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Michrom c18 column
Selection of iRT-peptides and definition of <t>iRT-C18</t> scale
C18 Column, supplied by Michrom, used in various techniques. Bioz Stars score: 92/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/c18 column/product/Michrom
Average 92 stars, based on 6 article reviews
Price from $9.99 to $1999.99
c18 column - by Bioz Stars, 2021-01
92/100 stars

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1) Product Images from "Using iRT, a normalized retention time for more targeted measurement of peptides"

Article Title: Using iRT, a normalized retention time for more targeted measurement of peptides

Journal: Proteomics

doi: 10.1002/pmic.201100463

Selection of iRT-peptides and definition of iRT-C18 scale
Figure Legend Snippet: Selection of iRT-peptides and definition of iRT-C18 scale

Techniques Used: Selection

Related Articles

Flow Cytometry:

Article Title: Identification of Pharmacological Chaperones for Gaucher Disease and Characterization of Their Effects on ?-Glucocerebrosidase by Hydrogen/Deuterium Exchange Mass Spectrometry
Article Snippet: .. [ ] Peptide fragments were eluted from the trap column and separated by C18 column (Magic C18, Michrom BioResources, Inc., Auburn, CA, USA) with a linear gradient of solvent B (13 %) to solvent B (40 %) over 23 min (solvent A, 0.05% TFA in water; solvent B, 95 % acetonitrile, 5% water, 0.0025 % TFA; flow rate 5 μL min−1 –10 μL min−1 ). .. Mass spectrometric analyses were carried out with a Thermo Finnigan LCQ3 mass spectrometer (Thermo Fisher Scientific, San Jose, CA) with a capillary temperature of 200°C.

Article Title: Analysis of the Rana catesbeiana tadpole tail fin proteome and phosphoproteome during T3-induced apoptosis: identification of a novel type I keratin
Article Snippet: .. The SCX fractions were first desalted on a C18 PepMap guard column (300 μm i.d. x 5 mm 5 μm, 100Å, LC Packings, Amsterdam) at 50 μl/minute flow rate for 15 min. Peptides were separated over a manually packed 75 μm × 15 cm C18 column (Magic C18Aq, 5μm, 100Å, Michrom Bioresources Inc., Auburn CA, USA) using a 85 min gradient of 5%-75% ACN in 0.1% formic acid flowing at 250 nL/min. .. The eluant was either sprayed directly into an Applied Biosystems QSTAR Pulsar i (Applied Biosystems/MDS SCIEX Concord, ON Canada) (ESI-QqTOF) mass spectrometer or spotted onto a MALDI target plate by the Probot for LC-MALDI analysis.

Article Title: Discovery of Histone Modification Crosstalk Networks by Stable Isotope Labeling of Amino Acids in Cell Culture Mass Spectrometry (SILAC MS) *
Article Snippet: .. Histones were separated on a 0.2 mm x 150 mm C18 column (3 μm, 200Å, Michrom Bioresources Inc., Auburn, CA) at a flow rate of 2 μl/min with mobile phase A containing H2 O with 0.1% Formic acid (FA) and mobile phase B containing ACN with 0.1% FA. .. Using a 120min gradient beginning with 2% mobile phase B, the phase B linearly increased to 5% in 10min, from 5% to 15% in 20min, from 15% to 30% in 45 min, from 30% to 50% in 15 min, and from 50% to 90% in 5 min. After washing at 90% B for 1 min, the column was equilibrated at 2% B for 24 min. A blank was run between each sample injection and a bovine histone standard was run every 10 runs for quality control.

Article Title: SILAC Peptide Ratio Calculator - A tool for SILAC Quantitation of Peptides and Posttranslational Modifications
Article Snippet: .. Histones were separated on a 0.2 mm × 150 mm C18 column (3 μm, 200Å, Michrom Bioresources Inc., Auburn, CA) at a flow rate of 2 μL/min with mobile phase A containing H2 O with 0.1% Formic acid (FA) and mobile phase B containing ACN with 0.1% FA. .. Using a 120 min gradient beginning with 2% mobile phase B, the phase B linearly increased to 5% in 10 min, from 5% to 15% in 20 min, from 15% to 30% in 45 min, from 30% to 50% in 15 min, and from 50% to 90% in 5 min. After washing at 90% B for 1 min, the column was equilibrated at 2% B for 24 min. A blank was run between each sample injection to check carryover and a bovine histone standard was run every 10 runs as a quality control.

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    Michrom c18 column
    Selection of iRT-peptides and definition of <t>iRT-C18</t> scale
    C18 Column, supplied by Michrom, used in various techniques. Bioz Stars score: 92/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/c18 column/product/Michrom
    Average 92 stars, based on 25 article reviews
    Price from $9.99 to $1999.99
    c18 column - by Bioz Stars, 2021-01
    92/100 stars
      Buy from Supplier

    85
    Michrom in house packed c18 microcapillary column
    Plumbing for automated analysis of multiple peptide samples using the HPLC autosampler and divert valve of LCQ mass spectrometer. A: In the waste mode, flow split before the peptide trap was blocked at valve position 6, so that all sample and solvent flowed through the trap. Peptides were trapped and solvent diverted to waste. The mass detector was set to Off during peptide trapping. B: In the source mode, flow split before the trap was on and diverted most solvent to waste. Flow split after the trap was blocked at valve position 6 to allow 150 nL/min of solvent gradient (detailed in Materials and Methods) to flow through the peptide trap to elute peptides into <t>C18</t> <t>microcapillary</t> column. Separated peptides were injected into the mass spectrometer for MS and MS/MS analysis. Backpressure was controlled with the length of peek tubing (0.0025″ ID) at valve position 4.
    In House Packed C18 Microcapillary Column, supplied by Michrom, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/in house packed c18 microcapillary column/product/Michrom
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    in house packed c18 microcapillary column - by Bioz Stars, 2021-01
    85/100 stars
      Buy from Supplier

    Image Search Results


    Selection of iRT-peptides and definition of iRT-C18 scale

    Journal: Proteomics

    Article Title: Using iRT, a normalized retention time for more targeted measurement of peptides

    doi: 10.1002/pmic.201100463

    Figure Lengend Snippet: Selection of iRT-peptides and definition of iRT-C18 scale

    Article Snippet: 100fmol each in 1 μg total protein) and measured in LC-MRM with a 90 min linear gradient (5%–35% acetonitrile as organic modifier with 0.1% formic acid) on a C18 column (Magic C18 AQ resin 3μm particle size/300Å pore size; Michrom, Leonberg, Germany).

    Techniques: Selection

    The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method (SIMAC, TiO 2 and IMAC) coupled to R3/C18 and MSA-LTQ ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.

    Journal: Journal of Clinical Bioinformatics

    Article Title: Discovering and validating unknown phospho-sites from p38 and HuR protein kinases in vitro by Phosphoproteomic and Bioinformatic tools

    doi: 10.1186/2043-9113-1-16

    Figure Lengend Snippet: The efficiency and reproducibility of the phosphopeptide purification and identification when using ~3 μg of protein kinases per each resin and/or phosphoenrichment method (SIMAC, TiO 2 and IMAC) coupled to R3/C18 and MSA-LTQ ion Trap mass spectrometer is illustrated . [A] Four triplicate experiments were carried out in order to identify the phosphopeptides. The phospho-site identifications were carried out from pooled and non-pooled assays (inter- and intra-assays) confirming a high reproducibility. The 6 phosphorylated peptides identified were isolated and validated in the four triplicate analyses, not only by Mascot (at least 4 continuously -y and -b ions matched)but also by manual inspection of all the spectra. SIMAC allowed the purification of 3 phosphorylated proteins: HuR RNA binding, p38 MAP Kinase and Trapped Ubiquitin-Like Protein Activation Complex, and 6 phosphorylated peptides related to those previously mentioned proteins. TiO 2 and IMAC allowed the isolation of 2 phoshorylated proteins: HuR RNA binding and p38 MAP Kinase, and 1 phosphopeptide related to the protein kinase HuR RNA binding. [B] SIMAC coupled to MSA allowed the identification of one more phosphopeptide compared to SIMAC coupled to DDNLMS3. Nevertheless, both strategies (SIMAC coupled to MSA and SIMAC coupled to DDNLMS3) allowed the identification of the same number of phosphorylated proteins (3). [C] and [D] Three phosphorylated proteins and six phosphopeptides were identified when using SIMAC coupled to MSA. From those three phosphoproteins identified, six phosphopeptides were identified: (a) TiO 2 coupled to MSA allowed the identification of two equal/same phosphorylated proteins and four equal/same phosphopeptides as SIMAC and (b) IMAC allowed the identification of one equal/same protein and two equal/same phosphopeptides. Thus, SIMAC is more efficient than the other tested resins for this study, while TiO 2 and IMAC corroborate the reproducibility of the phosphorylated proteins and phosphopeptides identified.

    Article Snippet: Each elute was then entered into a C18 reverse phase column (100 μm i.d., 10 cm long, 5 μm resin from Michrom Bioresources, Auburn, CA).

    Techniques: Purification, Mass Spectrometry, Isolation, RNA Binding Assay, Activation Assay

    Automation flow diagram and temperature control. The entire process is automated. A liquid handler mixes a protein solution with a deuterated buffer to initiate on-exchange, and adds a quench buffer after a programmed period of incubation. The quenched mixture is then loaded into the injector. Using an isocratic pump, the exchanged sample then flows from the injector through the protease column to a C18 trap. After a valve switch, a gradient is used to elute peptides from the trap via the C18 analytical column into the MS.

    Journal: Journal of Biomolecular Techniques : JBT

    Article Title: Rapid Analysis of Protein Structure and Dynamics by Hydrogen/Deuterium Exchange Mass Spectrometry

    doi:

    Figure Lengend Snippet: Automation flow diagram and temperature control. The entire process is automated. A liquid handler mixes a protein solution with a deuterated buffer to initiate on-exchange, and adds a quench buffer after a programmed period of incubation. The quenched mixture is then loaded into the injector. Using an isocratic pump, the exchanged sample then flows from the injector through the protease column to a C18 trap. After a valve switch, a gradient is used to elute peptides from the trap via the C18 analytical column into the MS.

    Article Snippet: Subsequently, the peptides loaded on C18 trap were eluted through C18 analytical column (Magic C18, 1.0 mm D × 50 mm, Michrom) with a linear gradient of 10% to 50% B over 30 min (solvent A was 0.05% trifluoroacetic acid in water, and B was 80% acetonitrile, 20% water, 0.01% trifluoroacetic acid).

    Techniques: Flow Cytometry, Incubation, Mass Spectrometry

    Plumbing for automated analysis of multiple peptide samples using the HPLC autosampler and divert valve of LCQ mass spectrometer. A: In the waste mode, flow split before the peptide trap was blocked at valve position 6, so that all sample and solvent flowed through the trap. Peptides were trapped and solvent diverted to waste. The mass detector was set to Off during peptide trapping. B: In the source mode, flow split before the trap was on and diverted most solvent to waste. Flow split after the trap was blocked at valve position 6 to allow 150 nL/min of solvent gradient (detailed in Materials and Methods) to flow through the peptide trap to elute peptides into C18 microcapillary column. Separated peptides were injected into the mass spectrometer for MS and MS/MS analysis. Backpressure was controlled with the length of peek tubing (0.0025″ ID) at valve position 4.

    Journal: Journal of Biomolecular Techniques : JBT

    Article Title: High-Throughput Analysis of Protein/Peptide Complexes by Immunoprecipitation and Automated LC-MS/MS

    doi:

    Figure Lengend Snippet: Plumbing for automated analysis of multiple peptide samples using the HPLC autosampler and divert valve of LCQ mass spectrometer. A: In the waste mode, flow split before the peptide trap was blocked at valve position 6, so that all sample and solvent flowed through the trap. Peptides were trapped and solvent diverted to waste. The mass detector was set to Off during peptide trapping. B: In the source mode, flow split before the trap was on and diverted most solvent to waste. Flow split after the trap was blocked at valve position 6 to allow 150 nL/min of solvent gradient (detailed in Materials and Methods) to flow through the peptide trap to elute peptides into C18 microcapillary column. Separated peptides were injected into the mass spectrometer for MS and MS/MS analysis. Backpressure was controlled with the length of peek tubing (0.0025″ ID) at valve position 4.

    Article Snippet: Our in-house packed C18 microcapillary column (75 μm × 12 cm packed with 5 μm, 300 Å Magic C18; Michrom BioResources, Auburn, CA) was tested for processing up to 40 samples.

    Techniques: High Performance Liquid Chromatography, Mass Spectrometry, Flow Cytometry, Injection