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Biowest SAS fetal bovine serum fbs
Crizotinib-induced apoptosis in Ba/F3 cells transformed by NPM-ALK. Ba/F3 cells were infected with an empty virus (-) and retrovirus expressing NPM-ALK or TEL-JAK2. (A) Whole cell lysates were immunoblotted with an anti-ALK antibody, anti-Flag antibody, anti-JAK2 antibody, anti-phospho-STAT3 antibody, anti-STAT3 antibody, anti-phospho-STAT5 antibody, anti-STAT5 antibody or anti-β-actin antibody. (B) Transduced Ba/F3 cells were incubated with <t>RPMI</t> containing 10% <t>FBS</t> in the absence of IL-3 for 2 days. Viable cell numbers at 24 hr and 48 hr were counted by the Trypan blue exclusion method. Values are the mean ± SD of three independent experiments. (C-F) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the presence of crizotinib (0.25, 0.5, 1 μM) and MMC (0.1, 1, 10 μg/mL) for 24 hr. (C) Cell viability was measured by the WST assay. Values are the mean ± S.D. of four independent experiments. (D) Cells were fixed, treated with propidium iodide, and subjected to a flow cytometric analysis. The percentages of cells in the sub-G1 phase were graphed. Values are the mean ± S.D. of four independent experiments. (E) To evaluate the apoptotic cell death, the chromatin DNA was isolated from cells and subjected to agarose gel electrophoresis. (F) Whole cell lysates were prepared and the phosphorylation of STAT3 and STAT5 was analyzed by immunoblotting. The relative phosphorylation level of STAT3 and STAT5 is shown in the graphs. Values are given as the mean ± SD of three independent experiments. *** P
Fetal Bovine Serum Fbs, supplied by Biowest SAS, used in various techniques. Bioz Stars score: 92/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Alpha-tocopherol attenuates the anti-tumor activity of crizotinib against cells transformed by NPM-ALK"

Article Title: Alpha-tocopherol attenuates the anti-tumor activity of crizotinib against cells transformed by NPM-ALK

Journal: PLoS ONE

doi: 10.1371/journal.pone.0183003

Crizotinib-induced apoptosis in Ba/F3 cells transformed by NPM-ALK. Ba/F3 cells were infected with an empty virus (-) and retrovirus expressing NPM-ALK or TEL-JAK2. (A) Whole cell lysates were immunoblotted with an anti-ALK antibody, anti-Flag antibody, anti-JAK2 antibody, anti-phospho-STAT3 antibody, anti-STAT3 antibody, anti-phospho-STAT5 antibody, anti-STAT5 antibody or anti-β-actin antibody. (B) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the absence of IL-3 for 2 days. Viable cell numbers at 24 hr and 48 hr were counted by the Trypan blue exclusion method. Values are the mean ± SD of three independent experiments. (C-F) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the presence of crizotinib (0.25, 0.5, 1 μM) and MMC (0.1, 1, 10 μg/mL) for 24 hr. (C) Cell viability was measured by the WST assay. Values are the mean ± S.D. of four independent experiments. (D) Cells were fixed, treated with propidium iodide, and subjected to a flow cytometric analysis. The percentages of cells in the sub-G1 phase were graphed. Values are the mean ± S.D. of four independent experiments. (E) To evaluate the apoptotic cell death, the chromatin DNA was isolated from cells and subjected to agarose gel electrophoresis. (F) Whole cell lysates were prepared and the phosphorylation of STAT3 and STAT5 was analyzed by immunoblotting. The relative phosphorylation level of STAT3 and STAT5 is shown in the graphs. Values are given as the mean ± SD of three independent experiments. *** P
Figure Legend Snippet: Crizotinib-induced apoptosis in Ba/F3 cells transformed by NPM-ALK. Ba/F3 cells were infected with an empty virus (-) and retrovirus expressing NPM-ALK or TEL-JAK2. (A) Whole cell lysates were immunoblotted with an anti-ALK antibody, anti-Flag antibody, anti-JAK2 antibody, anti-phospho-STAT3 antibody, anti-STAT3 antibody, anti-phospho-STAT5 antibody, anti-STAT5 antibody or anti-β-actin antibody. (B) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the absence of IL-3 for 2 days. Viable cell numbers at 24 hr and 48 hr were counted by the Trypan blue exclusion method. Values are the mean ± SD of three independent experiments. (C-F) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the presence of crizotinib (0.25, 0.5, 1 μM) and MMC (0.1, 1, 10 μg/mL) for 24 hr. (C) Cell viability was measured by the WST assay. Values are the mean ± S.D. of four independent experiments. (D) Cells were fixed, treated with propidium iodide, and subjected to a flow cytometric analysis. The percentages of cells in the sub-G1 phase were graphed. Values are the mean ± S.D. of four independent experiments. (E) To evaluate the apoptotic cell death, the chromatin DNA was isolated from cells and subjected to agarose gel electrophoresis. (F) Whole cell lysates were prepared and the phosphorylation of STAT3 and STAT5 was analyzed by immunoblotting. The relative phosphorylation level of STAT3 and STAT5 is shown in the graphs. Values are given as the mean ± SD of three independent experiments. *** P

Techniques Used: Transformation Assay, Infection, Expressing, Incubation, WST Assay, Flow Cytometry, Isolation, Agarose Gel Electrophoresis

2) Product Images from "JS-K, a glutathione/glutathione S-transferase-activated nitric oxide releasing prodrug inhibits androgen receptor and WNT-signaling in prostate cancer cells"

Article Title: JS-K, a glutathione/glutathione S-transferase-activated nitric oxide releasing prodrug inhibits androgen receptor and WNT-signaling in prostate cancer cells

Journal: BMC Cancer

doi: 10.1186/1471-2407-12-130

Release of NO from JS-K . (A) Generation of NO from JS-K in RPMI-1640 medium containing 10% fetal bovine serum was determined indirectly by photorimetric detection of nitrite according to Green et al. [ 31 ]. (B) Detection of nitrotyrosine by fluorescence microscopy in 22Rv1 cells: Generation of intracellular NO was detected indirectly by detection of nitrotyrosine (green). Cell nuclei were stained with DAPI. [A] untreated cells, [B] 2 μM JS-K neg , [C] 2 μM JS-K, [D] 200 μM DETA/NO.
Figure Legend Snippet: Release of NO from JS-K . (A) Generation of NO from JS-K in RPMI-1640 medium containing 10% fetal bovine serum was determined indirectly by photorimetric detection of nitrite according to Green et al. [ 31 ]. (B) Detection of nitrotyrosine by fluorescence microscopy in 22Rv1 cells: Generation of intracellular NO was detected indirectly by detection of nitrotyrosine (green). Cell nuclei were stained with DAPI. [A] untreated cells, [B] 2 μM JS-K neg , [C] 2 μM JS-K, [D] 200 μM DETA/NO.

Techniques Used: Fluorescence, Microscopy, Staining

3) Product Images from "Rice bran extract affects differentiation of mesenchymal stem cells potency into osteogenic cells"

Article Title: Rice bran extract affects differentiation of mesenchymal stem cells potency into osteogenic cells

Journal: Cytotechnology

doi: 10.1007/s10616-013-9570-6

Effect of RBE on rMSC differentiation a after rMSCs (passage = 1–3) were cultured for 3 days in serum-free STK1 medium or α-MEM supplemented with 15 % FBS with or without RBE. Cells were subsequently cultured
Figure Legend Snippet: Effect of RBE on rMSC differentiation a after rMSCs (passage = 1–3) were cultured for 3 days in serum-free STK1 medium or α-MEM supplemented with 15 % FBS with or without RBE. Cells were subsequently cultured

Techniques Used: Cell Culture

Effect of RBE on rMSC morphology. rMSCs (passage = 3) were cultured for 3 days in α-MEM supplemented with 15 % FBS or STK1, with or without RBE. The scale bar represents 90 μm
Figure Legend Snippet: Effect of RBE on rMSC morphology. rMSCs (passage = 3) were cultured for 3 days in α-MEM supplemented with 15 % FBS or STK1, with or without RBE. The scale bar represents 90 μm

Techniques Used: Cell Culture

4) Product Images from "Catalyser-21TM, a mineral water derived from leaf soil, inhibits tumor cell invasion and angiogenesis"

Article Title: Catalyser-21TM, a mineral water derived from leaf soil, inhibits tumor cell invasion and angiogenesis

Journal: Cytotechnology

doi: 10.1007/s10616-007-9073-4

Detection of H 2 O 2 scavenging activity of Catalyser-21 TM . Cultured HeLa cells were pretreated for 30 min with MEM containing 10% FBS with 3% Catalyser-21 TM , then incubated with 5 μM DCFH-DA for 30 min at 37°C. The fluorescence intensity of DCF was measured with a flow cytometer. The fluorescence intensity relative to that of control cells is presented as curves. Curve (a) is the fluorescence intensity obtained from control HeLa cells. Curve (b) is the fluorescence intensity obtained from HeLa cells treated with 3% Catalyser-21 TM . H 2 O 2 scavenging activity was judged positive, as the Catalyser-21 TM -treatment curve (b) was shifted to the left compared with the control curve (a)
Figure Legend Snippet: Detection of H 2 O 2 scavenging activity of Catalyser-21 TM . Cultured HeLa cells were pretreated for 30 min with MEM containing 10% FBS with 3% Catalyser-21 TM , then incubated with 5 μM DCFH-DA for 30 min at 37°C. The fluorescence intensity of DCF was measured with a flow cytometer. The fluorescence intensity relative to that of control cells is presented as curves. Curve (a) is the fluorescence intensity obtained from control HeLa cells. Curve (b) is the fluorescence intensity obtained from HeLa cells treated with 3% Catalyser-21 TM . H 2 O 2 scavenging activity was judged positive, as the Catalyser-21 TM -treatment curve (b) was shifted to the left compared with the control curve (a)

Techniques Used: Activity Assay, Cell Culture, Incubation, Fluorescence, Flow Cytometry, Cytometry

Suppression of VEGF transcription ( A ) and protein secretion ( B ) in HeLa cells by Catalyser-21 TM . ( A ) HeLa cells were cultured for 24 h in MEM containing 10% FBS. The culture medium was then removed and serum-free MEM containing 3% Catalyser-21 TM was added, followed by an additional 24 h incubation. VEGF and GAPDH transcripts were detected by RT-PCR using total RNA isolated from the treated and untreated HeLa cells and appropriately designed primers. Lane a, DNA fragments were amplified from total RNA of untreated HeLa cells. Lane b, DNA fragments were amplified from total RNA of 3% Catalyser-21 TM -treated HeLa cells. Amplified products were resolved by agarose gel electrophoresis and photographs were documented by a digital camera. Recorded images were analyzed by the NIH Image analyzer program (Image 1.62f ) using a personal computer. Values below the panel were normalized by arbitrarily setting the density of the VEGF 165 and VEGF 121 bands of untreated HeLa cells to 1.0. GAPDH transcripts were used as an internal control for cellular activity. ( B ) HeLa cells were treated as above and each supernatant was collected to measure VEGF secretion. The procedure for VEGF protein measurement is described in the Materials and methods. Differences were analyzed by Student’s t test (values are the mean ± SD; n = 3) and the asterisk represents a significant difference compared with the control (* p
Figure Legend Snippet: Suppression of VEGF transcription ( A ) and protein secretion ( B ) in HeLa cells by Catalyser-21 TM . ( A ) HeLa cells were cultured for 24 h in MEM containing 10% FBS. The culture medium was then removed and serum-free MEM containing 3% Catalyser-21 TM was added, followed by an additional 24 h incubation. VEGF and GAPDH transcripts were detected by RT-PCR using total RNA isolated from the treated and untreated HeLa cells and appropriately designed primers. Lane a, DNA fragments were amplified from total RNA of untreated HeLa cells. Lane b, DNA fragments were amplified from total RNA of 3% Catalyser-21 TM -treated HeLa cells. Amplified products were resolved by agarose gel electrophoresis and photographs were documented by a digital camera. Recorded images were analyzed by the NIH Image analyzer program (Image 1.62f ) using a personal computer. Values below the panel were normalized by arbitrarily setting the density of the VEGF 165 and VEGF 121 bands of untreated HeLa cells to 1.0. GAPDH transcripts were used as an internal control for cellular activity. ( B ) HeLa cells were treated as above and each supernatant was collected to measure VEGF secretion. The procedure for VEGF protein measurement is described in the Materials and methods. Differences were analyzed by Student’s t test (values are the mean ± SD; n = 3) and the asterisk represents a significant difference compared with the control (* p

Techniques Used: Cell Culture, Incubation, Reverse Transcription Polymerase Chain Reaction, Isolation, Amplification, Agarose Gel Electrophoresis, Activity Assay

Effect of Catalyser-21 TM on HeLa cell proliferation. HeLa cells were cultured in a 24-well microtiter plate with MEM containing 10% FBS for 24 h. The culture medium was then removed and replaced with MEM containing 10% FBS and various concentrations (3–50%) of Catalyser-21 TM , and the cells were incubated for another 24 h. A WST-1 assay was performed, and the data are expressed as the mean ± SD of three independent experiments
Figure Legend Snippet: Effect of Catalyser-21 TM on HeLa cell proliferation. HeLa cells were cultured in a 24-well microtiter plate with MEM containing 10% FBS for 24 h. The culture medium was then removed and replaced with MEM containing 10% FBS and various concentrations (3–50%) of Catalyser-21 TM , and the cells were incubated for another 24 h. A WST-1 assay was performed, and the data are expressed as the mean ± SD of three independent experiments

Techniques Used: Cell Culture, Incubation, WST-1 Assay

Suppression of MMP-2 expression ( A ) and invasiveness ( B ) of HT1080 cells by Catalyser-21 TM . ( A ) HT1080 cells were cultured for 24 h with MEM containing 10% FBS. The culture medium was replaced by fresh serum-free MEM containing Catalyser-21 TM and the cells were incubated for another 24 h. Total RNA was purified from Catalyser-21 TM -treated and untreated HT1080 cells and used for RT-PCR templates. Amplified products were resolved by agarose gel electrophoresis and analyzed as described in the legend of Fig. 3. Lane a, DNA fragments amplified from total RNA of untreated HT1080 cells. Lane b, DNA fragments amplified from total RNA of 3% Catalyser-21 TM -treated HT1080 cells. Values below the panels were normalized by arbitrarily setting the density of the MMP-2 and GAPDH bands of untreated HT1080 cells to 1.0. GAPDH transcripts were used as an internal control for cellular activity. ( B ) HT1080 cells were pretreated with Catalyser-21 TM for 24 h and then inoculated at 1 × 10 5 cells/well of the Matrigel chamber. The chambers were incubated at 37°C for 12 h, after which the cells that had invaded the lower collagen surface were fixed and stained with Diff-Quick (Sysmex, IL, USA). The invading cells were counted in three random fields under a light microscope. Differences were analyzed by Student’s t test (values are the mean ± SD; n = 3) and the asterisk represents a significant difference compared with the control (* p
Figure Legend Snippet: Suppression of MMP-2 expression ( A ) and invasiveness ( B ) of HT1080 cells by Catalyser-21 TM . ( A ) HT1080 cells were cultured for 24 h with MEM containing 10% FBS. The culture medium was replaced by fresh serum-free MEM containing Catalyser-21 TM and the cells were incubated for another 24 h. Total RNA was purified from Catalyser-21 TM -treated and untreated HT1080 cells and used for RT-PCR templates. Amplified products were resolved by agarose gel electrophoresis and analyzed as described in the legend of Fig. 3. Lane a, DNA fragments amplified from total RNA of untreated HT1080 cells. Lane b, DNA fragments amplified from total RNA of 3% Catalyser-21 TM -treated HT1080 cells. Values below the panels were normalized by arbitrarily setting the density of the MMP-2 and GAPDH bands of untreated HT1080 cells to 1.0. GAPDH transcripts were used as an internal control for cellular activity. ( B ) HT1080 cells were pretreated with Catalyser-21 TM for 24 h and then inoculated at 1 × 10 5 cells/well of the Matrigel chamber. The chambers were incubated at 37°C for 12 h, after which the cells that had invaded the lower collagen surface were fixed and stained with Diff-Quick (Sysmex, IL, USA). The invading cells were counted in three random fields under a light microscope. Differences were analyzed by Student’s t test (values are the mean ± SD; n = 3) and the asterisk represents a significant difference compared with the control (* p

Techniques Used: Expressing, Cell Culture, Incubation, Purification, Reverse Transcription Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis, Activity Assay, Staining, Diff-Quik, Light Microscopy

5) Product Images from "Alpha-tocopherol attenuates the anti-tumor activity of crizotinib against cells transformed by NPM-ALK"

Article Title: Alpha-tocopherol attenuates the anti-tumor activity of crizotinib against cells transformed by NPM-ALK

Journal: PLoS ONE

doi: 10.1371/journal.pone.0183003

Crizotinib-induced apoptosis in Ba/F3 cells transformed by NPM-ALK. Ba/F3 cells were infected with an empty virus (-) and retrovirus expressing NPM-ALK or TEL-JAK2. (A) Whole cell lysates were immunoblotted with an anti-ALK antibody, anti-Flag antibody, anti-JAK2 antibody, anti-phospho-STAT3 antibody, anti-STAT3 antibody, anti-phospho-STAT5 antibody, anti-STAT5 antibody or anti-β-actin antibody. (B) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the absence of IL-3 for 2 days. Viable cell numbers at 24 hr and 48 hr were counted by the Trypan blue exclusion method. Values are the mean ± SD of three independent experiments. (C-F) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the presence of crizotinib (0.25, 0.5, 1 μM) and MMC (0.1, 1, 10 μg/mL) for 24 hr. (C) Cell viability was measured by the WST assay. Values are the mean ± S.D. of four independent experiments. (D) Cells were fixed, treated with propidium iodide, and subjected to a flow cytometric analysis. The percentages of cells in the sub-G1 phase were graphed. Values are the mean ± S.D. of four independent experiments. (E) To evaluate the apoptotic cell death, the chromatin DNA was isolated from cells and subjected to agarose gel electrophoresis. (F) Whole cell lysates were prepared and the phosphorylation of STAT3 and STAT5 was analyzed by immunoblotting. The relative phosphorylation level of STAT3 and STAT5 is shown in the graphs. Values are given as the mean ± SD of three independent experiments. *** P
Figure Legend Snippet: Crizotinib-induced apoptosis in Ba/F3 cells transformed by NPM-ALK. Ba/F3 cells were infected with an empty virus (-) and retrovirus expressing NPM-ALK or TEL-JAK2. (A) Whole cell lysates were immunoblotted with an anti-ALK antibody, anti-Flag antibody, anti-JAK2 antibody, anti-phospho-STAT3 antibody, anti-STAT3 antibody, anti-phospho-STAT5 antibody, anti-STAT5 antibody or anti-β-actin antibody. (B) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the absence of IL-3 for 2 days. Viable cell numbers at 24 hr and 48 hr were counted by the Trypan blue exclusion method. Values are the mean ± SD of three independent experiments. (C-F) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the presence of crizotinib (0.25, 0.5, 1 μM) and MMC (0.1, 1, 10 μg/mL) for 24 hr. (C) Cell viability was measured by the WST assay. Values are the mean ± S.D. of four independent experiments. (D) Cells were fixed, treated with propidium iodide, and subjected to a flow cytometric analysis. The percentages of cells in the sub-G1 phase were graphed. Values are the mean ± S.D. of four independent experiments. (E) To evaluate the apoptotic cell death, the chromatin DNA was isolated from cells and subjected to agarose gel electrophoresis. (F) Whole cell lysates were prepared and the phosphorylation of STAT3 and STAT5 was analyzed by immunoblotting. The relative phosphorylation level of STAT3 and STAT5 is shown in the graphs. Values are given as the mean ± SD of three independent experiments. *** P

Techniques Used: Transformation Assay, Infection, Expressing, Incubation, WST Assay, Flow Cytometry, Isolation, Agarose Gel Electrophoresis

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Modification:

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Article Snippet: .. Dulbecco’s Modified Eagle’s Medium (DMEM), fetal bovine serum (FBS), and penicillin/streptomycin were purchased from Biowest (Riverside, MO, USA). ..

Article Title: Catalyser-21TM, a mineral water derived from leaf soil, inhibits tumor cell invasion and angiogenesis
Article Snippet: .. HeLa cells (a human cervical cancer cell line), HT1080 cells (a human fibrosarcoma cell line), and TIG-1 cells (normal human cells) were obtained from Health Science Research Resources Bank and cultured in modified Eagle’s medium (MEM) supplemented with 10% fetal bovine serum (FBS) (Biowest, France). .. Human umbilical vein endothelial cells (HUVEC) were obtained from Kurabo (Osaka, Japan) and were cultured in EBM-2 medium (Cambrex, MD, USA).

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Isolation:

Article Title: Rice bran extract affects differentiation of mesenchymal stem cells potency into osteogenic cells
Article Snippet: .. The isolated bone marrow cells were mixed with α-MEM (Wako, Osaka, Japan), supplemented with 15 % fetal bovine serum (FBS) (Biowest, Nuaillé, France) and 1 % penicillin–streptomycin (Wako), and seeded onto 6-cm tissue culture dishes (Sumitomo Bakelite, Tokyo, Japan). ..

Cell Culture:

Article Title: Catalyser-21TM, a mineral water derived from leaf soil, inhibits tumor cell invasion and angiogenesis
Article Snippet: .. HeLa cells (a human cervical cancer cell line), HT1080 cells (a human fibrosarcoma cell line), and TIG-1 cells (normal human cells) were obtained from Health Science Research Resources Bank and cultured in modified Eagle’s medium (MEM) supplemented with 10% fetal bovine serum (FBS) (Biowest, France). .. Human umbilical vein endothelial cells (HUVEC) were obtained from Kurabo (Osaka, Japan) and were cultured in EBM-2 medium (Cambrex, MD, USA).

Article Title: Alpha-tocopherol attenuates the anti-tumor activity of crizotinib against cells transformed by NPM-ALK
Article Snippet: .. These cells were cultured in RPMI-1640 medium (Nacalai Tesque, Tokyo, Japan) supplemented with 10% fetal bovine serum (FBS) (BioWest, Nuaillé, France), 100 units/ml penicillin (Nacalai Tesque), 100 μg/ml streptomycin (Nacalai Tesque), 2 ng/mL IL-3 (PEPROTECH), and 5 μg/mL puromycin (InVivoGen). .. SUDHL-1 and Ki-JK cells, derived from NPM-ALK-positive ALCL patients, were cultured in RPMI 1640 medium supplemented with 10% FBS (BioWest), 100 units/ml penicillin (Nacalai Tesque), and 100 μg/ml streptomycin (Nacalai Tesque) with or without IL-3 (2 ng/mL) at 37°C and 5% CO2 .

Article Title: Tetraspanin CD82 interaction with cholesterol promotes extracellular vesicle–mediated release of ezrin to inhibit tumour cell movement
Article Snippet: .. Du145 and PC3 human metastatic prostate cancer cell lines, LnCap human prostate cancer cell line and HT1080 human fibroblastoma cell line were obtained from ATCC (VA) and cultured in Dulbecco’s Modified Eagle Medium (DMEM) (Corning) supplemented with 10% foetal bovine serum (FBS) (Biowest, TX), penicillin and streptomycin. .. Exosome-depleted FBS (Exo-FBS) was obtained from System Biosciences (CA) and used for cell culture subject to exosome isolation.

Article Title: Interactions of human microglia cells with Japanese encephalitis virus
Article Snippet: .. Baby Hamster Kidney-21 cells (BHK-21) ([C-13], ATCC, Wesel, Germany) were cultured in Glasgow’s Minimum Essential Medium (GMEM) (Life Technologies, Zug, Switzerland) supplemented with 5% v/v Fetal Bovine Serum (FBS) (Biowest, Nuaillé, France) and Tryptose Phosphate Broth solution (Sigma-Aldrich, Saint Louis, MO) at 37 °C and 5% CO2 . .. Viruses: source, propagation and titration JEV vaccine, manufactured by Intercell AG (Vienna, Austria) and commercialized under the name Ixiaro® by Novartis (Basel, Switzerland), was obtained from the Inselspital Pharmacy (Bern, Switzerland).

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    Biowest SAS fbs
    (A,B) Time of addition assay for analysis of mechanism of CAM and SCM against influenza A/shanghai/37T (2009H1N1) infection. MDCK cells cultured in <t>DMEM</t> supplemented with 10% <t>FBS</t> (Biowest, France), penicillin (100 U/ml), and streptomycin (10 μg/ml) at 37°C/5% CO 2 were infected with influenza A/shanghai/37T (2009H1N1) at 0.1 MOI in DMEM containing 2 μg/mL TPCK-Trypsin. CAM and SCM diluted in DMEM to give a final concentration of 20 μM were added to mixture of virus and cells at 0, 0.5, 1, 2, 4, and 12 h post infection. Inhibition activity of CAM and SCM was measured by CPE reduction assay using CCK-8, according to the manufacturer’s instruction. The data were presented as means ± SE of triplicate assays and the experiment was repeated at least twice.
    Fbs, supplied by Biowest SAS, used in various techniques. Bioz Stars score: 92/100, based on 41 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/fbs/product/Biowest SAS
    Average 92 stars, based on 41 article reviews
    Price from $9.99 to $1999.99
    fbs - by Bioz Stars, 2020-07
    92/100 stars
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    Biowest SAS dextran charcoal treated fbs
    Release of NO from JS-K . (A) Generation of NO from JS-K in <t>RPMI-1640</t> medium containing 10% fetal bovine serum was determined indirectly by photorimetric detection of nitrite according to Green et al. [ 31 ]. (B) Detection of nitrotyrosine by fluorescence microscopy in 22Rv1 cells: Generation of intracellular NO was detected indirectly by detection of nitrotyrosine (green). Cell nuclei were stained with DAPI. [A] untreated cells, [B] 2 μM JS-K neg , [C] 2 μM JS-K, [D] 200 μM DETA/NO.
    Dextran Charcoal Treated Fbs, supplied by Biowest SAS, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dextran charcoal treated fbs/product/Biowest SAS
    Average 88 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    dextran charcoal treated fbs - by Bioz Stars, 2020-07
    88/100 stars
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    (A,B) Time of addition assay for analysis of mechanism of CAM and SCM against influenza A/shanghai/37T (2009H1N1) infection. MDCK cells cultured in DMEM supplemented with 10% FBS (Biowest, France), penicillin (100 U/ml), and streptomycin (10 μg/ml) at 37°C/5% CO 2 were infected with influenza A/shanghai/37T (2009H1N1) at 0.1 MOI in DMEM containing 2 μg/mL TPCK-Trypsin. CAM and SCM diluted in DMEM to give a final concentration of 20 μM were added to mixture of virus and cells at 0, 0.5, 1, 2, 4, and 12 h post infection. Inhibition activity of CAM and SCM was measured by CPE reduction assay using CCK-8, according to the manufacturer’s instruction. The data were presented as means ± SE of triplicate assays and the experiment was repeated at least twice.

    Journal: Frontiers in Microbiology

    Article Title: The Antihistamine Drugs Carbinoxamine Maleate and Chlorpheniramine Maleate Exhibit Potent Antiviral Activity Against a Broad Spectrum of Influenza Viruses

    doi: 10.3389/fmicb.2018.02643

    Figure Lengend Snippet: (A,B) Time of addition assay for analysis of mechanism of CAM and SCM against influenza A/shanghai/37T (2009H1N1) infection. MDCK cells cultured in DMEM supplemented with 10% FBS (Biowest, France), penicillin (100 U/ml), and streptomycin (10 μg/ml) at 37°C/5% CO 2 were infected with influenza A/shanghai/37T (2009H1N1) at 0.1 MOI in DMEM containing 2 μg/mL TPCK-Trypsin. CAM and SCM diluted in DMEM to give a final concentration of 20 μM were added to mixture of virus and cells at 0, 0.5, 1, 2, 4, and 12 h post infection. Inhibition activity of CAM and SCM was measured by CPE reduction assay using CCK-8, according to the manufacturer’s instruction. The data were presented as means ± SE of triplicate assays and the experiment was repeated at least twice.

    Article Snippet: Cells were cultured in DMEM (Thermo Fisher Scientific, Waltham, MA, United States) containing 10% FBS (Biowest, France), penicillin 100 U/ml, and streptomycin 10 μg/ml.

    Techniques: Chick Chorioallantoic Membrane Assay, Infection, Cell Culture, Concentration Assay, Inhibition, Activity Assay, CCK-8 Assay

    Crizotinib-induced apoptosis in Ba/F3 cells transformed by NPM-ALK. Ba/F3 cells were infected with an empty virus (-) and retrovirus expressing NPM-ALK or TEL-JAK2. (A) Whole cell lysates were immunoblotted with an anti-ALK antibody, anti-Flag antibody, anti-JAK2 antibody, anti-phospho-STAT3 antibody, anti-STAT3 antibody, anti-phospho-STAT5 antibody, anti-STAT5 antibody or anti-β-actin antibody. (B) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the absence of IL-3 for 2 days. Viable cell numbers at 24 hr and 48 hr were counted by the Trypan blue exclusion method. Values are the mean ± SD of three independent experiments. (C-F) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the presence of crizotinib (0.25, 0.5, 1 μM) and MMC (0.1, 1, 10 μg/mL) for 24 hr. (C) Cell viability was measured by the WST assay. Values are the mean ± S.D. of four independent experiments. (D) Cells were fixed, treated with propidium iodide, and subjected to a flow cytometric analysis. The percentages of cells in the sub-G1 phase were graphed. Values are the mean ± S.D. of four independent experiments. (E) To evaluate the apoptotic cell death, the chromatin DNA was isolated from cells and subjected to agarose gel electrophoresis. (F) Whole cell lysates were prepared and the phosphorylation of STAT3 and STAT5 was analyzed by immunoblotting. The relative phosphorylation level of STAT3 and STAT5 is shown in the graphs. Values are given as the mean ± SD of three independent experiments. *** P

    Journal: PLoS ONE

    Article Title: Alpha-tocopherol attenuates the anti-tumor activity of crizotinib against cells transformed by NPM-ALK

    doi: 10.1371/journal.pone.0183003

    Figure Lengend Snippet: Crizotinib-induced apoptosis in Ba/F3 cells transformed by NPM-ALK. Ba/F3 cells were infected with an empty virus (-) and retrovirus expressing NPM-ALK or TEL-JAK2. (A) Whole cell lysates were immunoblotted with an anti-ALK antibody, anti-Flag antibody, anti-JAK2 antibody, anti-phospho-STAT3 antibody, anti-STAT3 antibody, anti-phospho-STAT5 antibody, anti-STAT5 antibody or anti-β-actin antibody. (B) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the absence of IL-3 for 2 days. Viable cell numbers at 24 hr and 48 hr were counted by the Trypan blue exclusion method. Values are the mean ± SD of three independent experiments. (C-F) Transduced Ba/F3 cells were incubated with RPMI containing 10% FBS in the presence of crizotinib (0.25, 0.5, 1 μM) and MMC (0.1, 1, 10 μg/mL) for 24 hr. (C) Cell viability was measured by the WST assay. Values are the mean ± S.D. of four independent experiments. (D) Cells were fixed, treated with propidium iodide, and subjected to a flow cytometric analysis. The percentages of cells in the sub-G1 phase were graphed. Values are the mean ± S.D. of four independent experiments. (E) To evaluate the apoptotic cell death, the chromatin DNA was isolated from cells and subjected to agarose gel electrophoresis. (F) Whole cell lysates were prepared and the phosphorylation of STAT3 and STAT5 was analyzed by immunoblotting. The relative phosphorylation level of STAT3 and STAT5 is shown in the graphs. Values are given as the mean ± SD of three independent experiments. *** P

    Article Snippet: These cells were cultured in RPMI-1640 medium (Nacalai Tesque, Tokyo, Japan) supplemented with 10% fetal bovine serum (FBS) (BioWest, Nuaillé, France), 100 units/ml penicillin (Nacalai Tesque), 100 μg/ml streptomycin (Nacalai Tesque), 2 ng/mL IL-3 (PEPROTECH), and 5 μg/mL puromycin (InVivoGen).

    Techniques: Transformation Assay, Infection, Expressing, Incubation, WST Assay, Flow Cytometry, Isolation, Agarose Gel Electrophoresis

    Cell morphology and gene and protein expression of Col2a1, Col1a1, Sox9, and MMP13 in chondrocytes stimulated with RS. A. Rat chondrocytes were cultured with DMEM plus 5% RS (5R) or DMEM plus 10% FBS (10F) for 24 h, and cell cultures were analyzed by microscopy. The chondrocytes dedifferentiated into fibroblastic chondrocytes after normal medium (DMEM plus 10% FBS, 10F) was replaced with DMEM containing 5% RS (5R). B. Col2a1, Col1a1 and MMP13 protein levels were analyzed by western blot. Col1a1 and MMP13 protein expression increased and Col2a1 protein expression decreased in the 5R group when compared to the 10F group. C. In situ expression of Col2a1, Col1a1, and Sox9 were detected in chondrocytes cultured with 5% RS or 10% FBS. The blue color indicates DAPI staining of nuclei. Red indicates Col2a1 expression and green indicates Col1a1 or Sox9 expression. Col1a1 and Sox9 expression increased and Col2a1 expression decreased in the 5R group when compared to the 10F group. D. Chondrocytes were cultured with RS or FBS for 24 h, mRNA was isolated from the chondrocytes, and expression of matrix degradation enzymes and collagen synthesis genes were analyzed by qRT-PCR. Data are expressed as the mean ± SD from three separate experiments. * P

    Journal: American Journal of Translational Research

    Article Title: The MEK-ERK1/2 signaling pathway regulates hyaline cartilage formation and the redifferentiation of dedifferentiated chondrocytes in vitro

    doi:

    Figure Lengend Snippet: Cell morphology and gene and protein expression of Col2a1, Col1a1, Sox9, and MMP13 in chondrocytes stimulated with RS. A. Rat chondrocytes were cultured with DMEM plus 5% RS (5R) or DMEM plus 10% FBS (10F) for 24 h, and cell cultures were analyzed by microscopy. The chondrocytes dedifferentiated into fibroblastic chondrocytes after normal medium (DMEM plus 10% FBS, 10F) was replaced with DMEM containing 5% RS (5R). B. Col2a1, Col1a1 and MMP13 protein levels were analyzed by western blot. Col1a1 and MMP13 protein expression increased and Col2a1 protein expression decreased in the 5R group when compared to the 10F group. C. In situ expression of Col2a1, Col1a1, and Sox9 were detected in chondrocytes cultured with 5% RS or 10% FBS. The blue color indicates DAPI staining of nuclei. Red indicates Col2a1 expression and green indicates Col1a1 or Sox9 expression. Col1a1 and Sox9 expression increased and Col2a1 expression decreased in the 5R group when compared to the 10F group. D. Chondrocytes were cultured with RS or FBS for 24 h, mRNA was isolated from the chondrocytes, and expression of matrix degradation enzymes and collagen synthesis genes were analyzed by qRT-PCR. Data are expressed as the mean ± SD from three separate experiments. * P

    Article Snippet: Chondrocytes were isolated from the articular cartilage of 24-hour-old Sprague-Dawley (SD) rats and dispersed in 0.1% collagenase type II (C6885, Sigma-Aldrich, Switzerland) for 3 h. Chondrocytes were collected and cultured in Dulbecco’s Modified Eagle’s Medium (DMEM, Biowest, France) supplemented with 10% FBS (Biowest, France) and 1% penicillin-streptomycin.

    Techniques: Expressing, Cell Culture, Microscopy, Western Blot, In Situ, Staining, Isolation, Quantitative RT-PCR

    Analysis of GAG content and gene expression in chondrocytes cultured with the MEK inhibitor PD0325901. A. Chondrocytes were cultured in DMEM supplemented with 5% RS (5R), 10% FBS (10F), or 5% RS plus various PD0325901 concentrations for 24 h. Chondrocytes were stained with Safranin O (left), and the GAG content in the chondrocytes was measured using the DMB method (right). B. Gene expression of matrix degradation enzymes and collagen synthesis genes in chondrocytes was evaluated by qPCR after treatment with and without various concentrations of the MEK-ERK1/2 pathway inhibitor PD0325901. Data are expressed as the mean ± SD from three separate experiments. # P

    Journal: American Journal of Translational Research

    Article Title: The MEK-ERK1/2 signaling pathway regulates hyaline cartilage formation and the redifferentiation of dedifferentiated chondrocytes in vitro

    doi:

    Figure Lengend Snippet: Analysis of GAG content and gene expression in chondrocytes cultured with the MEK inhibitor PD0325901. A. Chondrocytes were cultured in DMEM supplemented with 5% RS (5R), 10% FBS (10F), or 5% RS plus various PD0325901 concentrations for 24 h. Chondrocytes were stained with Safranin O (left), and the GAG content in the chondrocytes was measured using the DMB method (right). B. Gene expression of matrix degradation enzymes and collagen synthesis genes in chondrocytes was evaluated by qPCR after treatment with and without various concentrations of the MEK-ERK1/2 pathway inhibitor PD0325901. Data are expressed as the mean ± SD from three separate experiments. # P

    Article Snippet: Chondrocytes were isolated from the articular cartilage of 24-hour-old Sprague-Dawley (SD) rats and dispersed in 0.1% collagenase type II (C6885, Sigma-Aldrich, Switzerland) for 3 h. Chondrocytes were collected and cultured in Dulbecco’s Modified Eagle’s Medium (DMEM, Biowest, France) supplemented with 10% FBS (Biowest, France) and 1% penicillin-streptomycin.

    Techniques: Expressing, Cell Culture, Staining, Real-time Polymerase Chain Reaction

    Release of NO from JS-K . (A) Generation of NO from JS-K in RPMI-1640 medium containing 10% fetal bovine serum was determined indirectly by photorimetric detection of nitrite according to Green et al. [ 31 ]. (B) Detection of nitrotyrosine by fluorescence microscopy in 22Rv1 cells: Generation of intracellular NO was detected indirectly by detection of nitrotyrosine (green). Cell nuclei were stained with DAPI. [A] untreated cells, [B] 2 μM JS-K neg , [C] 2 μM JS-K, [D] 200 μM DETA/NO.

    Journal: BMC Cancer

    Article Title: JS-K, a glutathione/glutathione S-transferase-activated nitric oxide releasing prodrug inhibits androgen receptor and WNT-signaling in prostate cancer cells

    doi: 10.1186/1471-2407-12-130

    Figure Lengend Snippet: Release of NO from JS-K . (A) Generation of NO from JS-K in RPMI-1640 medium containing 10% fetal bovine serum was determined indirectly by photorimetric detection of nitrite according to Green et al. [ 31 ]. (B) Detection of nitrotyrosine by fluorescence microscopy in 22Rv1 cells: Generation of intracellular NO was detected indirectly by detection of nitrotyrosine (green). Cell nuclei were stained with DAPI. [A] untreated cells, [B] 2 μM JS-K neg , [C] 2 μM JS-K, [D] 200 μM DETA/NO.

    Article Snippet: After transfection cells were grown in RPMI 1640 with 5% dextran charcoal treated steroid free, dextran charcoal treated FBS (FBSdcc; Biowest, Nuaillé, France) and treated with 5 nM DHT and different concentrations of JS-K. (2) WNT-signalling : Luciferase reporter plasmids pTopFlash (250 ng/well) and pFopFlash (250 ng/well) were mixed either with pbCAT expression vector (250 ng/well) or insert-free vector (250 ng/well). pRL-tk-luc (80 ng/well) was co-transfected to correct for transfection efficiency.

    Techniques: Fluorescence, Microscopy, Staining