT HEK293T cells infected with rSA11-VP7-WT and rSA11-VP7-E256R in three independent experiments. The purified PCR products targeting the VP7 gene were subjected to Sanger sequencing, and the results are shown in the chart (right panel). Direct sequencing of VP7 from rSA11-VP7-WT and rSA11-VP7-E256R viruses served as controls. The red box indicates the codon of mutated amino acids.

Techniques: Co-Immunoprecipitation Assay, Transfection, Expressing, Mutagenesis, Immunoprecipitation, Western Blot, Infection, Purification, Sequencing

The protein fragment complementation assay of the interactions between HHV-8 viral chemokines and CCR8. ( A ) Illustration of the NanoBiT-based protein fragment complementation assay of chemokine-receptor interaction. When a chemokine binds to its receptor on the plasma membrane of intact cells, their fused Small BiT (SmB; 1.3 kDa) and Large BiT (LgB; 17.6 kDa) fragments of Nano Luciferase (NLuc) are brought into proximity, which allows structural complementation thus yielding a functional enzyme acting on NLuc substrate, furimazine. ( B ) Schematic diagram of NanoBiT-fused CCR8. CCR8 was tagged with the bovine prolactin signal sequence (PSS) and the V5 epitope for efficient translocation into the endoplasmic reticulum and immunological detection of expression, respectively. ( C ) Immunofluorescence detection of cell surface expression of the NanoBiT-fused CCR8 protein transfected into 293T cells. DAPI (4’,6-diamidino-2-pheynylindole) was used to visualize cell nuclei. Red asterisks denote untransfected cells. Scale bar, 10 μm. ( D ) Schematic diagram of the NanoBiT-fused viral chemokines vCCL1 (D1-23) and vCCL2(D1-20), which lack their signal sequences. ( E ) Immunoblot detection of the NanoBiT-fused viral chemokines in the culture media. Red asterisks indicate the vCCL bands, and black asterisks indicate non-specific bands. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( F ) NanoBiT assays of vCCL-CCR8 interaction. The relative luminescence unit (RLU) was measured at 30 s after the mixture of the NanoBiT-fused vCCL and furimazine was added to the suspension of the NanoBiT-CCR8-transfected 293T cells. Each value represents the mean of triplicate samples from two independent experiments. Error bars represent standard deviations. The one-way ANOVA test was used to assess the statistical significance of differences between groups, and the t-test was used for post hoc comparisons. ***, p < 0.001.

Journal: Scientific Reports

Article Title: Nano-Luciferase complementation assay of human herpesvirus 8 chemo/cytokine-receptor interactions

doi: 10.1038/s41598-025-19281-3

Figure Lengend Snippet: The protein fragment complementation assay of the interactions between HHV-8 viral chemokines and CCR8. ( A ) Illustration of the NanoBiT-based protein fragment complementation assay of chemokine-receptor interaction. When a chemokine binds to its receptor on the plasma membrane of intact cells, their fused Small BiT (SmB; 1.3 kDa) and Large BiT (LgB; 17.6 kDa) fragments of Nano Luciferase (NLuc) are brought into proximity, which allows structural complementation thus yielding a functional enzyme acting on NLuc substrate, furimazine. ( B ) Schematic diagram of NanoBiT-fused CCR8. CCR8 was tagged with the bovine prolactin signal sequence (PSS) and the V5 epitope for efficient translocation into the endoplasmic reticulum and immunological detection of expression, respectively. ( C ) Immunofluorescence detection of cell surface expression of the NanoBiT-fused CCR8 protein transfected into 293T cells. DAPI (4’,6-diamidino-2-pheynylindole) was used to visualize cell nuclei. Red asterisks denote untransfected cells. Scale bar, 10 μm. ( D ) Schematic diagram of the NanoBiT-fused viral chemokines vCCL1 (D1-23) and vCCL2(D1-20), which lack their signal sequences. ( E ) Immunoblot detection of the NanoBiT-fused viral chemokines in the culture media. Red asterisks indicate the vCCL bands, and black asterisks indicate non-specific bands. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( F ) NanoBiT assays of vCCL-CCR8 interaction. The relative luminescence unit (RLU) was measured at 30 s after the mixture of the NanoBiT-fused vCCL and furimazine was added to the suspension of the NanoBiT-CCR8-transfected 293T cells. Each value represents the mean of triplicate samples from two independent experiments. Error bars represent standard deviations. The one-way ANOVA test was used to assess the statistical significance of differences between groups, and the t-test was used for post hoc comparisons. ***, p < 0.001.

Article Snippet: Human embryo kidney 293T (ATCC) and HeLa (ATCC) cell lines were cultured in DMEM media supplemented with 10% fetal bovine serum and 1% antibiotics of penicillin, streptomycin, and 1.5 μg/ml plasmocin (Invivogen) in a humidified incubator at 5% CO 2 at 37 °C.

Techniques: Protein-Fragment Complementation Assay, Clinical Proteomics, Membrane, Luciferase, Functional Assay, Sequencing, Translocation Assay, Expressing, Immunofluorescence, Transfection, Western Blot, Suspension

NanoBiT-based extensive analysis of human chemokine receptors interacting with HHV-8 chemokines. ( A ) V5-immunoblot analysis of the expression of twenty-five human chemokine receptors (CKRs) and the HHV-8-encoded viral chemokine receptor vGPCR. The CKRs were fused with PSS, LgB, and V5 as described in Fig. . 293T cells were transfected with the indicated CKR plasmids for 24 h, and whole-cell extracts were used for immunoblotting. EV indicates empty vector. The red asterisk indicates a non-specific immunoreactive band. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( B ) V5-immunofluorescence detection of cell surface expression of LgB-fused V5-CKRs transfected into 293T cells. Scale bar, 10 μm. Supplementary Fig. presents the original membranes of immunoblots. ( C ) NanoBiT analysis of vial chemokine-CKR interactions. The luminescence intensity was measured at 30 s after the mixture of SmB-fused vCCL (vCCL1, vCCL2, or vCCL3) and furimazine was added to the suspensions of cells expressing each LgB-fused V5-CKR. Each value in the heatmap indicates fold activation, determined by the ratio of RLU from treatment with each viral chemokine to the RLU from no treatment in CKR-transfected cells. Data represent the mean of triplicate samples from three independent experiments.

Journal: Scientific Reports

Article Title: Nano-Luciferase complementation assay of human herpesvirus 8 chemo/cytokine-receptor interactions

doi: 10.1038/s41598-025-19281-3

Figure Lengend Snippet: NanoBiT-based extensive analysis of human chemokine receptors interacting with HHV-8 chemokines. ( A ) V5-immunoblot analysis of the expression of twenty-five human chemokine receptors (CKRs) and the HHV-8-encoded viral chemokine receptor vGPCR. The CKRs were fused with PSS, LgB, and V5 as described in Fig. . 293T cells were transfected with the indicated CKR plasmids for 24 h, and whole-cell extracts were used for immunoblotting. EV indicates empty vector. The red asterisk indicates a non-specific immunoreactive band. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( B ) V5-immunofluorescence detection of cell surface expression of LgB-fused V5-CKRs transfected into 293T cells. Scale bar, 10 μm. Supplementary Fig. presents the original membranes of immunoblots. ( C ) NanoBiT analysis of vial chemokine-CKR interactions. The luminescence intensity was measured at 30 s after the mixture of SmB-fused vCCL (vCCL1, vCCL2, or vCCL3) and furimazine was added to the suspensions of cells expressing each LgB-fused V5-CKR. Each value in the heatmap indicates fold activation, determined by the ratio of RLU from treatment with each viral chemokine to the RLU from no treatment in CKR-transfected cells. Data represent the mean of triplicate samples from three independent experiments.

Techniques: Western Blot, Expressing, Transfection, Plasmid Preparation, Immunofluorescence, Activation Assay

NanoBiT assessment of vIL6-gp130-STAT3 interactions. ( A ) Schematic diagram of the vIL6 and gp130 proteins fused with the NanoBiT subunits at either their N- or C-termini. Expression of NanoBiT-tagged gp130 in 293T cells was examined using immunoblotting with anti-gp130 antibody. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( B ) NanoBiT assays of vIL6-gp130 interaction. The luminescence intensity was measured at 5 min after the mixture of NanoBiT-fused vIL6 and furimazine was added to the suspension of NanoBiT-gp130-transfected 293T cells. Each RLU value represents the mean of triplicate samples from a representative experiment. Error bars represent standard deviations. The one-way ANOVA test assessed the statistical significance of differences between groups, and the t-test was used for post hoc comparisons. **, p < 0.01; ***, p < 0.001. ( C ) Schematic diagram of the NanoBiT-fused FLAG-gp130 and mEGFP-STAT3 proteins. mEGFP refers to monomeric EGFP. ( D ) Co-immunoprecipitation assay of vIL-6-induced interaction of NanoBiT-fused gp130 and STAT3 proteins. 293T cells were single or double-transfected with plasmids encoding the indicated genes and, 24 h later, left untreated or treated with vIL-6-conditional medium for 5 min before cell lysis. FLAG-immunoprecipitates and cell extracts were immunoblotted with the indicated antibodies. The arrow indicates β-actin. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( E ) NanoBiT assays of vIL6-induced interaction between gp130 and STAT3. The luminescence intensity was recorded every minute for 10 min after the addition of empty vector-control medium or vIL6-conditional medium, together with furimazine, to the suspension of 293T cells transfected with Flag-gp130-LgB and/or mEGFP-STAT3-SmB. Each RLU value represents the mean of triplicate samples from a representative experiment. Error bars represent standard deviations.

Journal: Scientific Reports

Article Title: Nano-Luciferase complementation assay of human herpesvirus 8 chemo/cytokine-receptor interactions

doi: 10.1038/s41598-025-19281-3

Figure Lengend Snippet: NanoBiT assessment of vIL6-gp130-STAT3 interactions. ( A ) Schematic diagram of the vIL6 and gp130 proteins fused with the NanoBiT subunits at either their N- or C-termini. Expression of NanoBiT-tagged gp130 in 293T cells was examined using immunoblotting with anti-gp130 antibody. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( B ) NanoBiT assays of vIL6-gp130 interaction. The luminescence intensity was measured at 5 min after the mixture of NanoBiT-fused vIL6 and furimazine was added to the suspension of NanoBiT-gp130-transfected 293T cells. Each RLU value represents the mean of triplicate samples from a representative experiment. Error bars represent standard deviations. The one-way ANOVA test assessed the statistical significance of differences between groups, and the t-test was used for post hoc comparisons. **, p < 0.01; ***, p < 0.001. ( C ) Schematic diagram of the NanoBiT-fused FLAG-gp130 and mEGFP-STAT3 proteins. mEGFP refers to monomeric EGFP. ( D ) Co-immunoprecipitation assay of vIL-6-induced interaction of NanoBiT-fused gp130 and STAT3 proteins. 293T cells were single or double-transfected with plasmids encoding the indicated genes and, 24 h later, left untreated or treated with vIL-6-conditional medium for 5 min before cell lysis. FLAG-immunoprecipitates and cell extracts were immunoblotted with the indicated antibodies. The arrow indicates β-actin. Supplementary Fig. S4 presents the original membranes of the immunoblots. ( E ) NanoBiT assays of vIL6-induced interaction between gp130 and STAT3. The luminescence intensity was recorded every minute for 10 min after the addition of empty vector-control medium or vIL6-conditional medium, together with furimazine, to the suspension of 293T cells transfected with Flag-gp130-LgB and/or mEGFP-STAT3-SmB. Each RLU value represents the mean of triplicate samples from a representative experiment. Error bars represent standard deviations.

Techniques: Expressing, Western Blot, Suspension, Transfection, Co-Immunoprecipitation Assay, Lysis, Plasmid Preparation, Control

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