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DSMZ 8305c
Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, <t>8305C,</t> and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).
8305c, supplied by DSMZ, used in various techniques. Bioz Stars score: 93/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 32 article reviews
8305c - by Bioz Stars, 2026-06
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1) Product Images from "Optimized arenaviruses with tumor-tropic mutations promote safe anti-tumor efficacy via sustainable immune modulatory properties"

Article Title: Optimized arenaviruses with tumor-tropic mutations promote safe anti-tumor efficacy via sustainable immune modulatory properties

Journal: Cell Reports Medicine

doi: 10.1016/j.xcrm.2025.102411

Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, 8305C, and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).
Figure Legend Snippet: Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, 8305C, and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).

Techniques Used: Infection, Recombinant, Mutagenesis, Virus, Knock-Out, Control, Blocking Assay, Flow Cytometry



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Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, <t>8305C,</t> and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).
8305c, supplied by DSMZ, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, <t>8305C,</t> and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).
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Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, <t>8305C,</t> and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).
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Time-dependent inhibition of ATC-derived cell lines proliferation by ASA. Cells were seeded in 96-well plates, treated with ASA (10 mM for CAL-62, 5 mM for <t>8305C</t> and 8505C), and measured at 24-h time intervals. Data are reported as the mean ± SD.
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Image Search Results


Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, 8305C, and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).

Journal: Cell Reports Medicine

Article Title: Optimized arenaviruses with tumor-tropic mutations promote safe anti-tumor efficacy via sustainable immune modulatory properties

doi: 10.1016/j.xcrm.2025.102411

Figure Lengend Snippet: Analysis of different combinations of fast evolution mutations (A) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (lung adenocarcinoma: H1975 and A549; primary sarcoma: Gist-T1; melanoma metastasis: MaMel86a and MaMel51), myotubes and human skeletal muscle myoblasts (HSMM) ( n = 4–6; duplicates in 2–3 experimental replicates) with different recombinant viruses carrying a point mutation in the respective position. Notably, the GP mutation 492I always occurred alongside one single NP mutation. Hence, in all further analyses, the mention of mutation 492I mutation inherently includes the NP mutation, even if not explicitly stated. (B) Infection assays (MOI = 0.1, 16 h) of different murine cancer cells (oropharyngeal carcinoma: MOPC; Lewis lung carcinoma: LLC; prostate adenocarcinoma: TrampC2; colon adenocarcinoma: MC38) and human cancer cells (lung adenocarcinoma: H1975 and A549; melanoma metastasis: MaMel86a and MaMel51) ( n = 6; duplicates in 3 experimental replicates) using different recombinant viruses carrying specific point mutations. (C) Spider plots showing the factor of acceleration in propagation of the mutations tested in various human and murine tumor cells. The mean ratio for each mutated virus is given ( n = 4–6; duplicates in 2–3 experimental set ups). (D) Entry assay on human lung adenocarcinoma (A549) cells and A549-αDG knockout cells of recombination virus GP181M-185W-492I and control virus ( n = 6; duplicates in 3 independent experiments). (E) A549 lung adenocarcinoma cells were treated with CD164 blocking antibody or isotype control for 1 h and subsequently infected with the recombination virus GP181M-185W-492I (MOI 10) for 1, 5, and 15 min. The number of viral particles outside the cells per one cell is shown ( n = 6 cells analyzed per sample, ∗∗ p < 0.01). (F and G) Representative pictures for cells treated with isotype control (scale bars: left = 2 μm, right = 200 nm) (F) and CD164 blocking antibody (scale bars: left = 2 μm, right = 200 nm) (G) for 1 min of infection are shown. (H) Infection assays (MOI = 0.1, 16 h) of different human cancer cells (thyroid anaplastic carcinoma: Cal62, C643, 8305C, and 8505C; epidermoid carcinoma: A431; lung adenocarcinoma: KRAS-mutated: A549 and H23; EGFR-mutated: H1975, Alk-rearranged: H2228, WT/other: H1299, H1355, H1792, and H1373; small cell lung cancer: HCC-44; endocervical adenocarcinoma: HeLa; fibroblast liposarcoma: SW-872; colon adenocarcinoma: SW-480; bronchiole lung carcinoma: H358; hepatocellular carcinoma: HepG2) ( n = 6–8; duplicates in 3–4 experimental set ups) comparing WE, recombinant WE-CL13 and a recombinant virus carrying three point mutations as shown. For statistical analysis, WE-CL13-GP181M-185W-492I was compared to both WE and WE-CL13. (I) Hepatocytes ( n = 3; biological replicates; separate flasks), melanocytes ( n = 3; biological replicates; separate flasks), epithelial cells (InEpc, n = 3; biological replicates; separate flasks) and alveolar cells (ALI-cultures, n = 6; duplicates of 3 different patients) were infected with WE or WE-CL13-GP181M-185W-492I. Number of infected cells was determined 24 h with flow cytometry. For statistical analysis, the WE-CL13-GP181M-185W-492I virus was compared to the mock-infected control, but no significant difference was observed. However, a statistical difference between WE and WE-CL13-GP181M-185W-492I was detected. Data are presented as the mean ± SEM; ns = not significant, ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, and ∗∗∗∗ p < 0.0001 by t test (D, E, H, and I).

Article Snippet: 8305C (DSMZ: ACC133; RPMI-1640 with 10% FBS) and 8505C (DSMZ: ACC219; RPMI 1640 with 10% FBS) are human anaplastic thyroid carcinoma derived cells.

Techniques: Infection, Recombinant, Mutagenesis, Virus, Knock-Out, Control, Blocking Assay, Flow Cytometry

Figure 2. Immunofluorescence of 8305C cells stained with MC4R-antibody (A) and negative control (B), performed by omission of the primary antibody; immunofluorescence of HT-29 cells stained with MC4R-antibody (C) and negative control (D).

Journal: Journal of clinical medicine

Article Title: Melanocortin-4 Receptor Antagonism Inhibits Colorectal and Anaplastic Thyroid Cancer In Vitro and In Vivo.

doi: 10.3390/jcm14041165

Figure Lengend Snippet: Figure 2. Immunofluorescence of 8305C cells stained with MC4R-antibody (A) and negative control (B), performed by omission of the primary antibody; immunofluorescence of HT-29 cells stained with MC4R-antibody (C) and negative control (D).

Article Snippet: The Human ATC cell line 8305C with BRAF V600E mutation (ACC 133) was bought from the Leibniz Institute DSMZ-German Collection of Microorganisms and Cell Cultures GmbH (DSMZ, Germany).

Techniques: Immunofluorescence, Staining, Negative Control

Figure 5. Combination Index (CI)-fraction affected (Fa) plot at 72h concomitant combination treatment of ML+ vinorelbine in HT-29 cells proliferation inhibition. The symbols represent the combination in- dex values (synergism CI < 1) per fraction of cells affected by the combination (A). The 3-dimensional landscape of the dose matrix of combination responses for ML and vinorelbine based on the Loewe model in HT-29 (C), where blue reflects evidence of synergy and red represents evidence of antag- onism. Combination Index (CI)-fraction affected (Fa) plot of 72h concomitant combination of ML+ SN-38 in 8305C cell proliferation inhibition. The symbols represent the combination index values (synergism CI < 1) per fraction of cells affected by the combination (B). The 3-dimensional landscape of the dose matrix of combination responses for ML and SN-38 based on the Loewe model in 8305C (D), where blue reflects evidence of synergy and red represents evidence of antagonism.

Journal: Journal of clinical medicine

Article Title: Melanocortin-4 Receptor Antagonism Inhibits Colorectal and Anaplastic Thyroid Cancer In Vitro and In Vivo.

doi: 10.3390/jcm14041165

Figure Lengend Snippet: Figure 5. Combination Index (CI)-fraction affected (Fa) plot at 72h concomitant combination treatment of ML+ vinorelbine in HT-29 cells proliferation inhibition. The symbols represent the combination in- dex values (synergism CI < 1) per fraction of cells affected by the combination (A). The 3-dimensional landscape of the dose matrix of combination responses for ML and vinorelbine based on the Loewe model in HT-29 (C), where blue reflects evidence of synergy and red represents evidence of antag- onism. Combination Index (CI)-fraction affected (Fa) plot of 72h concomitant combination of ML+ SN-38 in 8305C cell proliferation inhibition. The symbols represent the combination index values (synergism CI < 1) per fraction of cells affected by the combination (B). The 3-dimensional landscape of the dose matrix of combination responses for ML and SN-38 based on the Loewe model in 8305C (D), where blue reflects evidence of synergy and red represents evidence of antagonism.

Article Snippet: The Human ATC cell line 8305C with BRAF V600E mutation (ACC 133) was bought from the Leibniz Institute DSMZ-German Collection of Microorganisms and Cell Cultures GmbH (DSMZ, Germany).

Techniques: Inhibition

Figure 9. Representative microscopic images of immunohistochemical staining of subcutaneous tumor samples 8305C treated with saline (control), ML00253764 (ML), and vinorelbine (VNR) at the end of a 17-day treatment, including active caspase 3 (A and B, respectively) and CD31 (C and D, respectively). Magnification, ×20.

Journal: Journal of clinical medicine

Article Title: Melanocortin-4 Receptor Antagonism Inhibits Colorectal and Anaplastic Thyroid Cancer In Vitro and In Vivo.

doi: 10.3390/jcm14041165

Figure Lengend Snippet: Figure 9. Representative microscopic images of immunohistochemical staining of subcutaneous tumor samples 8305C treated with saline (control), ML00253764 (ML), and vinorelbine (VNR) at the end of a 17-day treatment, including active caspase 3 (A and B, respectively) and CD31 (C and D, respectively). Magnification, ×20.

Article Snippet: The Human ATC cell line 8305C with BRAF V600E mutation (ACC 133) was bought from the Leibniz Institute DSMZ-German Collection of Microorganisms and Cell Cultures GmbH (DSMZ, Germany).

Techniques: Immunohistochemical staining, Staining, Saline, Control

Time-dependent inhibition of ATC-derived cell lines proliferation by ASA. Cells were seeded in 96-well plates, treated with ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), and measured at 24-h time intervals. Data are reported as the mean ± SD.

Journal: Cancers

Article Title: The Potential Therapeutic Value of Aspirin in Anaplastic Thyroid Cancer

doi: 10.3390/cancers16244203

Figure Lengend Snippet: Time-dependent inhibition of ATC-derived cell lines proliferation by ASA. Cells were seeded in 96-well plates, treated with ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), and measured at 24-h time intervals. Data are reported as the mean ± SD.

Article Snippet: The human ATC-derived cell lines 8305C, 8505C, and CAL-62 were purchased from DSMZ (Braunschweig, Germany).

Techniques: Inhibition, Derivative Assay

Effects of ASA on the anchorage-independent growth of ATC cells. Cells were grown in a soft agar gel mixed with cell culture medium ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C) for two weeks. Photos were finally acquired, and colonies having diameter ≥50 μm were counted. Bars represent the mean ± SE of three independent experiments. N.D., not detectable. ** p < 0.01; *** p < 0.001.

Journal: Cancers

Article Title: The Potential Therapeutic Value of Aspirin in Anaplastic Thyroid Cancer

doi: 10.3390/cancers16244203

Figure Lengend Snippet: Effects of ASA on the anchorage-independent growth of ATC cells. Cells were grown in a soft agar gel mixed with cell culture medium ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C) for two weeks. Photos were finally acquired, and colonies having diameter ≥50 μm were counted. Bars represent the mean ± SE of three independent experiments. N.D., not detectable. ** p < 0.01; *** p < 0.001.

Article Snippet: The human ATC-derived cell lines 8305C, 8505C, and CAL-62 were purchased from DSMZ (Braunschweig, Germany).

Techniques: Cell Culture

Phosphorylation status of Akt and MAPK in ATC-derived cell lines treated with ASA. Cells were incubated for 24 h ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), then protein extracts were prepared and analyzed by Western blot. Panel ( A ) Images from western blot. Panel ( B ) densitometric analyses. Bars represent the mean ± SE of three independent experiments. *, p < 0.05; ***, p < 0.001. Original western blots are presented in .

Journal: Cancers

Article Title: The Potential Therapeutic Value of Aspirin in Anaplastic Thyroid Cancer

doi: 10.3390/cancers16244203

Figure Lengend Snippet: Phosphorylation status of Akt and MAPK in ATC-derived cell lines treated with ASA. Cells were incubated for 24 h ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), then protein extracts were prepared and analyzed by Western blot. Panel ( A ) Images from western blot. Panel ( B ) densitometric analyses. Bars represent the mean ± SE of three independent experiments. *, p < 0.05; ***, p < 0.001. Original western blots are presented in .

Article Snippet: The human ATC-derived cell lines 8305C, 8505C, and CAL-62 were purchased from DSMZ (Braunschweig, Germany).

Techniques: Derivative Assay, Incubation, Western Blot

Time-dependent inhibition of ATC-derived cell lines proliferation by ASA. Cells were seeded in 96-well plates, treated with ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), and measured at 24-h time intervals. Data are reported as the mean ± SD.

Journal: Cancers

Article Title: The Potential Therapeutic Value of Aspirin in Anaplastic Thyroid Cancer

doi: 10.3390/cancers16244203

Figure Lengend Snippet: Time-dependent inhibition of ATC-derived cell lines proliferation by ASA. Cells were seeded in 96-well plates, treated with ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), and measured at 24-h time intervals. Data are reported as the mean ± SD.

Article Snippet: The human ATC-derived cell lines 8305C, 8505C, and CAL-62 were purchased from DSMZ (Braunschweig, Germany).

Techniques: Inhibition, Derivative Assay

Effects of ASA on the anchorage-independent growth of ATC cells. Cells were grown in a soft agar gel mixed with cell culture medium ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C) for two weeks. Photos were finally acquired, and colonies having diameter ≥50 μm were counted. Bars represent the mean ± SE of three independent experiments. N.D., not detectable. ** p < 0.01; *** p < 0.001.

Journal: Cancers

Article Title: The Potential Therapeutic Value of Aspirin in Anaplastic Thyroid Cancer

doi: 10.3390/cancers16244203

Figure Lengend Snippet: Effects of ASA on the anchorage-independent growth of ATC cells. Cells were grown in a soft agar gel mixed with cell culture medium ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C) for two weeks. Photos were finally acquired, and colonies having diameter ≥50 μm were counted. Bars represent the mean ± SE of three independent experiments. N.D., not detectable. ** p < 0.01; *** p < 0.001.

Article Snippet: The human ATC-derived cell lines 8305C, 8505C, and CAL-62 were purchased from DSMZ (Braunschweig, Germany).

Techniques: Cell Culture

Phosphorylation status of Akt and MAPK in ATC-derived cell lines treated with ASA. Cells were incubated for 24 h ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), then protein extracts were prepared and analyzed by Western blot. Panel ( A ) Images from western blot. Panel ( B ) densitometric analyses. Bars represent the mean ± SE of three independent experiments. *, p < 0.05; ***, p < 0.001. Original western blots are presented in .

Journal: Cancers

Article Title: The Potential Therapeutic Value of Aspirin in Anaplastic Thyroid Cancer

doi: 10.3390/cancers16244203

Figure Lengend Snippet: Phosphorylation status of Akt and MAPK in ATC-derived cell lines treated with ASA. Cells were incubated for 24 h ± ASA (10 mM for CAL-62, 5 mM for 8305C and 8505C), then protein extracts were prepared and analyzed by Western blot. Panel ( A ) Images from western blot. Panel ( B ) densitometric analyses. Bars represent the mean ± SE of three independent experiments. *, p < 0.05; ***, p < 0.001. Original western blots are presented in .

Article Snippet: The human ATC-derived cell lines 8305C, 8505C, and CAL-62 were purchased from DSMZ (Braunschweig, Germany).

Techniques: Phospho-proteomics, Derivative Assay, Incubation, Western Blot