thin layer chromatography  (Millipore)


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    Structured Review

    Millipore thin layer chromatography
    Thin Layer Chromatography, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 141 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/thin layer chromatography/product/Millipore
    Average 94 stars, based on 141 article reviews
    Price from $9.99 to $1999.99
    thin layer chromatography - by Bioz Stars, 2020-04
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    Article Title: The Stringent Response Determines the Ability of a Commensal Bacterium to Survive Starvation and to Persist in the Gut
    Article Snippet: To analyze labeled nucleotides by thin-layer chromatography, 3 μL of extract was spotted on PEI-cellulose TLC sheets (Sigma) and developed in 1.5 M KH2 PO4 (pH 3.9).

    Article Title: Design, Synthesis, and X-Ray Studies of Potent HIV-1 Protease Inhibitors incorporating aminothiochromane and aminotetrahydronaphthalene carboxamide derivatives as the P2 ligands.
    Article Snippet: Thin-layer chromatography was carried out using EMD Millipore TLC silica gel 60 F254 plates.

    Article Title: Design and Synthesis of Potent HIV-1 Protease Inhibitors Containing Bicyclic Oxazolidinone Scaffold as the P2 Ligands: Structure–Activity Studies and Biological and X-ray Structural Studies
    Article Snippet: Thin layer chromatography was carried out using EMD Millipore TLC silica gel 60 F254 plates.

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  • 88
    Millipore amauroderma rude
    Identification of ergosterol A. The structure and composition of ergosterol analyzed by EI-MS. B. Structure of ergosterol based on the NMR data. C. Measurement of ergosterol concentrations from Ganoderma sinense, Ganoderma lucidum, <t>Amauroderma</t> rude, Coriolus versicolor , and Ganoderma tsugae .
    Amauroderma Rude, supplied by Millipore, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Millipore a machipongonensis cultures
    Diverse members of the Bacteroidetes phylum induce rosette colony development. A maximum likelihood phylogeny inferred from 16S rDNA gene sequences reveals the evolutionary relationships among A. <t>machipongonensis</t> , other members of the Bacteroidetes phylum, and representative γ-proteobacteria (γ), α-proteobacteria (α), and Gram-positive (+) bacteria. All 15 members of the Algoriphagus genus ( Table 1 ), as well as six other species in the Bacteroidetes phylum, were competent to induce colony development (filled squares). In contrast, no species outside of Bacteroidetes and most of the non- Algoriphagus bacteria tested failed to induce rosette colony development (open squares). Scale bar, 0.1 substitutions per nucleotide position. DOI: http://dx.doi.org/10.7554/eLife.00013.006
    A Machipongonensis Cultures, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore human keratinocytes
    Rapamycin induced SPT and TGF‐β1 mRNA expression and TGF‐β1 induced ceramide synthesis and the mRNA levels of SPT in human <t>keratinocytes.</t> The mRNA levels of SPT (A, C) and TGF‐β1 (B) in human keratinocytes were measured by quantitative PCR and are expressed as a relative value to that of GAPDH. Ceramide levels in human keratinocytes were quantified by TLC. The ceramide levels (D) are expressed as a fold change relative to the band intensity in cells treated without TGF‐β1. Bars are given as mean ± SD ( n = 3). * P
    Human Keratinocytes, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Millipore α ce
    Tat/TAR-dependent phosphorylation of the RNAP II CTD stimulates cotranscriptional capping of viral mRNA. ( A ) HCE is recruited into HIV-1 TECs through phosphorylated RNAP II CTD. PICs were analyzed by Western blotting with <t>α-CE</t> antibody. TECs stalled at G36 and C81 were incubated with HCE and extensively washed to remove unbound proteins before Western blot analysis with α-CE antibody. The WT and TAR mutant (TM26) HIV-1 LTR templates are indicated. IN, input. ( B ) Tat/TAR-dependent phosphorylation of the RNAP II CTD stimulates capping of viral mRNA. The indicated TECs were supplemented with HCE and then incubated with [α- 32 P]GTP. GMP-labeled transcripts were analyzed by electrophoresis through 10% polyacrylamide gels containing 7 M urea in TBE buffer followed by autoradiography ( Upper ). GMP-labeled RNAs isolated from the indicated TECs were analyzed by S1 nuclease digestion followed by polyethyleneimine-cellulose TLC ( Lower ).
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    Identification of ergosterol A. The structure and composition of ergosterol analyzed by EI-MS. B. Structure of ergosterol based on the NMR data. C. Measurement of ergosterol concentrations from Ganoderma sinense, Ganoderma lucidum, Amauroderma rude, Coriolus versicolor , and Ganoderma tsugae .

    Journal: Oncotarget

    Article Title: Ergosterol purified from medicinal mushroom Amauroderma rude inhibits cancer growth in vitro and in vivo by up-regulating multiple tumor suppressors

    doi:

    Figure Lengend Snippet: Identification of ergosterol A. The structure and composition of ergosterol analyzed by EI-MS. B. Structure of ergosterol based on the NMR data. C. Measurement of ergosterol concentrations from Ganoderma sinense, Ganoderma lucidum, Amauroderma rude, Coriolus versicolor , and Ganoderma tsugae .

    Article Snippet: Western blotting After being treated with the purified compound of Amauroderma rude , cells were lysed by the lysis buffer containing protease inhibitor (CALBIOCHEM, USA) on ice for 30 min and centrifuged to obtain clear cell lysates.

    Techniques: Mass Spectrometry, Nuclear Magnetic Resonance

    Purification of anti-cancer ingredient and molecule from Amauroderma rude The dry fruit bodies of Amauroderma rude were extracted using 95% ethanol. The extract was subject to chromatography and HPLC purification as indicated. Human breast cancer cell cultures were used to screen the anti-cancer ingredients in each step until single pick was obtained from HPLC. AReth, ethanol extract of Amauroderma rude ; ARchl, chloroform fraction of Amauroderma rude ; P/A, ratios of petroleum ether to ether in the elution buffer; Meth, pure methanol used to elute the column; Fr, fraction number; TL, fractions obtained from the Thin layer Chromatography; inset, photo of a dry Amauroderma rude .

    Journal: Oncotarget

    Article Title: Ergosterol purified from medicinal mushroom Amauroderma rude inhibits cancer growth in vitro and in vivo by up-regulating multiple tumor suppressors

    doi:

    Figure Lengend Snippet: Purification of anti-cancer ingredient and molecule from Amauroderma rude The dry fruit bodies of Amauroderma rude were extracted using 95% ethanol. The extract was subject to chromatography and HPLC purification as indicated. Human breast cancer cell cultures were used to screen the anti-cancer ingredients in each step until single pick was obtained from HPLC. AReth, ethanol extract of Amauroderma rude ; ARchl, chloroform fraction of Amauroderma rude ; P/A, ratios of petroleum ether to ether in the elution buffer; Meth, pure methanol used to elute the column; Fr, fraction number; TL, fractions obtained from the Thin layer Chromatography; inset, photo of a dry Amauroderma rude .

    Article Snippet: Western blotting After being treated with the purified compound of Amauroderma rude , cells were lysed by the lysis buffer containing protease inhibitor (CALBIOCHEM, USA) on ice for 30 min and centrifuged to obtain clear cell lysates.

    Techniques: Purification, Chromatography, High Performance Liquid Chromatography, Thin Layer Chromatography

    Diverse members of the Bacteroidetes phylum induce rosette colony development. A maximum likelihood phylogeny inferred from 16S rDNA gene sequences reveals the evolutionary relationships among A. machipongonensis , other members of the Bacteroidetes phylum, and representative γ-proteobacteria (γ), α-proteobacteria (α), and Gram-positive (+) bacteria. All 15 members of the Algoriphagus genus ( Table 1 ), as well as six other species in the Bacteroidetes phylum, were competent to induce colony development (filled squares). In contrast, no species outside of Bacteroidetes and most of the non- Algoriphagus bacteria tested failed to induce rosette colony development (open squares). Scale bar, 0.1 substitutions per nucleotide position. DOI: http://dx.doi.org/10.7554/eLife.00013.006

    Journal: eLife

    Article Title: A bacterial sulfonolipid triggers multicellular development in the closest living relatives of animalsDecision letterAuthor response

    doi: 10.7554/eLife.00013.030

    Figure Lengend Snippet: Diverse members of the Bacteroidetes phylum induce rosette colony development. A maximum likelihood phylogeny inferred from 16S rDNA gene sequences reveals the evolutionary relationships among A. machipongonensis , other members of the Bacteroidetes phylum, and representative γ-proteobacteria (γ), α-proteobacteria (α), and Gram-positive (+) bacteria. All 15 members of the Algoriphagus genus ( Table 1 ), as well as six other species in the Bacteroidetes phylum, were competent to induce colony development (filled squares). In contrast, no species outside of Bacteroidetes and most of the non- Algoriphagus bacteria tested failed to induce rosette colony development (open squares). Scale bar, 0.1 substitutions per nucleotide position. DOI: http://dx.doi.org/10.7554/eLife.00013.006

    Article Snippet: Conditioned medium (CM) was generated by pelleting either choanoflagellates grown in cereal grass infused with seawater or A. machipongonensis cultures grown in seawater complete medium ( ) and filtering the culture supernatant through a 0.22 μm pore filter (Millipore) to remove live bacteria.

    Techniques:

    Frequency of rosette colonies in S. rosetta environmental isolate ATCC 50818, RCA with and without A. machipongonensis and a monoxenic line with A. machipongonensis feeder bacteria (Px1). Altering bacterial diversity in S. rosetta cultures alters the frequency of rosette colonies. Data are the whisker-box plots of the frequency of colonial cells in ATCC 50818 and a monoxenic culture of S. rosetta fed only A. machipongonensis bacteria (Px1) for three experiments. DOI: http://dx.doi.org/10.7554/eLife.00013.004

    Journal: eLife

    Article Title: A bacterial sulfonolipid triggers multicellular development in the closest living relatives of animalsDecision letterAuthor response

    doi: 10.7554/eLife.00013.030

    Figure Lengend Snippet: Frequency of rosette colonies in S. rosetta environmental isolate ATCC 50818, RCA with and without A. machipongonensis and a monoxenic line with A. machipongonensis feeder bacteria (Px1). Altering bacterial diversity in S. rosetta cultures alters the frequency of rosette colonies. Data are the whisker-box plots of the frequency of colonial cells in ATCC 50818 and a monoxenic culture of S. rosetta fed only A. machipongonensis bacteria (Px1) for three experiments. DOI: http://dx.doi.org/10.7554/eLife.00013.004

    Article Snippet: Conditioned medium (CM) was generated by pelleting either choanoflagellates grown in cereal grass infused with seawater or A. machipongonensis cultures grown in seawater complete medium ( ) and filtering the culture supernatant through a 0.22 μm pore filter (Millipore) to remove live bacteria.

    Techniques: Whisker Assay

    Separation of A. machipongonensis sphingolipids by thin layer chromatography (TLC). Lipids enriched in sphingolipids were separated by TLC after visualization with ammonium molybdate in 10% H 2 SO 4 . Bands (1-12) as well as regions between bands (A-F) were tested for morphogenic activity. Region F possessed activity and was further purified. DOI: http://dx.doi.org/10.7554/eLife.00013.009

    Journal: eLife

    Article Title: A bacterial sulfonolipid triggers multicellular development in the closest living relatives of animalsDecision letterAuthor response

    doi: 10.7554/eLife.00013.030

    Figure Lengend Snippet: Separation of A. machipongonensis sphingolipids by thin layer chromatography (TLC). Lipids enriched in sphingolipids were separated by TLC after visualization with ammonium molybdate in 10% H 2 SO 4 . Bands (1-12) as well as regions between bands (A-F) were tested for morphogenic activity. Region F possessed activity and was further purified. DOI: http://dx.doi.org/10.7554/eLife.00013.009

    Article Snippet: Conditioned medium (CM) was generated by pelleting either choanoflagellates grown in cereal grass infused with seawater or A. machipongonensis cultures grown in seawater complete medium ( ) and filtering the culture supernatant through a 0.22 μm pore filter (Millipore) to remove live bacteria.

    Techniques: Thin Layer Chromatography, Activity Assay, Purification

    Detection of RIF-1 in the conditioned medium of A. machipongonensis . RIF-1 (bottom panel) was detected in the conditioned medium after the broth was concentrated 250 times. DOI: http://dx.doi.org/10.7554/eLife.00013.027

    Journal: eLife

    Article Title: A bacterial sulfonolipid triggers multicellular development in the closest living relatives of animalsDecision letterAuthor response

    doi: 10.7554/eLife.00013.030

    Figure Lengend Snippet: Detection of RIF-1 in the conditioned medium of A. machipongonensis . RIF-1 (bottom panel) was detected in the conditioned medium after the broth was concentrated 250 times. DOI: http://dx.doi.org/10.7554/eLife.00013.027

    Article Snippet: Conditioned medium (CM) was generated by pelleting either choanoflagellates grown in cereal grass infused with seawater or A. machipongonensis cultures grown in seawater complete medium ( ) and filtering the culture supernatant through a 0.22 μm pore filter (Millipore) to remove live bacteria.

    Techniques:

    Rapamycin induced SPT and TGF‐β1 mRNA expression and TGF‐β1 induced ceramide synthesis and the mRNA levels of SPT in human keratinocytes. The mRNA levels of SPT (A, C) and TGF‐β1 (B) in human keratinocytes were measured by quantitative PCR and are expressed as a relative value to that of GAPDH. Ceramide levels in human keratinocytes were quantified by TLC. The ceramide levels (D) are expressed as a fold change relative to the band intensity in cells treated without TGF‐β1. Bars are given as mean ± SD ( n = 3). * P

    Journal: FEBS Open Bio

    Article Title: mTOR inhibition by rapamycin increases ceramide synthesis by promoting transforming growth factor‐β1/Smad signaling in the skin

    doi: 10.1002/2211-5463.12039

    Figure Lengend Snippet: Rapamycin induced SPT and TGF‐β1 mRNA expression and TGF‐β1 induced ceramide synthesis and the mRNA levels of SPT in human keratinocytes. The mRNA levels of SPT (A, C) and TGF‐β1 (B) in human keratinocytes were measured by quantitative PCR and are expressed as a relative value to that of GAPDH. Ceramide levels in human keratinocytes were quantified by TLC. The ceramide levels (D) are expressed as a fold change relative to the band intensity in cells treated without TGF‐β1. Bars are given as mean ± SD ( n = 3). * P

    Article Snippet: Human keratinocytes were seeded in 96‐well plates in culture medium at a density of 1 × 104 cells per well and were incubated for 24 h. Cells were treated with rapamycin (30 or 100 nm ; Calbiochem, Darmstadt, Germany) and 0.002% dimethyl sulfoxide (DMSO) as vehicle control for 24 h. In an additional experiment, cells were seeded in 6 or 96‐well plates.

    Techniques: Single-particle Tracking, Expressing, Real-time Polymerase Chain Reaction, Thin Layer Chromatography

    Effects of rapamycin on TGF‐β1/Smad signaling‐induced SPT mRNA expression in human keratinocytes. Cells were treated with TGF‐β1 (30 ng·mL −1 ) for 0, 12, 24, 36, or 48 h. The phosphorylations of Smad2 (Ser465/467) (A) and Smad3 (Ser423/425) (B, C) were determined by immunoblot analysis. * P

    Journal: FEBS Open Bio

    Article Title: mTOR inhibition by rapamycin increases ceramide synthesis by promoting transforming growth factor‐β1/Smad signaling in the skin

    doi: 10.1002/2211-5463.12039

    Figure Lengend Snippet: Effects of rapamycin on TGF‐β1/Smad signaling‐induced SPT mRNA expression in human keratinocytes. Cells were treated with TGF‐β1 (30 ng·mL −1 ) for 0, 12, 24, 36, or 48 h. The phosphorylations of Smad2 (Ser465/467) (A) and Smad3 (Ser423/425) (B, C) were determined by immunoblot analysis. * P

    Article Snippet: Human keratinocytes were seeded in 96‐well plates in culture medium at a density of 1 × 104 cells per well and were incubated for 24 h. Cells were treated with rapamycin (30 or 100 nm ; Calbiochem, Darmstadt, Germany) and 0.002% dimethyl sulfoxide (DMSO) as vehicle control for 24 h. In an additional experiment, cells were seeded in 6 or 96‐well plates.

    Techniques: Single-particle Tracking, Expressing

    Tat/TAR-dependent phosphorylation of the RNAP II CTD stimulates cotranscriptional capping of viral mRNA. ( A ) HCE is recruited into HIV-1 TECs through phosphorylated RNAP II CTD. PICs were analyzed by Western blotting with α-CE antibody. TECs stalled at G36 and C81 were incubated with HCE and extensively washed to remove unbound proteins before Western blot analysis with α-CE antibody. The WT and TAR mutant (TM26) HIV-1 LTR templates are indicated. IN, input. ( B ) Tat/TAR-dependent phosphorylation of the RNAP II CTD stimulates capping of viral mRNA. The indicated TECs were supplemented with HCE and then incubated with [α- 32 P]GTP. GMP-labeled transcripts were analyzed by electrophoresis through 10% polyacrylamide gels containing 7 M urea in TBE buffer followed by autoradiography ( Upper ). GMP-labeled RNAs isolated from the indicated TECs were analyzed by S1 nuclease digestion followed by polyethyleneimine-cellulose TLC ( Lower ).

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: The Tat/TAR-dependent phosphorylation of RNA polymerase II C-terminal domain stimulates cotranscriptional capping of HIV-1 mRNA

    doi: 10.1073/pnas.1835726100

    Figure Lengend Snippet: Tat/TAR-dependent phosphorylation of the RNAP II CTD stimulates cotranscriptional capping of viral mRNA. ( A ) HCE is recruited into HIV-1 TECs through phosphorylated RNAP II CTD. PICs were analyzed by Western blotting with α-CE antibody. TECs stalled at G36 and C81 were incubated with HCE and extensively washed to remove unbound proteins before Western blot analysis with α-CE antibody. The WT and TAR mutant (TM26) HIV-1 LTR templates are indicated. IN, input. ( B ) Tat/TAR-dependent phosphorylation of the RNAP II CTD stimulates capping of viral mRNA. The indicated TECs were supplemented with HCE and then incubated with [α- 32 P]GTP. GMP-labeled transcripts were analyzed by electrophoresis through 10% polyacrylamide gels containing 7 M urea in TBE buffer followed by autoradiography ( Upper ). GMP-labeled RNAs isolated from the indicated TECs were analyzed by S1 nuclease digestion followed by polyethyleneimine-cellulose TLC ( Lower ).

    Article Snippet: Antibodies used were α-CTD H5 and H14 (Covance, Richmond, CA), α-RNAP II (N-20), α-p62 subunit of TFIIH (Santa Cruz Biotechnology), α-CE , and α-2,2,7 -trimethylguanosine (Calbiochem).

    Techniques: Western Blot, Incubation, Mutagenesis, Labeling, Electrophoresis, Autoradiography, Isolation, Thin Layer Chromatography

    Interaction between HCE and CTD phosphorylated by P-TEFb. ( A ) Tat modifies the substrate specificity of CDK9. In vitro kinase assays were performed by incubating purified RNAP II with P-TEFb and ATP (100 μM) in the absence or presence of Tat. Phosphorylated CTD was analyzed by Western blot with specific antibody H5 (α-phosphoserine 2) or H14 (α-phosphoserine 5). The hypophosphorylated (IIa) and hyperphosphorylated (IIo) forms of the largest subunit of RNAP II are indicated. ( B ) Interaction of HCE and CTD phosphorylated by P-TEFb. HCE was incubated with bead-bound GST-CTD. Bead-bound proteins were eluted by boiling in SDS loading buffer and then analyzed by Western blot with α-CE antibody.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: The Tat/TAR-dependent phosphorylation of RNA polymerase II C-terminal domain stimulates cotranscriptional capping of HIV-1 mRNA

    doi: 10.1073/pnas.1835726100

    Figure Lengend Snippet: Interaction between HCE and CTD phosphorylated by P-TEFb. ( A ) Tat modifies the substrate specificity of CDK9. In vitro kinase assays were performed by incubating purified RNAP II with P-TEFb and ATP (100 μM) in the absence or presence of Tat. Phosphorylated CTD was analyzed by Western blot with specific antibody H5 (α-phosphoserine 2) or H14 (α-phosphoserine 5). The hypophosphorylated (IIa) and hyperphosphorylated (IIo) forms of the largest subunit of RNAP II are indicated. ( B ) Interaction of HCE and CTD phosphorylated by P-TEFb. HCE was incubated with bead-bound GST-CTD. Bead-bound proteins were eluted by boiling in SDS loading buffer and then analyzed by Western blot with α-CE antibody.

    Article Snippet: Antibodies used were α-CTD H5 and H14 (Covance, Richmond, CA), α-RNAP II (N-20), α-p62 subunit of TFIIH (Santa Cruz Biotechnology), α-CE , and α-2,2,7 -trimethylguanosine (Calbiochem).

    Techniques: In Vitro, Purification, Western Blot, Incubation