Structured Review

Waters Corporation c18 column
Histone preparation with Lys-propionylation, trypsin digestion, and N-terminal PIC-labeling. A , Sample preparation workflow. B , Relative ionization efficiencies H3 T3-R8 peptide in all modified forms. C , Recovery of H3 T3-R8 peptides following StageTip <t>C18</t> cleanup. All abundances are expressed relative to the unmodified peptide.
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1) Product Images from ""

Article Title:

Journal: Molecular & Cellular Proteomics : MCP

doi: 10.1074/mcp.O114.046573

Histone preparation with Lys-propionylation, trypsin digestion, and N-terminal PIC-labeling. A , Sample preparation workflow. B , Relative ionization efficiencies H3 T3-R8 peptide in all modified forms. C , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. All abundances are expressed relative to the unmodified peptide.
Figure Legend Snippet: Histone preparation with Lys-propionylation, trypsin digestion, and N-terminal PIC-labeling. A , Sample preparation workflow. B , Relative ionization efficiencies H3 T3-R8 peptide in all modified forms. C , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. All abundances are expressed relative to the unmodified peptide.

Techniques Used: Labeling, Sample Prep, Modification

Sources of discrepancy in H3K4 quantitation. A , Equimolar mixture of isotope-labeled, propionylated H3 T3-R8 peptide in eight modification states, injected in the milieu of endogenous histones from 293T cells. B , Time course of digestion releasing propionylated H3 T3-R8 from propionylated H3 A1-R17, where K4 is trimethylated. C , Relative ionization efficiencies of the propionylated H3 T3-R8 peptide in its various modified forms. D , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. In panels A , C , D , all abundances are expressed relative to the unmodified peptide.
Figure Legend Snippet: Sources of discrepancy in H3K4 quantitation. A , Equimolar mixture of isotope-labeled, propionylated H3 T3-R8 peptide in eight modification states, injected in the milieu of endogenous histones from 293T cells. B , Time course of digestion releasing propionylated H3 T3-R8 from propionylated H3 A1-R17, where K4 is trimethylated. C , Relative ionization efficiencies of the propionylated H3 T3-R8 peptide in its various modified forms. D , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. In panels A , C , D , all abundances are expressed relative to the unmodified peptide.

Techniques Used: Quantitation Assay, Labeling, Modification, Injection

Direct comparison of standard propionylation (Prop-x2) labeling and the hybrid (Prop-PIC) labeling method via LC-MS using a 1:1 mixture of labeled histone samples. A , Extracted ion chromatograms of the hydrophilic H3T3-R8 peptide (TK 4 QTAR) and its modified versions on C18 reverse-phase LC-MS. Retention times and relative abundances are increased by the hybrid labeling method. B , Quantitative comparison of the recoveries of each H3.1 histone tail peptide, where integrated peak areas for all modification states are combined. C , Quantitative comparison of the recoveries of the H3 T3-R8 peptide in its various modification states for the Prop-PIC versus Propx2 (integrated peak areas; n = 3, error bars are standard deviations).
Figure Legend Snippet: Direct comparison of standard propionylation (Prop-x2) labeling and the hybrid (Prop-PIC) labeling method via LC-MS using a 1:1 mixture of labeled histone samples. A , Extracted ion chromatograms of the hydrophilic H3T3-R8 peptide (TK 4 QTAR) and its modified versions on C18 reverse-phase LC-MS. Retention times and relative abundances are increased by the hybrid labeling method. B , Quantitative comparison of the recoveries of each H3.1 histone tail peptide, where integrated peak areas for all modification states are combined. C , Quantitative comparison of the recoveries of the H3 T3-R8 peptide in its various modification states for the Prop-PIC versus Propx2 (integrated peak areas; n = 3, error bars are standard deviations).

Techniques Used: Labeling, Liquid Chromatography with Mass Spectroscopy, Modification

2) Product Images from "Cooperative Interactions of Oligosaccharide and Peptide Moieties of a Glycopeptide Derived from IgE with Galectin-9 *"

Article Title: Cooperative Interactions of Oligosaccharide and Peptide Moieties of a Glycopeptide Derived from IgE with Galectin-9 *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M115.694448

RP-HPLC chromatograms of P23 digested with trypsin and P23-T11 digested with endoproteinase Glu-C. A and C , amino acid sequences of H-Lys13 ( A ) and H-Lys13-Try3 ( C ). Arrows , potential cleavage sites for trypsin ( A ) or endoproteinase Glu-C ( C ). H-Lys13-Try1 to - Try4 , predicted tryptic fragments of H-Lys13. H-Lys13-Try3-Glu1 and - Glu2 , predicted endoproteinase Glu-C fragments of H-Lys13-Try3. #, potential N -glycosylation sites. B and D , the trypsin digest of the P23 preparation (derived from 4.2 nmol of PE-TIB-141) ( B ) and the endoproteinase Glu-C digest of P23-T11 preparation (derived from 8.8 nmol of PE-TIB-141) ( D ) were analyzed on a C18 column. The column was developed with a linear gradient of 0–80% (v/v) acetonitrile in 0.1% (v/v) TFA.
Figure Legend Snippet: RP-HPLC chromatograms of P23 digested with trypsin and P23-T11 digested with endoproteinase Glu-C. A and C , amino acid sequences of H-Lys13 ( A ) and H-Lys13-Try3 ( C ). Arrows , potential cleavage sites for trypsin ( A ) or endoproteinase Glu-C ( C ). H-Lys13-Try1 to - Try4 , predicted tryptic fragments of H-Lys13. H-Lys13-Try3-Glu1 and - Glu2 , predicted endoproteinase Glu-C fragments of H-Lys13-Try3. #, potential N -glycosylation sites. B and D , the trypsin digest of the P23 preparation (derived from 4.2 nmol of PE-TIB-141) ( B ) and the endoproteinase Glu-C digest of P23-T11 preparation (derived from 8.8 nmol of PE-TIB-141) ( D ) were analyzed on a C18 column. The column was developed with a linear gradient of 0–80% (v/v) acetonitrile in 0.1% (v/v) TFA.

Techniques Used: High Performance Liquid Chromatography, Derivative Assay

3) Product Images from "Studies on the Metabolism and Biological Activity of the Epimers of Sulindac"

Article Title: Studies on the Metabolism and Biological Activity of the Epimers of Sulindac

Journal: Drug Metabolism and Disposition

doi: 10.1124/dmd.110.037663

Separation of sulindac and its metabolites from the plasma of rats 4 h after intraperitoneal injection of the R - and S -epimers of sulindac (see Materials and Methods ). Plasma samples were run on a C18 column and separated as described under Materials
Figure Legend Snippet: Separation of sulindac and its metabolites from the plasma of rats 4 h after intraperitoneal injection of the R - and S -epimers of sulindac (see Materials and Methods ). Plasma samples were run on a C18 column and separated as described under Materials

Techniques Used: Injection

4) Product Images from "Identification of neuromedin U precursor-related peptide and its possible role in the regulation of prolactin release"

Article Title: Identification of neuromedin U precursor-related peptide and its possible role in the regulation of prolactin release

Journal: Scientific Reports

doi: 10.1038/s41598-017-10319-9

Purification of NURP from rat brain extracts. ( a ) RP-HPLC on a μ-Bondasphere C18 column of the materials eluted from the immunoaffinity column for rat NURP. The peaks containing NURP36 (B1) and NURP33 (B2) are indicated by arrows. ( b ) Final purification of rat NURP36 (upper; B1) and rat NURP33 (lower; B2) using a Chemcosorb 3ODS-H column. Purified peptides are indicated by arrows.
Figure Legend Snippet: Purification of NURP from rat brain extracts. ( a ) RP-HPLC on a μ-Bondasphere C18 column of the materials eluted from the immunoaffinity column for rat NURP. The peaks containing NURP36 (B1) and NURP33 (B2) are indicated by arrows. ( b ) Final purification of rat NURP36 (upper; B1) and rat NURP33 (lower; B2) using a Chemcosorb 3ODS-H column. Purified peptides are indicated by arrows.

Techniques Used: Purification, High Performance Liquid Chromatography

5) Product Images from "Utilization of Metabolomics to Identify Serum Biomarkers for Hepatocellular Carcinoma in Patients with Liver Cirrhosis"

Article Title: Utilization of Metabolomics to Identify Serum Biomarkers for Hepatocellular Carcinoma in Patients with Liver Cirrhosis

Journal: Analytica chimica acta

doi: 10.1016/j.aca.2012.07.013

Detection of GCA in patient sample and its IS (1pmol on C18 column) by UPLC-SRM-MS.
Figure Legend Snippet: Detection of GCA in patient sample and its IS (1pmol on C18 column) by UPLC-SRM-MS.

Techniques Used: Mass Spectrometry

6) Product Images from "Separation of Five Flavonoids from Aerial Parts of Salvia Miltiorrhiza Bunge Using HSCCC and Their Antioxidant Activities"

Article Title: Separation of Five Flavonoids from Aerial Parts of Salvia Miltiorrhiza Bunge Using HSCCC and Their Antioxidant Activities

Journal: Molecules

doi: 10.3390/molecules24193448

( A ) HPLC analysis of the crude sample; ( B – F ) HPLC chromatograms and UV spectra of compounds 1 – 5 . Column: C18 column (Waters symmetry, 5 μm, 4.6 mm × 250 mm, i.d.); mobile phase: acetonitrile ( A ) 0.1% aqueous solution of formic acid (B) (0–15 min, 21:79, v / v ); flow rate: 1.0 mL/min; detection wavelength: 254 nm; column temperature: 25 °C.
Figure Legend Snippet: ( A ) HPLC analysis of the crude sample; ( B – F ) HPLC chromatograms and UV spectra of compounds 1 – 5 . Column: C18 column (Waters symmetry, 5 μm, 4.6 mm × 250 mm, i.d.); mobile phase: acetonitrile ( A ) 0.1% aqueous solution of formic acid (B) (0–15 min, 21:79, v / v ); flow rate: 1.0 mL/min; detection wavelength: 254 nm; column temperature: 25 °C.

Techniques Used: High Performance Liquid Chromatography, Flow Cytometry

7) Product Images from "Functionalized Polymeric Materials with Bio-Derived Antimicrobial Peptides for “Active” Packaging"

Article Title: Functionalized Polymeric Materials with Bio-Derived Antimicrobial Peptides for “Active” Packaging

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms20030601

Release analysis of 1018K6 from functionalized PET performed by reverse-phase HPLC chromatography on a C18 column after 24 h incubation at 4 °C in mozzarella brine ( a ) or pure water ( b ). After incubation, the solutions were recovered and injected on C18. The solution in contact with 1018K6-PET at time 0 ( t = 0) and 1018K6 peptide (50 μM) were used as controls.
Figure Legend Snippet: Release analysis of 1018K6 from functionalized PET performed by reverse-phase HPLC chromatography on a C18 column after 24 h incubation at 4 °C in mozzarella brine ( a ) or pure water ( b ). After incubation, the solutions were recovered and injected on C18. The solution in contact with 1018K6-PET at time 0 ( t = 0) and 1018K6 peptide (50 μM) were used as controls.

Techniques Used: Positron Emission Tomography, High Performance Liquid Chromatography, Chromatography, Incubation, Injection

Immobilization yield (%) of 1018K6 on PET surface determined by reverse-phase HPLC chromatography on a C18 column after the coulping reaction (24 h). Pre-activated PET surfaces by plasma were incubated for 24 h with 1018K6 (50 µM) in PBS pH 7.0. The solutions recovered after incubation were further analysed. The peptide solution placed in contact with the pre-activated surface at time 0 ( t = 0) was used as control. The chromatograms are representative of three independent experiments. Insert : Calibration curve of the C18 column obtained using different 1018K6 concentrations.
Figure Legend Snippet: Immobilization yield (%) of 1018K6 on PET surface determined by reverse-phase HPLC chromatography on a C18 column after the coulping reaction (24 h). Pre-activated PET surfaces by plasma were incubated for 24 h with 1018K6 (50 µM) in PBS pH 7.0. The solutions recovered after incubation were further analysed. The peptide solution placed in contact with the pre-activated surface at time 0 ( t = 0) was used as control. The chromatograms are representative of three independent experiments. Insert : Calibration curve of the C18 column obtained using different 1018K6 concentrations.

Techniques Used: Positron Emission Tomography, High Performance Liquid Chromatography, Chromatography, Incubation

8) Product Images from "Native Pyroglutamation of Huwentoxin-IV: A Post-Translational Modification that Increases the Trapping Ability to the Sodium Channel"

Article Title: Native Pyroglutamation of Huwentoxin-IV: A Post-Translational Modification that Increases the Trapping Ability to the Sodium Channel

Journal: PLoS ONE

doi: 10.1371/journal.pone.0065984

HPLC purification of mHWTX-IV. The peaks marked by * contain mHWTX-IV. (A) Elution profile of Ornithoctonus huwena Wang venom by ion-exchange HPLC. (B) Isolation of mHWTX-IV by RP-HPLC on a C18 column in a gradient of 10–50% acetonitrile over 50 min. (C) Further purification of mHWTX-IV by a repetitive RP-HPLC with a gradient of 28–40% acetonitrile over 30 min.
Figure Legend Snippet: HPLC purification of mHWTX-IV. The peaks marked by * contain mHWTX-IV. (A) Elution profile of Ornithoctonus huwena Wang venom by ion-exchange HPLC. (B) Isolation of mHWTX-IV by RP-HPLC on a C18 column in a gradient of 10–50% acetonitrile over 50 min. (C) Further purification of mHWTX-IV by a repetitive RP-HPLC with a gradient of 28–40% acetonitrile over 30 min.

Techniques Used: High Performance Liquid Chromatography, Purification, Isolation

9) Product Images from "Detection of 7-Dehydrocholesterol and Vitamin D3 Derivatives in Honey"

Article Title: Detection of 7-Dehydrocholesterol and Vitamin D3 Derivatives in Honey

Journal: Molecules

doi: 10.3390/molecules25112583

Detection of D3, 7DHC and L3 in honey. Whole honey extract was analyzed directly using a Zorbax Eclipse Plus C18 column connected to a Xevo G2 XS equipped with an ACQUITY UPLC I-Class System (Waters, Milford, MA) using a methanol gradient. The extracted ion chromatogram (EIC) was obtained using m/z = 407.329 [M + Na] + . Arrow 1, RT of D3 standard; arrow 2, RT of 7DHC standard; arrow 3, RT of L3 standard.
Figure Legend Snippet: Detection of D3, 7DHC and L3 in honey. Whole honey extract was analyzed directly using a Zorbax Eclipse Plus C18 column connected to a Xevo G2 XS equipped with an ACQUITY UPLC I-Class System (Waters, Milford, MA) using a methanol gradient. The extracted ion chromatogram (EIC) was obtained using m/z = 407.329 [M + Na] + . Arrow 1, RT of D3 standard; arrow 2, RT of 7DHC standard; arrow 3, RT of L3 standard.

Techniques Used:

Detection of 1,25(OH) 2 D3 in honey. ( A ) Whole extract was analyzed directly using LC-MS with a Zorbax Eclipse Plus C18 column with a methanol gradient. The EIC was obtained using m/z = 399.326 [M + H − H 2 O] + . ( B ) The sample was pre-purified using a C18 column, then analyzed using LC-MS with a Zorbax Eclipse Plus C18 column with an acetonitrile gradient. The EIC was obtained using m/z = 399.326 [M + H − H 2 O] + .
Figure Legend Snippet: Detection of 1,25(OH) 2 D3 in honey. ( A ) Whole extract was analyzed directly using LC-MS with a Zorbax Eclipse Plus C18 column with a methanol gradient. The EIC was obtained using m/z = 399.326 [M + H − H 2 O] + . ( B ) The sample was pre-purified using a C18 column, then analyzed using LC-MS with a Zorbax Eclipse Plus C18 column with an acetonitrile gradient. The EIC was obtained using m/z = 399.326 [M + H − H 2 O] + .

Techniques Used: Liquid Chromatography with Mass Spectroscopy, Purification

Detection of 25(OH)D3 in honey. After a pre-purification step using a C18 column with an acetonitrile gradient, the fraction was analyzed using LC-MS with a Zorbax Eclipse Plus C18 column with an acetonitrile gradient. The EIC was obtained using m/z = 383.331 [M + H − H 2 O] + .
Figure Legend Snippet: Detection of 25(OH)D3 in honey. After a pre-purification step using a C18 column with an acetonitrile gradient, the fraction was analyzed using LC-MS with a Zorbax Eclipse Plus C18 column with an acetonitrile gradient. The EIC was obtained using m/z = 383.331 [M + H − H 2 O] + .

Techniques Used: Purification, Liquid Chromatography with Mass Spectroscopy

Detection of 1,20(OH) 2 D3 in honey. ( A ) The peak corresponding in RT to standard was collected from commercially available honey using an Atlantis C18 column using a methanol gradient, then analyzed using LC-MS with an ACQUITY UPLC BEH C18 column with a methanol gradient. The EIC was obtained using m/z = 439.319 [M + Na] + . ( B ) The local honey sample was pre-purified using a C18 column, then analyzed using LC-MS with a Zorbax Eclipse Plus C18 column with an acetonitrile gradient. The EIC was obtained using m/z = 399.326 [M + H − H 2 O] + .
Figure Legend Snippet: Detection of 1,20(OH) 2 D3 in honey. ( A ) The peak corresponding in RT to standard was collected from commercially available honey using an Atlantis C18 column using a methanol gradient, then analyzed using LC-MS with an ACQUITY UPLC BEH C18 column with a methanol gradient. The EIC was obtained using m/z = 439.319 [M + Na] + . ( B ) The local honey sample was pre-purified using a C18 column, then analyzed using LC-MS with a Zorbax Eclipse Plus C18 column with an acetonitrile gradient. The EIC was obtained using m/z = 399.326 [M + H − H 2 O] + .

Techniques Used: Liquid Chromatography with Mass Spectroscopy, Purification

Detection of 20(OH)D3 and 20(OH)-7DHC in honey. ( A ) After a pre-purification step using an Atlantis C18 column with a methanol gradient, then analyzed using LC-MS with an ACQUITY UPLC BEH C18 column with a methanol gradient. The EIC was obtained using m/z = 423.324 [M + Na] + . ( B ) After extraction of commercially sourced honey, the sample was directly analyzed using LC-MS with a Pursuit 200Å PFP column with a methanol gradient. The EIC was obtained using m/z = 383.331 [M + H − H 2 O] + .
Figure Legend Snippet: Detection of 20(OH)D3 and 20(OH)-7DHC in honey. ( A ) After a pre-purification step using an Atlantis C18 column with a methanol gradient, then analyzed using LC-MS with an ACQUITY UPLC BEH C18 column with a methanol gradient. The EIC was obtained using m/z = 423.324 [M + Na] + . ( B ) After extraction of commercially sourced honey, the sample was directly analyzed using LC-MS with a Pursuit 200Å PFP column with a methanol gradient. The EIC was obtained using m/z = 383.331 [M + H − H 2 O] + .

Techniques Used: Purification, Liquid Chromatography with Mass Spectroscopy

10) Product Images from "PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry"

Article Title: PhTX-II a Basic Myotoxic Phospholipase A2 from Porthidium hyoprora Snake Venom, Pharmacological Characterization and Amino Acid Sequence by Mass Spectrometry

Journal: Toxins

doi: 10.3390/toxins6113077

Chromatographic and electrophoretic profile of Porthidium hyoprora venom fractioning on a µ-Bondapack C18 column, monitoring elution profile at 280 nm. Emphasized in black is fraction 11 ( * ) characterized as PhTX-II PLA 2 ; Insert: Electrophoretic profile in Tricine SDS-PAGE (1) Molecular mass markers; (2) PhTX-II not reduced; (3) PhTX-II reduced with DTT (1 M).
Figure Legend Snippet: Chromatographic and electrophoretic profile of Porthidium hyoprora venom fractioning on a µ-Bondapack C18 column, monitoring elution profile at 280 nm. Emphasized in black is fraction 11 ( * ) characterized as PhTX-II PLA 2 ; Insert: Electrophoretic profile in Tricine SDS-PAGE (1) Molecular mass markers; (2) PhTX-II not reduced; (3) PhTX-II reduced with DTT (1 M).

Techniques Used: Proximity Ligation Assay, SDS Page

11) Product Images from "One-pot multi-enzyme (OPME) chemoenzymatic synthesis of sialyl-Tn-MUC1 and sialyl-T-MUC1 glycopeptides containing natural or non-natural sialic acid"

Article Title: One-pot multi-enzyme (OPME) chemoenzymatic synthesis of sialyl-Tn-MUC1 and sialyl-T-MUC1 glycopeptides containing natural or non-natural sialic acid

Journal: Bioorganic & medicinal chemistry

doi: 10.1016/j.bmc.2013.02.040

Strategies for optimizing synthetic yields of the one-pot multienzyme (OPME) sialylation reactions by adding excess amount of CTP and removal of CMP byproduct by flash C18 cartridge purification (OPME synthesis of STn-MUC glycopeptide is used as an example).
Figure Legend Snippet: Strategies for optimizing synthetic yields of the one-pot multienzyme (OPME) sialylation reactions by adding excess amount of CTP and removal of CMP byproduct by flash C18 cartridge purification (OPME synthesis of STn-MUC glycopeptide is used as an example).

Techniques Used: Purification

12) Product Images from "Lecithin Retinol Acyltransferase Is a Founder Member of a Novel Family of Enzymes †"

Article Title: Lecithin Retinol Acyltransferase Is a Founder Member of a Novel Family of Enzymes †

Journal: Biochemistry

doi: 10.1021/bi035370p

tLRAT labeling by affinity labeling reagents. (A) HPLC chromatogram of [11,12- 3 H 2 ]RCA ( 2 ) labeled tLRAT peptide. RPHPLC was performed on a microcapillary C18 column (Vydac 218TP52). The peptides were eluted with a linear gradient from 0 to 70% acetonitrile with 0.1% TFA. Fractions were collected every minute (50 µL), and radioactivity was monitored by scintillation counting (Beckman LS6500) using Ultima Gold scintillation cocktail. (B) tLRAT labeling by alkali-cleavable affinity reagent BRCA ( 3 ). tLRAT was visualized by Coomassie blue staining, Western blot by anti-LRAT antibody/anti-rabbit Ig-HRP/ECL, and biotin blot by avidin-HRP/ ECL. The 40 kDa band represents the tLRAT homodimer. (C) MALDI TOF analysis of the BACMK ( 4 ) labeled tLRAT peptide. One peptide (MW = 1315) represents NNCEHF (763) + BACMK - Cl - Boc (552).
Figure Legend Snippet: tLRAT labeling by affinity labeling reagents. (A) HPLC chromatogram of [11,12- 3 H 2 ]RCA ( 2 ) labeled tLRAT peptide. RPHPLC was performed on a microcapillary C18 column (Vydac 218TP52). The peptides were eluted with a linear gradient from 0 to 70% acetonitrile with 0.1% TFA. Fractions were collected every minute (50 µL), and radioactivity was monitored by scintillation counting (Beckman LS6500) using Ultima Gold scintillation cocktail. (B) tLRAT labeling by alkali-cleavable affinity reagent BRCA ( 3 ). tLRAT was visualized by Coomassie blue staining, Western blot by anti-LRAT antibody/anti-rabbit Ig-HRP/ECL, and biotin blot by avidin-HRP/ ECL. The 40 kDa band represents the tLRAT homodimer. (C) MALDI TOF analysis of the BACMK ( 4 ) labeled tLRAT peptide. One peptide (MW = 1315) represents NNCEHF (763) + BACMK - Cl - Boc (552).

Techniques Used: Labeling, High Performance Liquid Chromatography, Radioactivity, Staining, Western Blot, Avidin-Biotin Assay

13) Product Images from "Development, characterization and comparisons of targeted and non-targeted metabolomics methods"

Article Title: Development, characterization and comparisons of targeted and non-targeted metabolomics methods

Journal: PLoS ONE

doi: 10.1371/journal.pone.0207082

Targeted vs non-targeted precision in NIST SRM 1950. Features from Orbi HILIC and Orbi C18 , selected manually or using the ‘lipidFrag’ function in our R-package, compared to features measured with QqQ HILIC and QqQ FI . Isomers or lipids from the low resolution QqQFI-method show up as duplicates in the list of compounds in the figure.
Figure Legend Snippet: Targeted vs non-targeted precision in NIST SRM 1950. Features from Orbi HILIC and Orbi C18 , selected manually or using the ‘lipidFrag’ function in our R-package, compared to features measured with QqQ HILIC and QqQ FI . Isomers or lipids from the low resolution QqQFI-method show up as duplicates in the list of compounds in the figure.

Techniques Used: Hydrophilic Interaction Liquid Chromatography

14) Product Images from "Pigment Production on L-Tryptophan Medium by Cryptococcus gattii and Cryptococcus neoformans"

Article Title: Pigment Production on L-Tryptophan Medium by Cryptococcus gattii and Cryptococcus neoformans

Journal: PLoS ONE

doi: 10.1371/journal.pone.0091901

TLC of the pink extracellular pigment. The TLC results of the C. neoformans concentrated supernatant under visible light, 254 nm, and 365 nm (Section A). The pink pigment separates into a major band (top) and a minor band (lower) which is located at the top of the tryptophan band (Section A). C 18 Sep-Pak column supernatant separation of fluorescent compounds which were then detected on TLC. The fluorescent compounds including tryptophan (blue fluorescence) were eluted with 20% methanol (section B). Multiple 5 ml 20% methanol fraction were collected. After the 8 th tube washing with 20% methanol fluorescent compounds were no longer detected in the fractions. The pink pigment was then eluted off the C18 Sep-Pak column with 40% to 50% methanol (section C). The eluted pink pigment formed two bands.
Figure Legend Snippet: TLC of the pink extracellular pigment. The TLC results of the C. neoformans concentrated supernatant under visible light, 254 nm, and 365 nm (Section A). The pink pigment separates into a major band (top) and a minor band (lower) which is located at the top of the tryptophan band (Section A). C 18 Sep-Pak column supernatant separation of fluorescent compounds which were then detected on TLC. The fluorescent compounds including tryptophan (blue fluorescence) were eluted with 20% methanol (section B). Multiple 5 ml 20% methanol fraction were collected. After the 8 th tube washing with 20% methanol fluorescent compounds were no longer detected in the fractions. The pink pigment was then eluted off the C18 Sep-Pak column with 40% to 50% methanol (section C). The eluted pink pigment formed two bands.

Techniques Used: Thin Layer Chromatography, Fluorescence

15) Product Images from "Estimation of angiotensin peptides in biological samples by LC/MS method"

Article Title: Estimation of angiotensin peptides in biological samples by LC/MS method

Journal: Analytical methods : advancing methods and applications

doi: 10.1039/C3AY41305E

Calibration curves, (A) Ang-(1-7) standard, (B) Ang II standard, showing dynamic range, linear regression, LOD and LOQ from peak area of C18-UPLC-ESI/MS.
Figure Legend Snippet: Calibration curves, (A) Ang-(1-7) standard, (B) Ang II standard, showing dynamic range, linear regression, LOD and LOQ from peak area of C18-UPLC-ESI/MS.

Techniques Used: Mass Spectrometry

16) Product Images from "Utilization of Metabolomics to Identify Serum Biomarkers for Hepatocellular Carcinoma in Patients with Liver Cirrhosis"

Article Title: Utilization of Metabolomics to Identify Serum Biomarkers for Hepatocellular Carcinoma in Patients with Liver Cirrhosis

Journal: Analytica chimica acta

doi: 10.1016/j.aca.2012.07.013

Detection of GCA in patient sample and its IS (1pmol on C18 column) by UPLC-SRM-MS.
Figure Legend Snippet: Detection of GCA in patient sample and its IS (1pmol on C18 column) by UPLC-SRM-MS.

Techniques Used: Mass Spectrometry

17) Product Images from "Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *"

Article Title: Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *

Journal: Molecular & Cellular Proteomics : MCP

doi: 10.1074/mcp.M112.023259

Extracted ion chromatogram of multiply sialylated and fucosylated glycoforms of the T3 peptide isolated from pooled plasma of HCC patients and separated by nano-reverse phase C18 chromatography after HILIC enrichment. The mass difference between the isoforms
Figure Legend Snippet: Extracted ion chromatogram of multiply sialylated and fucosylated glycoforms of the T3 peptide isolated from pooled plasma of HCC patients and separated by nano-reverse phase C18 chromatography after HILIC enrichment. The mass difference between the isoforms

Techniques Used: Isolation, Chromatography, Hydrophilic Interaction Liquid Chromatography

18) Product Images from "Isolation of the bioactive peptides CCHamide-1 and CCHamide-2 from Drosophila and their putative role in appetite regulation as ligands for G protein-coupled receptors"

Article Title: Isolation of the bioactive peptides CCHamide-1 and CCHamide-2 from Drosophila and their putative role in appetite regulation as ligands for G protein-coupled receptors

Journal: Frontiers in Endocrinology

doi: 10.3389/fendo.2012.00177

Purification of CCHamide-2 from fly extracts . Black bars indicate changes of [Ca 2 + ] i fluorescent signal in CHO-CG14593 cells. (A) G-50 gel filtration of the SP-III fraction of fly extracts. The active fraction was subjected to one step of CM-ion-exchange HPLC and three steps of RP-HPLC. (B–D) Final purification of the active fraction by RP-HPLC. (E) Nucleotide sequence and deduced amino acid sequence of CCHamide-2 cDNA. CCHamide-2 cDNA encodes a 136-residue peptides. The asterisk indicates a glycine residue that serves as an amide donor for C-terminal amidation. The CCHamide-2 sequence is underlined as (4). The other long-form of CCHamide-2 is translated from (2) or (3). (F) Chromatographic comparison by RP-HPLC of natural CCHamide-2 and synthetic CCHamide-2. Black bars (P2, P3) indicate the changes of [Ca 2 + ] i fluorescence signal in CHO-CG14593 cells. Each peptide was applied to a Symmetry C18 column with a linear gradient elution for 80 min. P2 and P3 represent active fractions containing natural CCHamide-2. (b) Synthetic long-form of CCHamide-2. (c) Synthetic CCHamide-2. (G) Active fractions of each chromatography and the amino acid sequence of CCHamide-2.
Figure Legend Snippet: Purification of CCHamide-2 from fly extracts . Black bars indicate changes of [Ca 2 + ] i fluorescent signal in CHO-CG14593 cells. (A) G-50 gel filtration of the SP-III fraction of fly extracts. The active fraction was subjected to one step of CM-ion-exchange HPLC and three steps of RP-HPLC. (B–D) Final purification of the active fraction by RP-HPLC. (E) Nucleotide sequence and deduced amino acid sequence of CCHamide-2 cDNA. CCHamide-2 cDNA encodes a 136-residue peptides. The asterisk indicates a glycine residue that serves as an amide donor for C-terminal amidation. The CCHamide-2 sequence is underlined as (4). The other long-form of CCHamide-2 is translated from (2) or (3). (F) Chromatographic comparison by RP-HPLC of natural CCHamide-2 and synthetic CCHamide-2. Black bars (P2, P3) indicate the changes of [Ca 2 + ] i fluorescence signal in CHO-CG14593 cells. Each peptide was applied to a Symmetry C18 column with a linear gradient elution for 80 min. P2 and P3 represent active fractions containing natural CCHamide-2. (b) Synthetic long-form of CCHamide-2. (c) Synthetic CCHamide-2. (G) Active fractions of each chromatography and the amino acid sequence of CCHamide-2.

Techniques Used: Purification, Filtration, High Performance Liquid Chromatography, Sequencing, Fluorescence, Chromatography

Purification of CCHamide-1 from fly extracts . Black bars indicate changes of [Ca 2 + ] i fluorescence signal in CHO-CG30106 cells. (A) G-50 gel filtration of the SP-III fraction of fly extracts. The active fraction was subjected to one step of CM-ion-exchange HPLC and three steps of RP-HPLC. (B) Final purification of the active fraction by RP-HPLC. (C) Nucleotide sequence and deduced amino acid sequence of CCHamide-1 cDNA. CCHamide-1 cDNA encode 182-residue peptides. The asterisk indicates a glycine residue that serves as an amide donor for C-terminal amidation. The CCHamide-1 sequence is underlined as (1). (D) Chromatographic comparison by RP-HPLC of natural CCHamide-1 and synthetic CCHamide-1. Black bar (P1) indicates the changes of [Ca 2 + ] i fluorescence signal in CHO-CG30106 cells. Each peptide was applied to a Symmetry C18 column (3.9 mm × 150 mm, Waters, MA, USA) with a 10–60% ACN/0.1% trifluoroacetic acid (TFA) linear gradient at a flow rate of 1 ml/min for 80 min. P1 represent active fraction containing natural CCHamide-1. (a) Synthetic CCHamide-1. (E) Active fractions of each chromatography and the amino acid sequence of CCHamide-1.
Figure Legend Snippet: Purification of CCHamide-1 from fly extracts . Black bars indicate changes of [Ca 2 + ] i fluorescence signal in CHO-CG30106 cells. (A) G-50 gel filtration of the SP-III fraction of fly extracts. The active fraction was subjected to one step of CM-ion-exchange HPLC and three steps of RP-HPLC. (B) Final purification of the active fraction by RP-HPLC. (C) Nucleotide sequence and deduced amino acid sequence of CCHamide-1 cDNA. CCHamide-1 cDNA encode 182-residue peptides. The asterisk indicates a glycine residue that serves as an amide donor for C-terminal amidation. The CCHamide-1 sequence is underlined as (1). (D) Chromatographic comparison by RP-HPLC of natural CCHamide-1 and synthetic CCHamide-1. Black bar (P1) indicates the changes of [Ca 2 + ] i fluorescence signal in CHO-CG30106 cells. Each peptide was applied to a Symmetry C18 column (3.9 mm × 150 mm, Waters, MA, USA) with a 10–60% ACN/0.1% trifluoroacetic acid (TFA) linear gradient at a flow rate of 1 ml/min for 80 min. P1 represent active fraction containing natural CCHamide-1. (a) Synthetic CCHamide-1. (E) Active fractions of each chromatography and the amino acid sequence of CCHamide-1.

Techniques Used: Purification, Fluorescence, Filtration, High Performance Liquid Chromatography, Sequencing, Flow Cytometry, Chromatography

19) Product Images from "Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae)"

Article Title: Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae)

Journal: Toxins

doi: 10.3390/toxins12080508

Coelution profile of native and synthetic cdg14a. The HPLC runs were carried out using an analytical C18 column and a gradient of 0.15% solvent B/min. ( A ) Native cdg14a isolated from Clavus davidgilmouri venom. ( B ) Synthetic cdg14a. ( C ) Mixture of the native and synthetic samples (1:2) of cdg14a.
Figure Legend Snippet: Coelution profile of native and synthetic cdg14a. The HPLC runs were carried out using an analytical C18 column and a gradient of 0.15% solvent B/min. ( A ) Native cdg14a isolated from Clavus davidgilmouri venom. ( B ) Synthetic cdg14a. ( C ) Mixture of the native and synthetic samples (1:2) of cdg14a.

Techniques Used: High Performance Liquid Chromatography, Isolation

Chemical synthesis and folding of cdg14a. ( A ) HPLC chromatogram of a crude linear cdg14a eluted on an analytical C18 column using a gradient ranging from 5% to 65% solvent B in 30 min with 1 mL/min flow rate. ( B ) HPLC chromatogram of a crude linear cdg14a modified with 2-aminoethyl methanethiosulfonate hydrobromide (MTSEA) (HPLC conditions are the same as in panel A). ( C ) oxidative folding of cdg14a monitored by HPLC, using a C18 column and a gradient ranging from 15% to 45% solvent B, with a flow rate 1 mL/min. Single asterisk denotes the native-like fold of cdg14a. ( D ) zoom-in on 4 h oxidative folding time point (black HPLC trace) with all possible folding isomers identified at 220 nm. The red trace represents the native folding isomer with the globular-like connectivity Cys3-Cys15, Cys9-Cys20; green trace represents ribbon-like folding isomer with the Cys3-Cys20, Cys9-Cys15 connectivity; blue trace represents the fast folding product with the bead-like connectivity Cys3-Cys9, Cys15-Cys20. The traces were collected using the same gradient as described for panel ( C ).
Figure Legend Snippet: Chemical synthesis and folding of cdg14a. ( A ) HPLC chromatogram of a crude linear cdg14a eluted on an analytical C18 column using a gradient ranging from 5% to 65% solvent B in 30 min with 1 mL/min flow rate. ( B ) HPLC chromatogram of a crude linear cdg14a modified with 2-aminoethyl methanethiosulfonate hydrobromide (MTSEA) (HPLC conditions are the same as in panel A). ( C ) oxidative folding of cdg14a monitored by HPLC, using a C18 column and a gradient ranging from 15% to 45% solvent B, with a flow rate 1 mL/min. Single asterisk denotes the native-like fold of cdg14a. ( D ) zoom-in on 4 h oxidative folding time point (black HPLC trace) with all possible folding isomers identified at 220 nm. The red trace represents the native folding isomer with the globular-like connectivity Cys3-Cys15, Cys9-Cys20; green trace represents ribbon-like folding isomer with the Cys3-Cys20, Cys9-Cys15 connectivity; blue trace represents the fast folding product with the bead-like connectivity Cys3-Cys9, Cys15-Cys20. The traces were collected using the same gradient as described for panel ( C ).

Techniques Used: High Performance Liquid Chromatography, Modification

Purification of cdg14a by high-performance liquid chromatography (HPLC) using C18 semi-preparative and analytical columns. The elution profiles show two different wavelengths used: 220 nm (black) and 280 nm (grey), with the elution gradient indicated by a blue line. ( A ) Chromatogram of the crude venom extract using a C18 semi-preparative column with linear gradient ranging from 6% to 60% solvent B (90% acetonitrile with 0.1% trifluoroacetic acid) at 0.9% solvent B/min, followed by 60% to 100% at 1.3% solvent B/min. The peak of the bioactive fraction is indicated by an arrow. ( B ) Chromatogram of the bioactive fraction reinjected in the HPLC using a C18 analytical column run at a shallower linear gradient ranging from 23% to 27% solvent B at 0.15% solvent B/min. The peak of the subfraction containing the bioactive peptide cdg14a is indicated by an arrow. ( C ) Chromatogram of the purified peptide cdg14a, showing a single, symmetrical peak.
Figure Legend Snippet: Purification of cdg14a by high-performance liquid chromatography (HPLC) using C18 semi-preparative and analytical columns. The elution profiles show two different wavelengths used: 220 nm (black) and 280 nm (grey), with the elution gradient indicated by a blue line. ( A ) Chromatogram of the crude venom extract using a C18 semi-preparative column with linear gradient ranging from 6% to 60% solvent B (90% acetonitrile with 0.1% trifluoroacetic acid) at 0.9% solvent B/min, followed by 60% to 100% at 1.3% solvent B/min. The peak of the bioactive fraction is indicated by an arrow. ( B ) Chromatogram of the bioactive fraction reinjected in the HPLC using a C18 analytical column run at a shallower linear gradient ranging from 23% to 27% solvent B at 0.15% solvent B/min. The peak of the subfraction containing the bioactive peptide cdg14a is indicated by an arrow. ( C ) Chromatogram of the purified peptide cdg14a, showing a single, symmetrical peak.

Techniques Used: Purification, High Performance Liquid Chromatography

20) Product Images from "Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae)"

Article Title: Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae)

Journal: Toxins

doi: 10.3390/toxins12080508

Coelution profile of native and synthetic cdg14a. The HPLC runs were carried out using an analytical C18 column and a gradient of 0.15% solvent B/min. ( A ) Native cdg14a isolated from Clavus davidgilmouri venom. ( B ) Synthetic cdg14a. ( C ) Mixture of the native and synthetic samples (1:2) of cdg14a.
Figure Legend Snippet: Coelution profile of native and synthetic cdg14a. The HPLC runs were carried out using an analytical C18 column and a gradient of 0.15% solvent B/min. ( A ) Native cdg14a isolated from Clavus davidgilmouri venom. ( B ) Synthetic cdg14a. ( C ) Mixture of the native and synthetic samples (1:2) of cdg14a.

Techniques Used: High Performance Liquid Chromatography, Isolation

Chemical synthesis and folding of cdg14a. ( A ) HPLC chromatogram of a crude linear cdg14a eluted on an analytical C18 column using a gradient ranging from 5% to 65% solvent B in 30 min with 1 mL/min flow rate. ( B ) HPLC chromatogram of a crude linear cdg14a modified with 2-aminoethyl methanethiosulfonate hydrobromide (MTSEA) (HPLC conditions are the same as in panel A). ( C ) oxidative folding of cdg14a monitored by HPLC, using a C18 column and a gradient ranging from 15% to 45% solvent B, with a flow rate 1 mL/min. Single asterisk denotes the native-like fold of cdg14a. ( D ) zoom-in on 4 h oxidative folding time point (black HPLC trace) with all possible folding isomers identified at 220 nm. The red trace represents the native folding isomer with the globular-like connectivity Cys3-Cys15, Cys9-Cys20; green trace represents ribbon-like folding isomer with the Cys3-Cys20, Cys9-Cys15 connectivity; blue trace represents the fast folding product with the bead-like connectivity Cys3-Cys9, Cys15-Cys20. The traces were collected using the same gradient as described for panel ( C ).
Figure Legend Snippet: Chemical synthesis and folding of cdg14a. ( A ) HPLC chromatogram of a crude linear cdg14a eluted on an analytical C18 column using a gradient ranging from 5% to 65% solvent B in 30 min with 1 mL/min flow rate. ( B ) HPLC chromatogram of a crude linear cdg14a modified with 2-aminoethyl methanethiosulfonate hydrobromide (MTSEA) (HPLC conditions are the same as in panel A). ( C ) oxidative folding of cdg14a monitored by HPLC, using a C18 column and a gradient ranging from 15% to 45% solvent B, with a flow rate 1 mL/min. Single asterisk denotes the native-like fold of cdg14a. ( D ) zoom-in on 4 h oxidative folding time point (black HPLC trace) with all possible folding isomers identified at 220 nm. The red trace represents the native folding isomer with the globular-like connectivity Cys3-Cys15, Cys9-Cys20; green trace represents ribbon-like folding isomer with the Cys3-Cys20, Cys9-Cys15 connectivity; blue trace represents the fast folding product with the bead-like connectivity Cys3-Cys9, Cys15-Cys20. The traces were collected using the same gradient as described for panel ( C ).

Techniques Used: High Performance Liquid Chromatography, Modification

Purification of cdg14a by high-performance liquid chromatography (HPLC) using C18 semi-preparative and analytical columns. The elution profiles show two different wavelengths used: 220 nm (black) and 280 nm (grey), with the elution gradient indicated by a blue line. ( A ) Chromatogram of the crude venom extract using a C18 semi-preparative column with linear gradient ranging from 6% to 60% solvent B (90% acetonitrile with 0.1% trifluoroacetic acid) at 0.9% solvent B/min, followed by 60% to 100% at 1.3% solvent B/min. The peak of the bioactive fraction is indicated by an arrow. ( B ) Chromatogram of the bioactive fraction reinjected in the HPLC using a C18 analytical column run at a shallower linear gradient ranging from 23% to 27% solvent B at 0.15% solvent B/min. The peak of the subfraction containing the bioactive peptide cdg14a is indicated by an arrow. ( C ) Chromatogram of the purified peptide cdg14a, showing a single, symmetrical peak.
Figure Legend Snippet: Purification of cdg14a by high-performance liquid chromatography (HPLC) using C18 semi-preparative and analytical columns. The elution profiles show two different wavelengths used: 220 nm (black) and 280 nm (grey), with the elution gradient indicated by a blue line. ( A ) Chromatogram of the crude venom extract using a C18 semi-preparative column with linear gradient ranging from 6% to 60% solvent B (90% acetonitrile with 0.1% trifluoroacetic acid) at 0.9% solvent B/min, followed by 60% to 100% at 1.3% solvent B/min. The peak of the bioactive fraction is indicated by an arrow. ( B ) Chromatogram of the bioactive fraction reinjected in the HPLC using a C18 analytical column run at a shallower linear gradient ranging from 23% to 27% solvent B at 0.15% solvent B/min. The peak of the subfraction containing the bioactive peptide cdg14a is indicated by an arrow. ( C ) Chromatogram of the purified peptide cdg14a, showing a single, symmetrical peak.

Techniques Used: Purification, High Performance Liquid Chromatography

21) Product Images from "Pharmacokinetic and nephroprotective benefits of using Schisandra chinensis extracts in a cyclosporine A-based immune-suppressive regime"

Article Title: Pharmacokinetic and nephroprotective benefits of using Schisandra chinensis extracts in a cyclosporine A-based immune-suppressive regime

Journal: Drug Design, Development and Therapy

doi: 10.2147/DDDT.S89876

Evaluation of the components in Schisandra chinensis extracts (SCE) using high-performance liquid chromatography assay. Notes: ( A ) The mixture of the three reference compounds. ( B ) The sample of SCE. Chromatographic separation was performed on a Kromasil C18 column (250 mm ×4.6 mm id, 5 μm) at 35°C. The mobile phase consisted of eluents A (water) and B (methanol). The elution program was optimized and conducted as follows: a linear gradient of 68–70% B (0–5 minutes), a linear gradient of 70–75% B (5–15 minutes), an isocratic elution of 75% B (15–38 minutes), a linear gradient of 75–68% B (38–39 minutes), an isocratic elution of 68% B (39–45 minutes). The peaks were recorded using PDA absorbance at 254 nm and the solvent flow rate was kept at 1.0 mL/min.
Figure Legend Snippet: Evaluation of the components in Schisandra chinensis extracts (SCE) using high-performance liquid chromatography assay. Notes: ( A ) The mixture of the three reference compounds. ( B ) The sample of SCE. Chromatographic separation was performed on a Kromasil C18 column (250 mm ×4.6 mm id, 5 μm) at 35°C. The mobile phase consisted of eluents A (water) and B (methanol). The elution program was optimized and conducted as follows: a linear gradient of 68–70% B (0–5 minutes), a linear gradient of 70–75% B (5–15 minutes), an isocratic elution of 75% B (15–38 minutes), a linear gradient of 75–68% B (38–39 minutes), an isocratic elution of 68% B (39–45 minutes). The peaks were recorded using PDA absorbance at 254 nm and the solvent flow rate was kept at 1.0 mL/min.

Techniques Used: High Performance Liquid Chromatography, Flow Cytometry

22) Product Images from "Development, characterization and comparisons of targeted and non-targeted metabolomics methods"

Article Title: Development, characterization and comparisons of targeted and non-targeted metabolomics methods

Journal: PLoS ONE

doi: 10.1371/journal.pone.0207082

Targeted vs non-targeted precision in NIST SRM 1950. Features from Orbi HILIC and Orbi C18 , selected manually or using the ‘lipidFrag’ function in our R-package, compared to features measured with QqQ HILIC and QqQ FI . Isomers or lipids from the low resolution QqQFI-method show up as duplicates in the list of compounds in the figure.
Figure Legend Snippet: Targeted vs non-targeted precision in NIST SRM 1950. Features from Orbi HILIC and Orbi C18 , selected manually or using the ‘lipidFrag’ function in our R-package, compared to features measured with QqQ HILIC and QqQ FI . Isomers or lipids from the low resolution QqQFI-method show up as duplicates in the list of compounds in the figure.

Techniques Used: Hydrophilic Interaction Liquid Chromatography

23) Product Images from "Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *"

Article Title: Site-specific Glycoforms of Haptoglobin in Liver Cirrhosis and Hepatocellular Carcinoma *

Journal: Molecular & Cellular Proteomics : MCP

doi: 10.1074/mcp.M112.023259

Extracted ion chromatogram of multiply sialylated and fucosylated glycoforms of the T3 peptide isolated from pooled plasma of HCC patients and separated by nano-reverse phase C18 chromatography after HILIC enrichment. The mass difference between the isoforms
Figure Legend Snippet: Extracted ion chromatogram of multiply sialylated and fucosylated glycoforms of the T3 peptide isolated from pooled plasma of HCC patients and separated by nano-reverse phase C18 chromatography after HILIC enrichment. The mass difference between the isoforms

Techniques Used: Isolation, Chromatography, Hydrophilic Interaction Liquid Chromatography

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Countercurrent Chromatography:

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Centrifugation:

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Flow Cytometry:

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Mass Spectrometry:

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Injection:

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    Waters Corporation c18 ost xbridge column
    Purification of non-palindromic dsDNA. ( a ) DNA elution profile of 0.5 mg of 28-bp DNA corresponding to the human mitochondrial LSP sequence (LSP 28mer) from a Waters X-Bridge <t>OST</t> <t>C18</t> column. DNA absorbance was monitored at 260 nm (black trace, left Y -axis), as DNA was eluted from the column using an acetonitrile gradient (gray trace, right Y -axis). Numbers correspond to fractions collected for purity analysis. Numbers correspond as follows: 1, phosphoramodite DNA synthesis material; 2–3, ssDNA 28 mer LSP DNA; 4–6, ds n–LSP DNA products; and 7–9, full length 28 mer LSP DNA. ( b ) Eight percent polyacrylamide native gel analysis and ( c ) 16% polyacrylamide 7 M urea denaturing gel analysis of fractions collected in (a) as indicated by numbers.
    C18 Ost Xbridge Column, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation symmetry c18 column
    Purification of stingray ghrelin-like peptide (GRLN-LP) from stomach extracts . Black bars indicate the measured fluorescence changes in intracellular calcium ion concentrations in CHO cells expressing rat GHS-R1a (CHO-GHSR62). (A) Carboxymethyl (CM)-cation ion-exchange HPLC (pH 4.8) of the SP-III fraction of stomach extracts. The GRLN-like activity was divided into four groups (A-D). (B) Preparative reverse-phase (RP)-HPLC (Symmetry <t>C18,</t> 3.9 × 150 mm) of group B after purification with an anti-rat GRLN1-11 immuno-affinity column. (C) Final purification of the active fraction indicated in (B) by another RP-HPLC (Vydac diphenyl, 219TP5215, 2.1 × 150 mm).
    Symmetry C18 Column, supplied by Waters Corporation, used in various techniques. Bioz Stars score: 92/100, based on 716 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Waters Corporation acquity uplc beh300 c18 chromatographic column
    Reversed-phase chromatographic profile of Transferon. Comparison between sample matrix (black line) and batch 15A01 of Transferon (blue line). Chromatographic profile exhibits 4 main peaks with k > 1 and absolute retention time of 2.2 min (P1), 4.3 min (P2), 6.4 min (P3), and 8.2 min (P4). Figure S1 shows that this chromatographic profile is consistent between the 10 analyzed Transferon batches. Transferon samples were analyzed using an <t>Acquity</t> ™ <t>UPLC</t> ™ <t>BEH300</t> <t>C18</t> chromatographic column (2.1 mm × 150 mm) and TFA (0.1%)-H 2 O and TFA (0.1%)-acetonitrile as the mobile phase at 0.4 mL/min using a gradient configuration. The column temperature was maintained at 30°C, and UV detection was performed at 214 nm. Chromatographic profiles were analyzed using Empower ™ (ApexTrack method) to obtain the relative area percentage and absolute retention time for each peak. AU: area units.
    Acquity Uplc Beh300 C18 Chromatographic Column, supplied by Waters Corporation, 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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    Purification of non-palindromic dsDNA. ( a ) DNA elution profile of 0.5 mg of 28-bp DNA corresponding to the human mitochondrial LSP sequence (LSP 28mer) from a Waters X-Bridge OST C18 column. DNA absorbance was monitored at 260 nm (black trace, left Y -axis), as DNA was eluted from the column using an acetonitrile gradient (gray trace, right Y -axis). Numbers correspond to fractions collected for purity analysis. Numbers correspond as follows: 1, phosphoramodite DNA synthesis material; 2–3, ssDNA 28 mer LSP DNA; 4–6, ds n–LSP DNA products; and 7–9, full length 28 mer LSP DNA. ( b ) Eight percent polyacrylamide native gel analysis and ( c ) 16% polyacrylamide 7 M urea denaturing gel analysis of fractions collected in (a) as indicated by numbers.

    Journal: Nucleic Acids Research

    Article Title: Reversed-phase ion-pair liquid chromatography method for purification of duplex DNA with single base pair resolution

    doi: 10.1093/nar/gkt815

    Figure Lengend Snippet: Purification of non-palindromic dsDNA. ( a ) DNA elution profile of 0.5 mg of 28-bp DNA corresponding to the human mitochondrial LSP sequence (LSP 28mer) from a Waters X-Bridge OST C18 column. DNA absorbance was monitored at 260 nm (black trace, left Y -axis), as DNA was eluted from the column using an acetonitrile gradient (gray trace, right Y -axis). Numbers correspond to fractions collected for purity analysis. Numbers correspond as follows: 1, phosphoramodite DNA synthesis material; 2–3, ssDNA 28 mer LSP DNA; 4–6, ds n–LSP DNA products; and 7–9, full length 28 mer LSP DNA. ( b ) Eight percent polyacrylamide native gel analysis and ( c ) 16% polyacrylamide 7 M urea denaturing gel analysis of fractions collected in (a) as indicated by numbers.

    Article Snippet: After the Sep-Pak-purified single-stranded oligos were annealed, 0.5 mg of ds 28mer DNA was purified by reversed-phase ion-pair HPLC on a Waters C18 OST XBridge column with a 5–12% acetonitrile gradient over the course of 40 min ( a).

    Techniques: Purification, Sequencing, DNA Synthesis

    Purification of stingray ghrelin-like peptide (GRLN-LP) from stomach extracts . Black bars indicate the measured fluorescence changes in intracellular calcium ion concentrations in CHO cells expressing rat GHS-R1a (CHO-GHSR62). (A) Carboxymethyl (CM)-cation ion-exchange HPLC (pH 4.8) of the SP-III fraction of stomach extracts. The GRLN-like activity was divided into four groups (A-D). (B) Preparative reverse-phase (RP)-HPLC (Symmetry C18, 3.9 × 150 mm) of group B after purification with an anti-rat GRLN1-11 immuno-affinity column. (C) Final purification of the active fraction indicated in (B) by another RP-HPLC (Vydac diphenyl, 219TP5215, 2.1 × 150 mm).

    Journal: BMC Biochemistry

    Article Title: Ghrelin-like peptide with fatty acid modification and O-glycosylation in the red stingray, Dasyatis akajei

    doi: 10.1186/1471-2091-10-30

    Figure Lengend Snippet: Purification of stingray ghrelin-like peptide (GRLN-LP) from stomach extracts . Black bars indicate the measured fluorescence changes in intracellular calcium ion concentrations in CHO cells expressing rat GHS-R1a (CHO-GHSR62). (A) Carboxymethyl (CM)-cation ion-exchange HPLC (pH 4.8) of the SP-III fraction of stomach extracts. The GRLN-like activity was divided into four groups (A-D). (B) Preparative reverse-phase (RP)-HPLC (Symmetry C18, 3.9 × 150 mm) of group B after purification with an anti-rat GRLN1-11 immuno-affinity column. (C) Final purification of the active fraction indicated in (B) by another RP-HPLC (Vydac diphenyl, 219TP5215, 2.1 × 150 mm).

    Article Snippet: The samples were first applied to a preparative RP-HPLC with a Symmetry C18 column (3.9 × 150 mm, Waters) at a flow rate of 1 ml/min under a linear gradient from 10% to 60% acetonitlile containing 0.1% TFA for 40 min.

    Techniques: Purification, Fluorescence, Expressing, High Performance Liquid Chromatography, Activity Assay, Affinity Column

    Histone preparation with Lys-propionylation, trypsin digestion, and N-terminal PIC-labeling. A , Sample preparation workflow. B , Relative ionization efficiencies H3 T3-R8 peptide in all modified forms. C , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. All abundances are expressed relative to the unmodified peptide.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title:

    doi: 10.1074/mcp.O114.046573

    Figure Lengend Snippet: Histone preparation with Lys-propionylation, trypsin digestion, and N-terminal PIC-labeling. A , Sample preparation workflow. B , Relative ionization efficiencies H3 T3-R8 peptide in all modified forms. C , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. All abundances are expressed relative to the unmodified peptide.

    Article Snippet: Peptides were loaded onto a C18 column (BEH-C18; 100 μm i.d. x 10 cm; 1.7 μm particles, 130Å pores; Waters Corp., Milford, MA) for 10 min at 1.5 μl per minute in 2% solvent B (0.1% v/v formic acid, 98% v/v acetonitrile) and separated at 1 μl per minute by a linear gradient from 2% solvent B to 25% solvent B over 60 min followed by a ramp to 40% B in 15 min, then to 90% B and re-equilibration at 2% B for a 90-min total run time.

    Techniques: Labeling, Sample Prep, Modification

    Sources of discrepancy in H3K4 quantitation. A , Equimolar mixture of isotope-labeled, propionylated H3 T3-R8 peptide in eight modification states, injected in the milieu of endogenous histones from 293T cells. B , Time course of digestion releasing propionylated H3 T3-R8 from propionylated H3 A1-R17, where K4 is trimethylated. C , Relative ionization efficiencies of the propionylated H3 T3-R8 peptide in its various modified forms. D , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. In panels A , C , D , all abundances are expressed relative to the unmodified peptide.

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title:

    doi: 10.1074/mcp.O114.046573

    Figure Lengend Snippet: Sources of discrepancy in H3K4 quantitation. A , Equimolar mixture of isotope-labeled, propionylated H3 T3-R8 peptide in eight modification states, injected in the milieu of endogenous histones from 293T cells. B , Time course of digestion releasing propionylated H3 T3-R8 from propionylated H3 A1-R17, where K4 is trimethylated. C , Relative ionization efficiencies of the propionylated H3 T3-R8 peptide in its various modified forms. D , Recovery of H3 T3-R8 peptides following StageTip C18 cleanup. In panels A , C , D , all abundances are expressed relative to the unmodified peptide.

    Article Snippet: Peptides were loaded onto a C18 column (BEH-C18; 100 μm i.d. x 10 cm; 1.7 μm particles, 130Å pores; Waters Corp., Milford, MA) for 10 min at 1.5 μl per minute in 2% solvent B (0.1% v/v formic acid, 98% v/v acetonitrile) and separated at 1 μl per minute by a linear gradient from 2% solvent B to 25% solvent B over 60 min followed by a ramp to 40% B in 15 min, then to 90% B and re-equilibration at 2% B for a 90-min total run time.

    Techniques: Quantitation Assay, Labeling, Modification, Injection

    Direct comparison of standard propionylation (Prop-x2) labeling and the hybrid (Prop-PIC) labeling method via LC-MS using a 1:1 mixture of labeled histone samples. A , Extracted ion chromatograms of the hydrophilic H3T3-R8 peptide (TK 4 QTAR) and its modified versions on C18 reverse-phase LC-MS. Retention times and relative abundances are increased by the hybrid labeling method. B , Quantitative comparison of the recoveries of each H3.1 histone tail peptide, where integrated peak areas for all modification states are combined. C , Quantitative comparison of the recoveries of the H3 T3-R8 peptide in its various modification states for the Prop-PIC versus Propx2 (integrated peak areas; n = 3, error bars are standard deviations).

    Journal: Molecular & Cellular Proteomics : MCP

    Article Title:

    doi: 10.1074/mcp.O114.046573

    Figure Lengend Snippet: Direct comparison of standard propionylation (Prop-x2) labeling and the hybrid (Prop-PIC) labeling method via LC-MS using a 1:1 mixture of labeled histone samples. A , Extracted ion chromatograms of the hydrophilic H3T3-R8 peptide (TK 4 QTAR) and its modified versions on C18 reverse-phase LC-MS. Retention times and relative abundances are increased by the hybrid labeling method. B , Quantitative comparison of the recoveries of each H3.1 histone tail peptide, where integrated peak areas for all modification states are combined. C , Quantitative comparison of the recoveries of the H3 T3-R8 peptide in its various modification states for the Prop-PIC versus Propx2 (integrated peak areas; n = 3, error bars are standard deviations).

    Article Snippet: Peptides were loaded onto a C18 column (BEH-C18; 100 μm i.d. x 10 cm; 1.7 μm particles, 130Å pores; Waters Corp., Milford, MA) for 10 min at 1.5 μl per minute in 2% solvent B (0.1% v/v formic acid, 98% v/v acetonitrile) and separated at 1 μl per minute by a linear gradient from 2% solvent B to 25% solvent B over 60 min followed by a ramp to 40% B in 15 min, then to 90% B and re-equilibration at 2% B for a 90-min total run time.

    Techniques: Labeling, Liquid Chromatography with Mass Spectroscopy, Modification

    Reversed-phase chromatographic profile of Transferon. Comparison between sample matrix (black line) and batch 15A01 of Transferon (blue line). Chromatographic profile exhibits 4 main peaks with k > 1 and absolute retention time of 2.2 min (P1), 4.3 min (P2), 6.4 min (P3), and 8.2 min (P4). Figure S1 shows that this chromatographic profile is consistent between the 10 analyzed Transferon batches. Transferon samples were analyzed using an Acquity ™ UPLC ™ BEH300 C18 chromatographic column (2.1 mm × 150 mm) and TFA (0.1%)-H 2 O and TFA (0.1%)-acetonitrile as the mobile phase at 0.4 mL/min using a gradient configuration. The column temperature was maintained at 30°C, and UV detection was performed at 214 nm. Chromatographic profiles were analyzed using Empower ™ (ApexTrack method) to obtain the relative area percentage and absolute retention time for each peak. AU: area units.

    Journal: BioMed Research International

    Article Title: Physicochemical Characteristics of Transferon™ Batches

    doi: 10.1155/2016/7935181

    Figure Lengend Snippet: Reversed-phase chromatographic profile of Transferon. Comparison between sample matrix (black line) and batch 15A01 of Transferon (blue line). Chromatographic profile exhibits 4 main peaks with k > 1 and absolute retention time of 2.2 min (P1), 4.3 min (P2), 6.4 min (P3), and 8.2 min (P4). Figure S1 shows that this chromatographic profile is consistent between the 10 analyzed Transferon batches. Transferon samples were analyzed using an Acquity ™ UPLC ™ BEH300 C18 chromatographic column (2.1 mm × 150 mm) and TFA (0.1%)-H 2 O and TFA (0.1%)-acetonitrile as the mobile phase at 0.4 mL/min using a gradient configuration. The column temperature was maintained at 30°C, and UV detection was performed at 214 nm. Chromatographic profiles were analyzed using Empower ™ (ApexTrack method) to obtain the relative area percentage and absolute retention time for each peak. AU: area units.

    Article Snippet: Chromatographic separation was performed using an Acquity UPLC BEH300 C18 chromatographic column (1.7 μ m, 2.1 mm × 150 mm) (Waters) with gradient workflow of 0.4 mL/min of ultrapure purified water (Merck Millipore Co., Darmstadt, Germany) with 0.1% trifluoroacetic acid (TFA) (Sigma-Aldrich, Missouri, USA) and acetonitrile (Mallinckrodt Baker, Pennsylvania, USA) and 0.1% TFA (Sigma-Aldrich).

    Techniques: