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  • 99
    Lonza glutamine
    Glutamine, supplied by Lonza, used in various techniques. Bioz Stars score: 99/100, based on 1059 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti mouse igg h l cross adsorbed secondary antibody
    In vivo expression of non-tenocyte markers PPARγ, collagen type II, and osteocalcin in rats implanted with hTSCs treated with various concentrations of PGE 2 and their respective hematoxylin and eosin (H E) stained tissue sections. hTSCs cultured with three concentrations (0.1, 10, and 100 ng/ml) of PGE 2 were implanted subcutaneously into rats; later, immunohistochemical and histological analyses were performed on tissue sections. For the immunohistochemical staining, fixed tissue sections were incubated with mouse anti-human PPARγ antibody, mouse anti-collagen type II (Collagen II) antibody, or mouse anti-human osteocalcin antibody. Cy3-conjugated goat anti-mouse <t>IgG</t> was then used to detect primary binding. Nuclei were stained with Hoechst (blue). Expression levels of PPARγ, collagen type II, and osteocalcin (red) were lower in cells treated with 0.1 ng/ml PGE 2 ( A–C ) than those treated with the higher concentrations (10 and 100 ng/ml) of PGE 2 ( E–G, I–K ). H E staining was also performed on tissue sections ( D, H, L ). More cells (black dots; see insets in D , H , and L ) were observed in tissues implanted with hTSCs that had been treated with high concentrations of PGE 2 in culture ( H, L ). Specifically, at 100 ng/ml ( L ), cells were concentrated in a specific region (triangle). Additionally, semi-quantification of the stained cells was performed by counting immuno-positive cells and calculating percentage staining ( M ) (*p
    Goat Anti Mouse Igg H L Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 14005 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    thermo fisher l glutamine
    In vivo expression of non-tenocyte markers PPARγ, collagen type II, and osteocalcin in rats implanted with hTSCs treated with various concentrations of PGE 2 and their respective hematoxylin and eosin (H E) stained tissue sections. hTSCs cultured with three concentrations (0.1, 10, and 100 ng/ml) of PGE 2 were implanted subcutaneously into rats; later, immunohistochemical and histological analyses were performed on tissue sections. For the immunohistochemical staining, fixed tissue sections were incubated with mouse anti-human PPARγ antibody, mouse anti-collagen type II (Collagen II) antibody, or mouse anti-human osteocalcin antibody. Cy3-conjugated goat anti-mouse <t>IgG</t> was then used to detect primary binding. Nuclei were stained with Hoechst (blue). Expression levels of PPARγ, collagen type II, and osteocalcin (red) were lower in cells treated with 0.1 ng/ml PGE 2 ( A–C ) than those treated with the higher concentrations (10 and 100 ng/ml) of PGE 2 ( E–G, I–K ). H E staining was also performed on tissue sections ( D, H, L ). More cells (black dots; see insets in D , H , and L ) were observed in tissues implanted with hTSCs that had been treated with high concentrations of PGE 2 in culture ( H, L ). Specifically, at 100 ng/ml ( L ), cells were concentrated in a specific region (triangle). Additionally, semi-quantification of the stained cells was performed by counting immuno-positive cells and calculating percentage staining ( M ) (*p
    L Glutamine, supplied by thermo fisher, used in various techniques. Bioz Stars score: 99/100, based on 146399 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore l glutamine
    Incorporation of labelled precursor metabolites into purine and pyrimidine synthesis is strongly reduced during infection. Control cells and infected cells were cultured with either ( A )  l -glutamine-amide- 15 N or ( B )  d -glucose- 13 C 6  for 12 h. Mean percentages of incorporation levels of labelled precursors are presented ( n  = 3). Proportions of complete labelled nucleotides and nucleotide-sugars are black, labelled sugar moieties are presented as grey pattern and unlabelled metabolite amounts are displayed as light grey.
    L Glutamine, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 52942 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore poly l lysine
    IL-1-induced MMP3 expression depends on the ERK-mediated pathway. A , human gingival fibroblasts were plated on <t>fibronectin</t> ( FN ) or poly- l -lysine ( PL ) and treated with vehicle or IL-1 (40 ng/ml) overnight. Cell lysates were immunoblotted ( WB ) for MEK or
    Poly L Lysine, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 27394 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore dtt
    Shown are 600 MHz 1 H- 15 N HSQC spectra of Parkin IBR 307–384 . ( a ) Folded 0.2 mM IBR 307–384 in 25 mM phosphate buffer (pH 6.95), 100 mM <t>NaCl,</t> 1 mM <t>DTT</t> at 25°C. ( b ) Spectrum of IBR 307–384 from a upon EDTA addition showing the
    Dtt, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 38144 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    GE Healthcare rpmi 1640 medium
    (A) LDH release from MCF-7 cells subjected to 2 μmol/L fluopsin C treatment. MCF-7 cells were treated with 1% Triton-X-100 (Sigma) in <t>RPMI-1640</t> medium for 10 min as the 100% LDH release control. b P
    Rpmi 1640 Medium, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 12494 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher goat anti rabbit igg h l cross adsorbed secondary antibody
    (A) LDH release from MCF-7 cells subjected to 2 μmol/L fluopsin C treatment. MCF-7 cells were treated with 1% Triton-X-100 (Sigma) in <t>RPMI-1640</t> medium for 10 min as the 100% LDH release control. b P
    Goat Anti Rabbit Igg H L Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 14891 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare rpmi 1640
    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete <t>RPMI</t> 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.
    Rpmi 1640, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 9823 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher donkey anti rabbit igg h l highly cross adsorbed secondary antibody
    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete <t>RPMI</t> 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.
    Donkey Anti Rabbit Igg H L Highly Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 9653 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher goat anti mouse igg h l highly cross adsorbed secondary antibody
    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete <t>RPMI</t> 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.
    Goat Anti Mouse Igg H L Highly Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 9004 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare l glutamine
    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete <t>RPMI</t> 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.
    L Glutamine, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 99/100, based on 7060 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore l ascorbic acid
    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete <t>RPMI</t> 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.
    L Ascorbic Acid, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 4898 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore l cysteine
    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete <t>RPMI</t> 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.
    L Cysteine, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3331 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher donkey anti mouse igg h l highly cross adsorbed secondary antibody
    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete <t>RPMI</t> 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.
    Donkey Anti Mouse Igg H L Highly Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 6700 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore non essential amino acids
    Effect of the necrotic condition or nutritional deficiency on the mRNA expression of FADS1 ( a , b ), FADS2 ( c , d ), and FADS3 ( e , f ). Human brain (glioblastoma astrocytoma) U-87 MG cell line cultured in EMEM medium with 10% FBS, 2 mM l -glutamine, 1 mM sodium pyruvate, 1% <t>non-essential</t> <t>amino</t> <t>acids,</t> 100 U/mL penicillin, and 100 µg/mL streptomycin. U-87 MG cells were seeded in 6-well plates. After 72 h incubation, cells were washed three times with PBS solution. Next, cells were cultured for 24 h under three different conditions (control, nutrient deficiency, and necrotic). Control cells were suspended in full medium, while starved cells were grown in medium with low concentration of l -glutamine (0.2 mM) and without sodium pyruvate. For the induction of necrotic conditions, cells were incubated in medium supplemented with 200 µM H 2 O 2 . After 24 h of incubation, the cells were trypsinized and analyzed using qRT-PCR. **—statistically significant difference in the expression of a given desaturase between the tumor area according to the Wilcoxon signed-rank test ( p
    Non Essential Amino Acids, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 5847 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher m l glutamine
    Effect of the necrotic condition or nutritional deficiency on the mRNA expression of FADS1 ( a , b ), FADS2 ( c , d ), and FADS3 ( e , f ). Human brain (glioblastoma astrocytoma) U-87 MG cell line cultured in EMEM medium with 10% FBS, 2 mM l -glutamine, 1 mM sodium pyruvate, 1% <t>non-essential</t> <t>amino</t> <t>acids,</t> 100 U/mL penicillin, and 100 µg/mL streptomycin. U-87 MG cells were seeded in 6-well plates. After 72 h incubation, cells were washed three times with PBS solution. Next, cells were cultured for 24 h under three different conditions (control, nutrient deficiency, and necrotic). Control cells were suspended in full medium, while starved cells were grown in medium with low concentration of l -glutamine (0.2 mM) and without sodium pyruvate. For the induction of necrotic conditions, cells were incubated in medium supplemented with 200 µM H 2 O 2 . After 24 h of incubation, the cells were trypsinized and analyzed using qRT-PCR. **—statistically significant difference in the expression of a given desaturase between the tumor area according to the Wilcoxon signed-rank test ( p
    M L Glutamine, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 4264 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Abcam goat anti rabbit igg h l hrp
    F-ATPase/VGCC protein complex verification. a. 1D immunoblot analysis of the VGCC α2δ-1 subunit in neutrophils. The VGCC α2δ-1 subunit-containing protein complexes in a NativePAGE Novex 4–16% Bis-Tris gel were detected at approximately 750 kDa via immunoblotting, the same position as the F-ATPase F1 β-subunit. b. 2D immunoblot analysis of the F-ATPase and VGCC protein complex. Plasma membrane lysed by 2% digitonin was loaded and run on a BN-PAGE gel. One lane (Sample) was cut and equilibrated in SDS loading buffer, followed by fixation on a SDS-PAGE gel for 2D electrophoretic analysis. Two separate immunoblot analyses with a primary antibody against the VGCC α2δ-1 subunit or the F-ATPase F1 β-subunit were performed. The F-ATPase F1 β-subunit appears vertically below the VGCC α2δ-1 subunit in the same PVDF membrane. c. Immunofluorescence colocalization analysis of F-ATPase and VGCC. Representative images show that the VGCC α2δ-1 subunit and F-ATPase F1 β-subunit colocalized on the plasma membrane of neutrophils. d. Immunoprecipitation of VGCC α2δ-1 subunit and F-ATPase from plasma membrane protein in human neutrophils. Samples were immunoprecipitated with a mouse monoclonal antibody against α2 of the VGCC α2δ-1 subunit. F-ATPase was detected with a mouse monoclonal antibody against the F-ATPase F1 α-subunit or β-subunit and an <t>HRP-conjugated</t> goat anti-mouse <t>IgG</t> light chain specifically bound antibody. IgG control experiment did not detect F-ATPase
    Goat Anti Rabbit Igg H L Hrp, supplied by Abcam, used in various techniques. Bioz Stars score: 99/100, based on 2991 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore poly l ornithine
    BrainPhys increases neuronal morphology and Aβ secretion in SH-SY5Y cells. SH-SY5Y neuroblastoma cells pre-differentiated with RA for five-seven days and thereafter seeded onto <t>poly-l-ornithine-</t> and <t>laminin-coated</t> plates and cultured either in standard medium (DMEM/F12) or BrainPhys for 7–14 days. ( A ) Phase contrast images of SH-SY5Y cells cultured in standard DMEM/F12 medium (left panel) and cells cultured in BrainPhys media for 7 days (middle panel) or 14 days (right panel) are shown. Increased neuronal morphology with longer and highly branched neurites is observed in BrainPhys-cultured SH-SY5Y cells already after 7 days (middle panel) and increase further with another 7 days (right panel) of BrainPhys culturing. Representative images from one out of three experiments are shown. Scale bar = 100 μM. ( B ) Concentrations of secreted Aβ peptides measured from cell-conditioned media of SH-SY5Y cells cultured in either DMEM/F12 supplemented with retinoic acid for 7 days or in BrainPhys media for 14 days. BrainPhys significantly increases the secretion of both (I) Aβ40 and (II) Aβ42 as compared to the standard medium (Aβ38 is below the lower limit of detection of the assay). Mean values of three separate experiments were analysed with Student’s t-test. **p ≤ 0.01. Bars represent mean +/− SEM. ( C ) The cell numbers from phase contrast images from three separate experiments were analysed with Student’s t-test. No significant differences in cell numbers were observed between NMM- and BrainPhys-cultured neurons. Bars represent mean +/− SEM presented as relative to NMM.
    Poly L Ornithine, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 3744 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher leibovitz s l 15 medium
    Flow cytometry analysis of mesenchymal stem cell markers CD105 and CD90 in MDA-MB-231 cells. A. Results from flow cytometry analysis, with series of gates set for CD105+ or CD90+ identification. R2, R3, R4 and R5 represented cell subpopulations identified as CD105 + /CD90 +  (0.99%), CD105+/CD90- cell subpopulation (4.93%), CD105 - /CD90 -  cell subpopulation (90.77%) and CD105-/CD90+ cell subpopulation (3.31%) respectively. Morphology of cultured MDA-MB-231 cells in Leibovitz’s L-15 media by phase-contrast microscopy (×100) was shown in B, while sorted CD105 + /CD90 +  and CD105 - /CD90 -  subpopulations after 72 hours incubation (×200) shown in C.
    Leibovitz S L 15 Medium, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3482 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Mediatech l glutamine
    Flow cytometry analysis of mesenchymal stem cell markers CD105 and CD90 in MDA-MB-231 cells. A. Results from flow cytometry analysis, with series of gates set for CD105+ or CD90+ identification. R2, R3, R4 and R5 represented cell subpopulations identified as CD105 + /CD90 +  (0.99%), CD105+/CD90- cell subpopulation (4.93%), CD105 - /CD90 -  cell subpopulation (90.77%) and CD105-/CD90+ cell subpopulation (3.31%) respectively. Morphology of cultured MDA-MB-231 cells in Leibovitz’s L-15 media by phase-contrast microscopy (×100) was shown in B, while sorted CD105 + /CD90 +  and CD105 - /CD90 -  subpopulations after 72 hours incubation (×200) shown in C.
    L Glutamine, supplied by Mediatech, used in various techniques. Bioz Stars score: 92/100, based on 6178 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore n acetylcysteine
    Characterization of serine-glycine one-carbon pathway in KL cells a, Detailed graph of SGOC network. Enzymatic inhibitors used in this study are marked in red. b, Reactive oxygen species in K or KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2 were measured by DCFDA (left) and CellRox staining (right). Data are normalized to cell number (n=4). c, Six-day proliferation assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing lack of growth rescue by <t>N-acetylcysteine</t> (NAC). Data are expressed as relative to day 0 (n=6). d, Three-day growth assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing the lack of rescue by excess nucleosides (adenosine, guanosine, thymidine, uridine, cytidine, 1 mM each). Data are presented as percentage of the growth of shControl cells (n=16). e, Proliferation of K or KL cells treated with aminooxyacetate (AOA). Data are expressed as relative to day 0 (n=8). f, Five-day proliferation of K or KL cells treated with AOA and/or NAC. Data are expressed as relative to day 0 (n=6). g, Data from RNA-seq ( left panel ) and quantitative proteomics ( right panel ) showing levels of genes involved in the production of SAM in K and KL. The data plotted are expressed as mean-centered values. h, Proliferation of K or KL cells treated with 2 mM cycloleucine. Data are expressed as percentage of the growth of vehicle treated cells (n=12). Shown are data pooled from two (b–f, h) experiments. For all panels, error bars are standard deviation unless otherwise stated and statistical significance is indicated as follows: *P
    N Acetylcysteine, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2976 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher donkey anti goat igg h l cross adsorbed secondary antibody
    Characterization of serine-glycine one-carbon pathway in KL cells a, Detailed graph of SGOC network. Enzymatic inhibitors used in this study are marked in red. b, Reactive oxygen species in K or KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2 were measured by DCFDA (left) and CellRox staining (right). Data are normalized to cell number (n=4). c, Six-day proliferation assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing lack of growth rescue by <t>N-acetylcysteine</t> (NAC). Data are expressed as relative to day 0 (n=6). d, Three-day growth assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing the lack of rescue by excess nucleosides (adenosine, guanosine, thymidine, uridine, cytidine, 1 mM each). Data are presented as percentage of the growth of shControl cells (n=16). e, Proliferation of K or KL cells treated with aminooxyacetate (AOA). Data are expressed as relative to day 0 (n=8). f, Five-day proliferation of K or KL cells treated with AOA and/or NAC. Data are expressed as relative to day 0 (n=6). g, Data from RNA-seq ( left panel ) and quantitative proteomics ( right panel ) showing levels of genes involved in the production of SAM in K and KL. The data plotted are expressed as mean-centered values. h, Proliferation of K or KL cells treated with 2 mM cycloleucine. Data are expressed as percentage of the growth of vehicle treated cells (n=12). Shown are data pooled from two (b–f, h) experiments. For all panels, error bars are standard deviation unless otherwise stated and statistical significance is indicated as follows: *P
    Donkey Anti Goat Igg H L Cross Adsorbed Secondary Antibody, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 4241 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    In vivo expression of non-tenocyte markers PPARγ, collagen type II, and osteocalcin in rats implanted with hTSCs treated with various concentrations of PGE 2 and their respective hematoxylin and eosin (H E) stained tissue sections. hTSCs cultured with three concentrations (0.1, 10, and 100 ng/ml) of PGE 2 were implanted subcutaneously into rats; later, immunohistochemical and histological analyses were performed on tissue sections. For the immunohistochemical staining, fixed tissue sections were incubated with mouse anti-human PPARγ antibody, mouse anti-collagen type II (Collagen II) antibody, or mouse anti-human osteocalcin antibody. Cy3-conjugated goat anti-mouse IgG was then used to detect primary binding. Nuclei were stained with Hoechst (blue). Expression levels of PPARγ, collagen type II, and osteocalcin (red) were lower in cells treated with 0.1 ng/ml PGE 2 ( A–C ) than those treated with the higher concentrations (10 and 100 ng/ml) of PGE 2 ( E–G, I–K ). H E staining was also performed on tissue sections ( D, H, L ). More cells (black dots; see insets in D , H , and L ) were observed in tissues implanted with hTSCs that had been treated with high concentrations of PGE 2 in culture ( H, L ). Specifically, at 100 ng/ml ( L ), cells were concentrated in a specific region (triangle). Additionally, semi-quantification of the stained cells was performed by counting immuno-positive cells and calculating percentage staining ( M ) (*p

    Journal: PLoS ONE

    Article Title: Prostaglandin E2 (PGE2) Exerts Biphasic Effects on Human Tendon Stem Cells

    doi: 10.1371/journal.pone.0087706

    Figure Lengend Snippet: In vivo expression of non-tenocyte markers PPARγ, collagen type II, and osteocalcin in rats implanted with hTSCs treated with various concentrations of PGE 2 and their respective hematoxylin and eosin (H E) stained tissue sections. hTSCs cultured with three concentrations (0.1, 10, and 100 ng/ml) of PGE 2 were implanted subcutaneously into rats; later, immunohistochemical and histological analyses were performed on tissue sections. For the immunohistochemical staining, fixed tissue sections were incubated with mouse anti-human PPARγ antibody, mouse anti-collagen type II (Collagen II) antibody, or mouse anti-human osteocalcin antibody. Cy3-conjugated goat anti-mouse IgG was then used to detect primary binding. Nuclei were stained with Hoechst (blue). Expression levels of PPARγ, collagen type II, and osteocalcin (red) were lower in cells treated with 0.1 ng/ml PGE 2 ( A–C ) than those treated with the higher concentrations (10 and 100 ng/ml) of PGE 2 ( E–G, I–K ). H E staining was also performed on tissue sections ( D, H, L ). More cells (black dots; see insets in D , H , and L ) were observed in tissues implanted with hTSCs that had been treated with high concentrations of PGE 2 in culture ( H, L ). Specifically, at 100 ng/ml ( L ), cells were concentrated in a specific region (triangle). Additionally, semi-quantification of the stained cells was performed by counting immuno-positive cells and calculating percentage staining ( M ) (*p

    Article Snippet: The cells were then washed three times with PBS, followed by incubation with Cy3-conjugated goat anti-mouse IgG (1∶500; Invitrogen, Cat. # A10521) secondary antibody at room temperature for 2 hrs.

    Techniques: In Vivo, Expressing, Staining, Cell Culture, Immunohistochemistry, Incubation, Binding Assay

    Incorporation of labelled precursor metabolites into purine and pyrimidine synthesis is strongly reduced during infection. Control cells and infected cells were cultured with either ( A )  l -glutamine-amide- 15 N or ( B )  d -glucose- 13 C 6  for 12 h. Mean percentages of incorporation levels of labelled precursors are presented ( n  = 3). Proportions of complete labelled nucleotides and nucleotide-sugars are black, labelled sugar moieties are presented as grey pattern and unlabelled metabolite amounts are displayed as light grey.

    Journal: Metabolites

    Article Title: Staphylococcus aureus Infection Reduces Nutrition Uptake and Nucleotide Biosynthesis in a Human Airway Epithelial Cell Line

    doi: 10.3390/metabo6040041

    Figure Lengend Snippet: Incorporation of labelled precursor metabolites into purine and pyrimidine synthesis is strongly reduced during infection. Control cells and infected cells were cultured with either ( A ) l -glutamine-amide- 15 N or ( B ) d -glucose- 13 C 6 for 12 h. Mean percentages of incorporation levels of labelled precursors are presented ( n = 3). Proportions of complete labelled nucleotides and nucleotide-sugars are black, labelled sugar moieties are presented as grey pattern and unlabelled metabolite amounts are displayed as light grey.

    Article Snippet: Metabolic Inhibitors and Labelled Precursors To inhibit glutamine dependent metabolic reactions, we applied two glutamine analogues namely 6-diazo-5-oxo-l -norleucine (DON) with a final concentration of 0.5 mmol/L and azaserine (both obtained from Sigma Aldrich) with a final concentration of 0.028 mmol/L to the incubation medium for 12 h. In our 15 N labelling approach we used RPMI 1640 R7509 medium as incubation medium as described above but replaced unlabelled glutamine with 2 mmol/L of l -glutamine-(amide-15 N) (obtained from Sigma Aldrich).

    Techniques: Infection, Cell Culture

    IL-1-induced MMP3 expression depends on the ERK-mediated pathway. A , human gingival fibroblasts were plated on fibronectin ( FN ) or poly- l -lysine ( PL ) and treated with vehicle or IL-1 (40 ng/ml) overnight. Cell lysates were immunoblotted ( WB ) for MEK or

    Journal: The Journal of Biological Chemistry

    Article Title: Importance of Protein-tyrosine Phosphatase-? Catalytic Domains for Interactions with SHP-2 and Interleukin-1-induced Matrix Metalloproteinase-3 Expression *

    doi: 10.1074/jbc.M110.102426

    Figure Lengend Snippet: IL-1-induced MMP3 expression depends on the ERK-mediated pathway. A , human gingival fibroblasts were plated on fibronectin ( FN ) or poly- l -lysine ( PL ) and treated with vehicle or IL-1 (40 ng/ml) overnight. Cell lysates were immunoblotted ( WB ) for MEK or

    Article Snippet: Fibronectin, poly- l -lysine, BSA, puromycin, doxycycline, and mouse monoclonal antibodies to vinculin, phosphotyrosine (clone PY-20), and β-actin were from Sigma.

    Techniques: Expressing, Western Blot

    Shown are 600 MHz 1 H- 15 N HSQC spectra of Parkin IBR 307–384 . ( a ) Folded 0.2 mM IBR 307–384 in 25 mM phosphate buffer (pH 6.95), 100 mM NaCl, 1 mM DTT at 25°C. ( b ) Spectrum of IBR 307–384 from a upon EDTA addition showing the

    Journal:

    Article Title: Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease

    doi: 10.1073/pnas.0610548104

    Figure Lengend Snippet: Shown are 600 MHz 1 H- 15 N HSQC spectra of Parkin IBR 307–384 . ( a ) Folded 0.2 mM IBR 307–384 in 25 mM phosphate buffer (pH 6.95), 100 mM NaCl, 1 mM DTT at 25°C. ( b ) Spectrum of IBR 307–384 from a upon EDTA addition showing the

    Article Snippet: Proteins were dialyzed against 25 mM Na2 HPO4 pH 6.95, 100 mM NaCl, and 1 mM DTT and concentrated to 0.2–0.9 mM by ultrafiltration (Millipore, Mississauga, ON, Canada) for NMR experiments.

    Techniques:

    Relationship between RESET and the UPR, Related to Figure 7 (A) Extended data set for Figure 7 A. NRK cells stably expressing the XBP1-mCherry UPR reporter and GFP-PrP ∗ were treated with 0.5 mM dithiothreitol (DTT). Time series were collected over the course of 18 hr starting 5 min after addition of DTT. For each time point, both GFP-PrP ∗ and XBP1-mCh were imaged. Scale bar, 10 μm. (B) Flp-In T-REx HEK293 cells (Invitrogen) expressing wild-type human PrP at the FRT locus were induced with the indicated concentrations of doxycycline for 24 hr. Total cell lysates were analyzed by immunoblotting with the 3F4 monoclonal antibody, using total hamster brain homogenate as a standard. Loading was controlled by β-tubulin immunoblot. Similar levels of expression of PrP were seen with transient transfection and doxycycline induction in the Flp-In T-REx HEK293 cells. (C) Flp-In T-REx HEK293 cells, either untransfected, or stably transfected with the indicated PrP construct, were transfected with an ATF6-luciferase UPR reporter (or control plasmid), then induced with 5 ng/ml doxycycline for 16 hr. Cells were then assessed for luciferase activity. Five individual wells of cells were measured for each condition (gray bars). The mean of the five replicates (±SD) is shown with the black bars, and indicated below the graph. (D) Flp-In T-REx HEK293 cells, which were either untransfected (UT) or stably transfected with the indicated inducible PrP construct (C179A is YFP-PrP ∗ ), were transfected with an ATF6-luciferase reporter. Expression of PrP constructs was induced with 5 ng/ml doxycycline for 16 hr. Triplicate wells were then assessed for luciferase activity (mean ± SD). In parallel, Flp-In T-REx HEK293 cells were transfected with an ATF6-luciferase reporter, treated with the indicated concentrations of dithiothreitol (DTT) for 16 hr, and analyzed in triplicate for luciferase activity (mean ± SD).

    Journal: Cell

    Article Title: ER Stress-Induced Clearance of Misfolded GPI-Anchored Proteins via the Secretory Pathway

    doi: 10.1016/j.cell.2014.06.026

    Figure Lengend Snippet: Relationship between RESET and the UPR, Related to Figure 7 (A) Extended data set for Figure 7 A. NRK cells stably expressing the XBP1-mCherry UPR reporter and GFP-PrP ∗ were treated with 0.5 mM dithiothreitol (DTT). Time series were collected over the course of 18 hr starting 5 min after addition of DTT. For each time point, both GFP-PrP ∗ and XBP1-mCh were imaged. Scale bar, 10 μm. (B) Flp-In T-REx HEK293 cells (Invitrogen) expressing wild-type human PrP at the FRT locus were induced with the indicated concentrations of doxycycline for 24 hr. Total cell lysates were analyzed by immunoblotting with the 3F4 monoclonal antibody, using total hamster brain homogenate as a standard. Loading was controlled by β-tubulin immunoblot. Similar levels of expression of PrP were seen with transient transfection and doxycycline induction in the Flp-In T-REx HEK293 cells. (C) Flp-In T-REx HEK293 cells, either untransfected, or stably transfected with the indicated PrP construct, were transfected with an ATF6-luciferase UPR reporter (or control plasmid), then induced with 5 ng/ml doxycycline for 16 hr. Cells were then assessed for luciferase activity. Five individual wells of cells were measured for each condition (gray bars). The mean of the five replicates (±SD) is shown with the black bars, and indicated below the graph. (D) Flp-In T-REx HEK293 cells, which were either untransfected (UT) or stably transfected with the indicated inducible PrP construct (C179A is YFP-PrP ∗ ), were transfected with an ATF6-luciferase reporter. Expression of PrP constructs was induced with 5 ng/ml doxycycline for 16 hr. Triplicate wells were then assessed for luciferase activity (mean ± SD). In parallel, Flp-In T-REx HEK293 cells were transfected with an ATF6-luciferase reporter, treated with the indicated concentrations of dithiothreitol (DTT) for 16 hr, and analyzed in triplicate for luciferase activity (mean ± SD).

    Article Snippet: Drug Treatments Working concentrations are 0.1 μM thapsigargin, 0.5 mM dithiothreitol, 5 mM methyl-β-cyclodextrin, and 1 μM brefeldin A. Lysosomal protease inhibitors refer to 125 μM leupeptin + protease inhibitor cocktail (Sigma P8340) diluted 1:100.

    Techniques: Stable Transfection, Expressing, Transfection, Construct, Luciferase, Plasmid Preparation, Activity Assay

    ER Stress Induces Rapid Relocalization and Degradation of ER-Retained Misfolded PrP (A) Diagrams of YFP-tagged wild-type PrP (YFP-PrP) and YFP-tagged misfolded PrP (YFP-PrP ∗ ) depicting the GPI-anchor (yellow), two N-linked glycans (blue), the disulfide bond (black), and the YFP-tag (green). YFP-PrP ∗ lacks the intramolecular disulfide bond. (B) Steady-state localization of YFP-PrP (left) and YFP-PrP ∗ (right). CFP-KDEL marks the ER. (C) Time-lapse images of YFP-PrP ∗ -expressing cells after treatment with thapsigargin (TG, top) or with dithiothreitol (DTT, bottom) (D) Steady-state chase experiment performed using YFP-PrP ∗ -expressing cells. The top panel shows an autoradiograph of YFP-PrP ∗ immunoprecipitations from a representative experiment, and the bottom panel shows quantification from multiple experiments (mean ± SE; n = 4). Scale bars, 10 μm. See also Movies S1 and S2 and Figure S1 .

    Journal: Cell

    Article Title: ER Stress-Induced Clearance of Misfolded GPI-Anchored Proteins via the Secretory Pathway

    doi: 10.1016/j.cell.2014.06.026

    Figure Lengend Snippet: ER Stress Induces Rapid Relocalization and Degradation of ER-Retained Misfolded PrP (A) Diagrams of YFP-tagged wild-type PrP (YFP-PrP) and YFP-tagged misfolded PrP (YFP-PrP ∗ ) depicting the GPI-anchor (yellow), two N-linked glycans (blue), the disulfide bond (black), and the YFP-tag (green). YFP-PrP ∗ lacks the intramolecular disulfide bond. (B) Steady-state localization of YFP-PrP (left) and YFP-PrP ∗ (right). CFP-KDEL marks the ER. (C) Time-lapse images of YFP-PrP ∗ -expressing cells after treatment with thapsigargin (TG, top) or with dithiothreitol (DTT, bottom) (D) Steady-state chase experiment performed using YFP-PrP ∗ -expressing cells. The top panel shows an autoradiograph of YFP-PrP ∗ immunoprecipitations from a representative experiment, and the bottom panel shows quantification from multiple experiments (mean ± SE; n = 4). Scale bars, 10 μm. See also Movies S1 and S2 and Figure S1 .

    Article Snippet: Drug Treatments Working concentrations are 0.1 μM thapsigargin, 0.5 mM dithiothreitol, 5 mM methyl-β-cyclodextrin, and 1 μM brefeldin A. Lysosomal protease inhibitors refer to 125 μM leupeptin + protease inhibitor cocktail (Sigma P8340) diluted 1:100.

    Techniques: Expressing, Autoradiography

    (A) LDH release from MCF-7 cells subjected to 2 μmol/L fluopsin C treatment. MCF-7 cells were treated with 1% Triton-X-100 (Sigma) in RPMI-1640 medium for 10 min as the 100% LDH release control. b P

    Journal: Acta Pharmacologica Sinica

    Article Title: Fluopsin C induces oncosis of human breast adenocarcinoma cells

    doi: 10.1038/aps.2013.44

    Figure Lengend Snippet: (A) LDH release from MCF-7 cells subjected to 2 μmol/L fluopsin C treatment. MCF-7 cells were treated with 1% Triton-X-100 (Sigma) in RPMI-1640 medium for 10 min as the 100% LDH release control. b P

    Article Snippet: The MCF-7 and HL7702 cells were maintained in RPMI-1640 medium (Hyclone, Thermo Fisher Scientific, Beijing, China), and the MD-MBA-231 cells were cultured in modified DMEM (Gibco, Invitrogen Corporation, Grand Island, NY, USA).

    Techniques:

    Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete RPMI 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.

    Journal: Frontiers in Immunology

    Article Title: Analysis of the Interaction between Globular Head Modules of Human C1q and Its Candidate Receptor gC1qR

    doi: 10.3389/fimmu.2016.00567

    Figure Lengend Snippet: Interaction of ghA, ghB, and ghC with monocyte/macrophages . PMBCs (1 × 10 6 ) were seeded on 13 mm coverslips and incubated in complete RPMI 1640 medium for 2 weeks at 37°C in 5% CO 2 incubator. Cells were treated with 10 μg of each globular head module and incubated with serum-free RPMI 1640 medium for 1 h at 37°C. After washing with PBS, cells were fixed with 4% PFA, permeabilzed with Triton X-100, and probed with anti-gC1qR polyclonal antibody and anti-MBP monoclonal antibody to reveal gC1qR and bound globular head modules, respectively. Cells were washed and treated with Alexa Fluor 488 conjugated secondary goat anti-rabbit antibody and Alexa Fluor 647 conjugated secondary donkey anti-mouse antibody and the nucleus was stained with Hoechst 33342. Cells were then examined under Leica fluorescence microscope with 40× magnification. In the merged images gC1qR is green; globular heads are red; and nucleus is blue. Arrows point to bound globular heads with colocalization of globular heads and gC1qR seen in orange in the merged images. Scale bars: 10 μm.

    Article Snippet: To isolate monocytes, blood in RPMI 1640 was separated on a Ficol column (Ficol-Plaque Plus, GE healthcare) by centrifugation at 2000 rpm for 16 min at room temperature.

    Techniques: Incubation, Staining, Fluorescence, Microscopy

    Effect of the necrotic condition or nutritional deficiency on the mRNA expression of FADS1 ( a , b ), FADS2 ( c , d ), and FADS3 ( e , f ). Human brain (glioblastoma astrocytoma) U-87 MG cell line cultured in EMEM medium with 10% FBS, 2 mM l -glutamine, 1 mM sodium pyruvate, 1% non-essential amino acids, 100 U/mL penicillin, and 100 µg/mL streptomycin. U-87 MG cells were seeded in 6-well plates. After 72 h incubation, cells were washed three times with PBS solution. Next, cells were cultured for 24 h under three different conditions (control, nutrient deficiency, and necrotic). Control cells were suspended in full medium, while starved cells were grown in medium with low concentration of l -glutamine (0.2 mM) and without sodium pyruvate. For the induction of necrotic conditions, cells were incubated in medium supplemented with 200 µM H 2 O 2 . After 24 h of incubation, the cells were trypsinized and analyzed using qRT-PCR. **—statistically significant difference in the expression of a given desaturase between the tumor area according to the Wilcoxon signed-rank test ( p

    Journal: Biomolecules

    Article Title: Expression of SCD and FADS2 Is Lower in the Necrotic Core and Growing Tumor Area than in the Peritumoral Area of Glioblastoma Multiforme

    doi: 10.3390/biom10050727

    Figure Lengend Snippet: Effect of the necrotic condition or nutritional deficiency on the mRNA expression of FADS1 ( a , b ), FADS2 ( c , d ), and FADS3 ( e , f ). Human brain (glioblastoma astrocytoma) U-87 MG cell line cultured in EMEM medium with 10% FBS, 2 mM l -glutamine, 1 mM sodium pyruvate, 1% non-essential amino acids, 100 U/mL penicillin, and 100 µg/mL streptomycin. U-87 MG cells were seeded in 6-well plates. After 72 h incubation, cells were washed three times with PBS solution. Next, cells were cultured for 24 h under three different conditions (control, nutrient deficiency, and necrotic). Control cells were suspended in full medium, while starved cells were grown in medium with low concentration of l -glutamine (0.2 mM) and without sodium pyruvate. For the induction of necrotic conditions, cells were incubated in medium supplemented with 200 µM H 2 O 2 . After 24 h of incubation, the cells were trypsinized and analyzed using qRT-PCR. **—statistically significant difference in the expression of a given desaturase between the tumor area according to the Wilcoxon signed-rank test ( p

    Article Snippet: Cell Culture and Treatment Human brain cells (glioblastoma astrocytoma, U-87 MG cell line) from the European Collection of Authenticated Cell Cultures (ECACC) were cultured in eagle’s minimum essential medium (EMEM), (Sigma-Aldrich, Poznań, Poland) supplemented with 10% (v /v ) heat-inactivated fetal bovine serum (FBS; Gibco Limited, Poznań Poland), 2 mM l -glutamine, 1 mM sodium pyruvate (Sigma-Aldrich, Poznań, Poland), 1% non-essential amino acids (Sigma-Aldrich, Poznań, Poland), 100 U/mL penicillin (Gibco Limited, Poznań, Poland), and 100 µg/mL streptomycin (Gibco Limited, Poznań, Poland), at 37 °C in a humidified atmosphere of 95% air and 5% CO2 .

    Techniques: Expressing, Cell Culture, Incubation, Concentration Assay, Quantitative RT-PCR

    The effect of necrotic condition or nutritional deficiency on the mRNA expression of SCD ( a , b ) and SCD5 ( c , d ). Human brain (glioblastoma astrocytoma) U-87 MG cell line cultured in eagle’s minimum essential medium (EMEM) with 10% fetal bovine serum (FBS), 2 mM l -glutamine, 1 mM sodium pyruvate, 1% non essential amino acids, 100 U/mL penicillin, and 100 µg/mL streptomycin. U-87 MG cells were seeded in 6-well plates. After 72 h incubation, cells were washed three times with phosphate-buffered saline (PBS) solution and cultured for 24 h under three different conditions (control, nutrient deficiency, and necrotic). Control cells were suspended in full medium, starved cells were grown in medium with a low concentration of l -glutamine (0.2 mM) and without sodium pyruvate. For the induction of necrotic conditions, cells were incubated in medium supplemented with 200 µM H 2 O 2 . After 24 h of incubation, the cells were trypsinized and analyzed using qRT-PCR. **—statistically significant difference in the expression of a given desaturase between the tumor area according to the Wilcoxon signed-rank test ( p

    Journal: Biomolecules

    Article Title: Expression of SCD and FADS2 Is Lower in the Necrotic Core and Growing Tumor Area than in the Peritumoral Area of Glioblastoma Multiforme

    doi: 10.3390/biom10050727

    Figure Lengend Snippet: The effect of necrotic condition or nutritional deficiency on the mRNA expression of SCD ( a , b ) and SCD5 ( c , d ). Human brain (glioblastoma astrocytoma) U-87 MG cell line cultured in eagle’s minimum essential medium (EMEM) with 10% fetal bovine serum (FBS), 2 mM l -glutamine, 1 mM sodium pyruvate, 1% non essential amino acids, 100 U/mL penicillin, and 100 µg/mL streptomycin. U-87 MG cells were seeded in 6-well plates. After 72 h incubation, cells were washed three times with phosphate-buffered saline (PBS) solution and cultured for 24 h under three different conditions (control, nutrient deficiency, and necrotic). Control cells were suspended in full medium, starved cells were grown in medium with a low concentration of l -glutamine (0.2 mM) and without sodium pyruvate. For the induction of necrotic conditions, cells were incubated in medium supplemented with 200 µM H 2 O 2 . After 24 h of incubation, the cells were trypsinized and analyzed using qRT-PCR. **—statistically significant difference in the expression of a given desaturase between the tumor area according to the Wilcoxon signed-rank test ( p

    Article Snippet: Cell Culture and Treatment Human brain cells (glioblastoma astrocytoma, U-87 MG cell line) from the European Collection of Authenticated Cell Cultures (ECACC) were cultured in eagle’s minimum essential medium (EMEM), (Sigma-Aldrich, Poznań, Poland) supplemented with 10% (v /v ) heat-inactivated fetal bovine serum (FBS; Gibco Limited, Poznań Poland), 2 mM l -glutamine, 1 mM sodium pyruvate (Sigma-Aldrich, Poznań, Poland), 1% non-essential amino acids (Sigma-Aldrich, Poznań, Poland), 100 U/mL penicillin (Gibco Limited, Poznań, Poland), and 100 µg/mL streptomycin (Gibco Limited, Poznań, Poland), at 37 °C in a humidified atmosphere of 95% air and 5% CO2 .

    Techniques: Expressing, Cell Culture, Incubation, Concentration Assay, Quantitative RT-PCR

    F-ATPase/VGCC protein complex verification. a. 1D immunoblot analysis of the VGCC α2δ-1 subunit in neutrophils. The VGCC α2δ-1 subunit-containing protein complexes in a NativePAGE Novex 4–16% Bis-Tris gel were detected at approximately 750 kDa via immunoblotting, the same position as the F-ATPase F1 β-subunit. b. 2D immunoblot analysis of the F-ATPase and VGCC protein complex. Plasma membrane lysed by 2% digitonin was loaded and run on a BN-PAGE gel. One lane (Sample) was cut and equilibrated in SDS loading buffer, followed by fixation on a SDS-PAGE gel for 2D electrophoretic analysis. Two separate immunoblot analyses with a primary antibody against the VGCC α2δ-1 subunit or the F-ATPase F1 β-subunit were performed. The F-ATPase F1 β-subunit appears vertically below the VGCC α2δ-1 subunit in the same PVDF membrane. c. Immunofluorescence colocalization analysis of F-ATPase and VGCC. Representative images show that the VGCC α2δ-1 subunit and F-ATPase F1 β-subunit colocalized on the plasma membrane of neutrophils. d. Immunoprecipitation of VGCC α2δ-1 subunit and F-ATPase from plasma membrane protein in human neutrophils. Samples were immunoprecipitated with a mouse monoclonal antibody against α2 of the VGCC α2δ-1 subunit. F-ATPase was detected with a mouse monoclonal antibody against the F-ATPase F1 α-subunit or β-subunit and an HRP-conjugated goat anti-mouse IgG light chain specifically bound antibody. IgG control experiment did not detect F-ATPase

    Journal: Cell Communication and Signaling : CCS

    Article Title: F0F1 ATP synthase regulates extracellular calcium influx in human neutrophils by interacting with Cav2.3 and modulates neutrophil accumulation in the lipopolysaccharide-challenged lung

    doi: 10.1186/s12964-020-0515-3

    Figure Lengend Snippet: F-ATPase/VGCC protein complex verification. a. 1D immunoblot analysis of the VGCC α2δ-1 subunit in neutrophils. The VGCC α2δ-1 subunit-containing protein complexes in a NativePAGE Novex 4–16% Bis-Tris gel were detected at approximately 750 kDa via immunoblotting, the same position as the F-ATPase F1 β-subunit. b. 2D immunoblot analysis of the F-ATPase and VGCC protein complex. Plasma membrane lysed by 2% digitonin was loaded and run on a BN-PAGE gel. One lane (Sample) was cut and equilibrated in SDS loading buffer, followed by fixation on a SDS-PAGE gel for 2D electrophoretic analysis. Two separate immunoblot analyses with a primary antibody against the VGCC α2δ-1 subunit or the F-ATPase F1 β-subunit were performed. The F-ATPase F1 β-subunit appears vertically below the VGCC α2δ-1 subunit in the same PVDF membrane. c. Immunofluorescence colocalization analysis of F-ATPase and VGCC. Representative images show that the VGCC α2δ-1 subunit and F-ATPase F1 β-subunit colocalized on the plasma membrane of neutrophils. d. Immunoprecipitation of VGCC α2δ-1 subunit and F-ATPase from plasma membrane protein in human neutrophils. Samples were immunoprecipitated with a mouse monoclonal antibody against α2 of the VGCC α2δ-1 subunit. F-ATPase was detected with a mouse monoclonal antibody against the F-ATPase F1 α-subunit or β-subunit and an HRP-conjugated goat anti-mouse IgG light chain specifically bound antibody. IgG control experiment did not detect F-ATPase

    Article Snippet: Voltage-gated calcium channel (VGCC) α2δ-1 was detected with a rabbit polyclonal antibody against the VGCC α2δ-1 subunit (1:200, C5105, Sigma-Aldrich, St. Louis, MO, USA) and an HRP-conjugated goat anti-rabbit IgG H & L (1:2000, ab6721, Abcam, Cambridge, UK).

    Techniques: Polyacrylamide Gel Electrophoresis, SDS Page, Immunofluorescence, Immunoprecipitation

    BrainPhys increases neuronal morphology and Aβ secretion in SH-SY5Y cells. SH-SY5Y neuroblastoma cells pre-differentiated with RA for five-seven days and thereafter seeded onto poly-l-ornithine- and laminin-coated plates and cultured either in standard medium (DMEM/F12) or BrainPhys for 7–14 days. ( A ) Phase contrast images of SH-SY5Y cells cultured in standard DMEM/F12 medium (left panel) and cells cultured in BrainPhys media for 7 days (middle panel) or 14 days (right panel) are shown. Increased neuronal morphology with longer and highly branched neurites is observed in BrainPhys-cultured SH-SY5Y cells already after 7 days (middle panel) and increase further with another 7 days (right panel) of BrainPhys culturing. Representative images from one out of three experiments are shown. Scale bar = 100 μM. ( B ) Concentrations of secreted Aβ peptides measured from cell-conditioned media of SH-SY5Y cells cultured in either DMEM/F12 supplemented with retinoic acid for 7 days or in BrainPhys media for 14 days. BrainPhys significantly increases the secretion of both (I) Aβ40 and (II) Aβ42 as compared to the standard medium (Aβ38 is below the lower limit of detection of the assay). Mean values of three separate experiments were analysed with Student’s t-test. **p ≤ 0.01. Bars represent mean +/− SEM. ( C ) The cell numbers from phase contrast images from three separate experiments were analysed with Student’s t-test. No significant differences in cell numbers were observed between NMM- and BrainPhys-cultured neurons. Bars represent mean +/− SEM presented as relative to NMM.

    Journal: Scientific Reports

    Article Title: Accelerated neuronal and synaptic maturation by BrainPhys medium increases Aβ secretion and alters Aβ peptide ratios from iPSC-derived cortical neurons

    doi: 10.1038/s41598-020-57516-7

    Figure Lengend Snippet: BrainPhys increases neuronal morphology and Aβ secretion in SH-SY5Y cells. SH-SY5Y neuroblastoma cells pre-differentiated with RA for five-seven days and thereafter seeded onto poly-l-ornithine- and laminin-coated plates and cultured either in standard medium (DMEM/F12) or BrainPhys for 7–14 days. ( A ) Phase contrast images of SH-SY5Y cells cultured in standard DMEM/F12 medium (left panel) and cells cultured in BrainPhys media for 7 days (middle panel) or 14 days (right panel) are shown. Increased neuronal morphology with longer and highly branched neurites is observed in BrainPhys-cultured SH-SY5Y cells already after 7 days (middle panel) and increase further with another 7 days (right panel) of BrainPhys culturing. Representative images from one out of three experiments are shown. Scale bar = 100 μM. ( B ) Concentrations of secreted Aβ peptides measured from cell-conditioned media of SH-SY5Y cells cultured in either DMEM/F12 supplemented with retinoic acid for 7 days or in BrainPhys media for 14 days. BrainPhys significantly increases the secretion of both (I) Aβ40 and (II) Aβ42 as compared to the standard medium (Aβ38 is below the lower limit of detection of the assay). Mean values of three separate experiments were analysed with Student’s t-test. **p ≤ 0.01. Bars represent mean +/− SEM. ( C ) The cell numbers from phase contrast images from three separate experiments were analysed with Student’s t-test. No significant differences in cell numbers were observed between NMM- and BrainPhys-cultured neurons. Bars represent mean +/− SEM presented as relative to NMM.

    Article Snippet: At this point, the cells were counted using a NucleoCounter® NC-200™ (Chemometec) and re-plated at a confluency of 50 000 cells/cm2 onto poly-L-ornithine (Sigma Aldrich) and laminin-coated plates in NMM (see Supporting Table ).

    Techniques: Cell Culture

    Flow cytometry analysis of mesenchymal stem cell markers CD105 and CD90 in MDA-MB-231 cells. A. Results from flow cytometry analysis, with series of gates set for CD105+ or CD90+ identification. R2, R3, R4 and R5 represented cell subpopulations identified as CD105 + /CD90 +  (0.99%), CD105+/CD90- cell subpopulation (4.93%), CD105 - /CD90 -  cell subpopulation (90.77%) and CD105-/CD90+ cell subpopulation (3.31%) respectively. Morphology of cultured MDA-MB-231 cells in Leibovitz’s L-15 media by phase-contrast microscopy (×100) was shown in B, while sorted CD105 + /CD90 +  and CD105 - /CD90 -  subpopulations after 72 hours incubation (×200) shown in C.

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: Isolation and characterization of CD105+/CD90+ subpopulation in breast cancer MDA-MB-231 cell line

    doi:

    Figure Lengend Snippet: Flow cytometry analysis of mesenchymal stem cell markers CD105 and CD90 in MDA-MB-231 cells. A. Results from flow cytometry analysis, with series of gates set for CD105+ or CD90+ identification. R2, R3, R4 and R5 represented cell subpopulations identified as CD105 + /CD90 + (0.99%), CD105+/CD90- cell subpopulation (4.93%), CD105 - /CD90 - cell subpopulation (90.77%) and CD105-/CD90+ cell subpopulation (3.31%) respectively. Morphology of cultured MDA-MB-231 cells in Leibovitz’s L-15 media by phase-contrast microscopy (×100) was shown in B, while sorted CD105 + /CD90 + and CD105 - /CD90 - subpopulations after 72 hours incubation (×200) shown in C.

    Article Snippet: Cells were cultured in Leibovitz’s L-15 medium (GIBCO, USA) containing 10% fetal bovine serum (FBS) and Penicillin/Streptomycin, and at 37°C in a humidified 5% CO2 atmosphere.

    Techniques: Flow Cytometry, Cytometry, Multiple Displacement Amplification, Cell Culture, Microscopy, Incubation

    Characterization of serine-glycine one-carbon pathway in KL cells a, Detailed graph of SGOC network. Enzymatic inhibitors used in this study are marked in red. b, Reactive oxygen species in K or KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2 were measured by DCFDA (left) and CellRox staining (right). Data are normalized to cell number (n=4). c, Six-day proliferation assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing lack of growth rescue by N-acetylcysteine (NAC). Data are expressed as relative to day 0 (n=6). d, Three-day growth assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing the lack of rescue by excess nucleosides (adenosine, guanosine, thymidine, uridine, cytidine, 1 mM each). Data are presented as percentage of the growth of shControl cells (n=16). e, Proliferation of K or KL cells treated with aminooxyacetate (AOA). Data are expressed as relative to day 0 (n=8). f, Five-day proliferation of K or KL cells treated with AOA and/or NAC. Data are expressed as relative to day 0 (n=6). g, Data from RNA-seq ( left panel ) and quantitative proteomics ( right panel ) showing levels of genes involved in the production of SAM in K and KL. The data plotted are expressed as mean-centered values. h, Proliferation of K or KL cells treated with 2 mM cycloleucine. Data are expressed as percentage of the growth of vehicle treated cells (n=12). Shown are data pooled from two (b–f, h) experiments. For all panels, error bars are standard deviation unless otherwise stated and statistical significance is indicated as follows: *P

    Journal: Nature

    Article Title: LKB1 loss links serine metabolism to DNA methylation and tumourigenesis

    doi: 10.1038/nature20132

    Figure Lengend Snippet: Characterization of serine-glycine one-carbon pathway in KL cells a, Detailed graph of SGOC network. Enzymatic inhibitors used in this study are marked in red. b, Reactive oxygen species in K or KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2 were measured by DCFDA (left) and CellRox staining (right). Data are normalized to cell number (n=4). c, Six-day proliferation assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing lack of growth rescue by N-acetylcysteine (NAC). Data are expressed as relative to day 0 (n=6). d, Three-day growth assay of KL cells transduced with shControl, shPSAT1-1 or shPSAT1-2, showing the lack of rescue by excess nucleosides (adenosine, guanosine, thymidine, uridine, cytidine, 1 mM each). Data are presented as percentage of the growth of shControl cells (n=16). e, Proliferation of K or KL cells treated with aminooxyacetate (AOA). Data are expressed as relative to day 0 (n=8). f, Five-day proliferation of K or KL cells treated with AOA and/or NAC. Data are expressed as relative to day 0 (n=6). g, Data from RNA-seq ( left panel ) and quantitative proteomics ( right panel ) showing levels of genes involved in the production of SAM in K and KL. The data plotted are expressed as mean-centered values. h, Proliferation of K or KL cells treated with 2 mM cycloleucine. Data are expressed as percentage of the growth of vehicle treated cells (n=12). Shown are data pooled from two (b–f, h) experiments. For all panels, error bars are standard deviation unless otherwise stated and statistical significance is indicated as follows: *P

    Article Snippet: Laminin (23017-95), 2NBDG (N13195), DCFDA (C6827), CellROX Green , CyQuant NF , bovine pituitary extract (13038-14), HBSS, RPMI, DMEM, DMEM:F12, MEM penicillin-streptomycin, pyruvate solution, fetal bovine serum (FBS) Alexa 488 and 568-conjugated secondary antibodies from Life Technologies; nicotinamide (N3376), trypsin inhibitor (T6522), dexamethasone (D4902), S-adenosylmethionine (A2408), 3,3,5-tri-iodo-L-thyronine (91990), oligomycin (75351), antimycin A (A8674), 2-deoxyglucose (D6134), dichloroacetate (347795), collagenase (C7657), glucose (G7528), aminooxyacetate , N-acetylcysteine (A9165), adenosine (A4036), guanosine (G6264), thymidine (T1895), uridine (U3003), cytidine (C4654), cycloleucine , cholera toxin (C8052), L-serine (S4500), betaine (61962), dimethylglycine (D1156), tamoxifen (T5148) and methylene blue (M4159) from Sigma; FCCP (0453), decitabine (2624), RG108 (3295), EGCG (4524), Compound C (3093), Torin 1 (4247) and galloflavin (4795) from Tocris; mouse EGF (354001), NuSerum IV (355104), ITS+ Premix (354352) and matrigel (354234) from Corning; SGI1027 (S7276) from Selleckchem; caspase-Glo 3/7 kit (G811A) and Celltiter-Glo kit (G755B) from Promega; 13 C-U-Glucose (CLM-1396-1) and 15 N-Glutamine (NLM-1016-1) from Cambridge Isotope Laboratories Inc; dispase (165-859) from Roche; lactate assay kit (K607-100) from Biovision Inc; Vectashield with DAPI (H1500) from Vector Laboratories; Bridge-IT SAM assay kit (1-1-1003B) from Medionics; meDIP kit (55009) from Active Motif; 3DZA (9000785) from Cayman Chemicals; Adeno-FlpO (1760) from Vector Biolabs; Adeno-Cre-eGFP from the Viral Vector Core Facility, University of Iowa.

    Techniques: Transduction, Staining, Proliferation Assay, Growth Assay, RNA Sequencing Assay, Standard Deviation