Structured Review

Waters Corporation reverse phase hplc
<t>NP1-HPLC</t> assay of CALU and the U-substituted sequences after 2.5 h of <t>UVB</t> irradiation at pH 7.5. A) NP1-HPLC trace for parent CALU sequence in 150 mM NaCl and sequences containing site-specific uracil substitutions. MALDI confirmed the assignment of pT(G)=pT(G) and pT(G)=pU(G) photoproducts. B) Sequences used in mapping of CALU G-quadruplex photoproduct sites.
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1) Product Images from "Photocrosslinking of G-Quadruplex Forming Sequences found in Human Promoters"

Article Title: Photocrosslinking of G-Quadruplex Forming Sequences found in Human Promoters

Journal: Photochemistry and photobiology

doi: 10.1111/php.12991

NP1-HPLC assay of CALU and the U-substituted sequences after 2.5 h of UVB irradiation at pH 7.5. A) NP1-HPLC trace for parent CALU sequence in 150 mM NaCl and sequences containing site-specific uracil substitutions. MALDI confirmed the assignment of pT(G)=pT(G) and pT(G)=pU(G) photoproducts. B) Sequences used in mapping of CALU G-quadruplex photoproduct sites.
Figure Legend Snippet: NP1-HPLC assay of CALU and the U-substituted sequences after 2.5 h of UVB irradiation at pH 7.5. A) NP1-HPLC trace for parent CALU sequence in 150 mM NaCl and sequences containing site-specific uracil substitutions. MALDI confirmed the assignment of pT(G)=pT(G) and pT(G)=pU(G) photoproducts. B) Sequences used in mapping of CALU G-quadruplex photoproduct sites.

Techniques Used: High Performance Liquid Chromatography, Irradiation, Sequencing

2) Product Images from "Galloyl-RGD as a new cosmetic ingredient"

Article Title: Galloyl-RGD as a new cosmetic ingredient

Journal: BMC Biochemistry

doi: 10.1186/1471-2091-15-18

Galloyl-RGD purification by HPLC. (a) Before HPLC purification using a C18 preparative column there were many compounds which the rate in galloyl-RGD was about 30% and were shown 8 peaks at least. (b) Purity of galloyl-RGD increased to 95% after HPLC purification using a C18 preparative column and was detected only 1 peak.
Figure Legend Snippet: Galloyl-RGD purification by HPLC. (a) Before HPLC purification using a C18 preparative column there were many compounds which the rate in galloyl-RGD was about 30% and were shown 8 peaks at least. (b) Purity of galloyl-RGD increased to 95% after HPLC purification using a C18 preparative column and was detected only 1 peak.

Techniques Used: Purification, High Performance Liquid Chromatography

3) Product Images from "Determination of Ghrelin Structure in the Barfin Flounder (Verasper moseri) and Involvement of Ingested Fatty Acids in Ghrelin Acylation"

Article Title: Determination of Ghrelin Structure in the Barfin Flounder (Verasper moseri) and Involvement of Ingested Fatty Acids in Ghrelin Acylation

Journal: Frontiers in Endocrinology

doi: 10.3389/fendo.2013.00117

Distribution of ghrelin activity in fractions separated by reverse-phase HPLC . Ghrelin activity in the equivalent of 100 mg stomach tissue is expressed in terms of fluorescence change in CHO cells expressing rat GHS-R1a. The maximum changes in fluorescence are plotted. The numbers of samples used are as follows: control (Cont, n = 4); n -heptanoic acid (C7)-enriched feed ( n = 4); n -octanoic acid (C8)-enriched feed ( n = 6); and n -non-anoic acid (C9)-enriched feed ( n = 6). The values for each group were compared to the control values by analysis of variance followed by Fisher’s protected least significant difference test. Differences were considered significant at P
Figure Legend Snippet: Distribution of ghrelin activity in fractions separated by reverse-phase HPLC . Ghrelin activity in the equivalent of 100 mg stomach tissue is expressed in terms of fluorescence change in CHO cells expressing rat GHS-R1a. The maximum changes in fluorescence are plotted. The numbers of samples used are as follows: control (Cont, n = 4); n -heptanoic acid (C7)-enriched feed ( n = 4); n -octanoic acid (C8)-enriched feed ( n = 6); and n -non-anoic acid (C9)-enriched feed ( n = 6). The values for each group were compared to the control values by analysis of variance followed by Fisher’s protected least significant difference test. Differences were considered significant at P

Techniques Used: Activity Assay, High Performance Liquid Chromatography, Fluorescence, Expressing

Representative absorption spectra and activity data obtained at various points during the purification of ghrelin from the stomach of barfin flounder fed normal feed . (A) Carboxyl methyl ion-exchange HPLC. Black bars indicate ghrelin activity measured using CHO cells expressing rat GHS-R1a. The fractions were divided into groups a–g on the basis of ghrelin activity. (B) Reverse-phase HPLC of group “e” on a symmetry 300 C18 column. The arrow indicates the major peak. (C) Reverse-phase HPLC of group “e” on a diphenyl column. The peak labeled P1 corresponds to the peak indicated by the arrow in (B) ; this peak corresponds to the peptide obtained in the highest yield from the stomach of fish fed normal feed. (D) The peptide (P2) obtained in the second highest yield (isolated from group “g”). (E) The peptides (P3 and P4) obtained in the third and fourth highest yields (isolated from group “c”).
Figure Legend Snippet: Representative absorption spectra and activity data obtained at various points during the purification of ghrelin from the stomach of barfin flounder fed normal feed . (A) Carboxyl methyl ion-exchange HPLC. Black bars indicate ghrelin activity measured using CHO cells expressing rat GHS-R1a. The fractions were divided into groups a–g on the basis of ghrelin activity. (B) Reverse-phase HPLC of group “e” on a symmetry 300 C18 column. The arrow indicates the major peak. (C) Reverse-phase HPLC of group “e” on a diphenyl column. The peak labeled P1 corresponds to the peak indicated by the arrow in (B) ; this peak corresponds to the peptide obtained in the highest yield from the stomach of fish fed normal feed. (D) The peptide (P2) obtained in the second highest yield (isolated from group “g”). (E) The peptides (P3 and P4) obtained in the third and fourth highest yields (isolated from group “c”).

Techniques Used: Activity Assay, Purification, High Performance Liquid Chromatography, Expressing, Labeling, Fluorescence In Situ Hybridization, Isolation

Distribution of ghrelin activity in fractions separated by ion-exchange HPLC of samples obtained from fish fed (A) normal feed, (B) n -heptanoic acid (C7)-enriched feed, (C) n -octanoic acid (C8)-enriched feed, and (D) n -non-anoic acid (C9)-enriched feed . The fractions were assigned to groups a–w on the basis of their ghrelin activity. Ghrelin activity in the equivalent of 400 mg stomach tissue is expressed in terms of fluorescence change in CHO cells expressing rat GHS-R1a The maximum changes in fluorescence are plotted.
Figure Legend Snippet: Distribution of ghrelin activity in fractions separated by ion-exchange HPLC of samples obtained from fish fed (A) normal feed, (B) n -heptanoic acid (C7)-enriched feed, (C) n -octanoic acid (C8)-enriched feed, and (D) n -non-anoic acid (C9)-enriched feed . The fractions were assigned to groups a–w on the basis of their ghrelin activity. Ghrelin activity in the equivalent of 400 mg stomach tissue is expressed in terms of fluorescence change in CHO cells expressing rat GHS-R1a The maximum changes in fluorescence are plotted.

Techniques Used: Activity Assay, High Performance Liquid Chromatography, Fluorescence In Situ Hybridization, Fluorescence, Expressing

4) Product Images from "Fesselin, a Synaptopodin-like Protein, Stimulates Actin Nucleation and Polymerization †"

Article Title: Fesselin, a Synaptopodin-like Protein, Stimulates Actin Nucleation and Polymerization †

Journal: Biochemistry

doi: 10.1021/bi011806u

Both fesselin polypeptides have actin polymerization activity. (A) SDS–polyacrylamide (7%) gel electrophoresis showing that fesselin promotes actin polymerization. Each assay contained 5 μM skeletal muscle G-actin in 5 mM Tris-HCl, 0.2 mM ATP, 0.5 mM DTT, 0.1 mM CaCl 2 , and 0.01% NaN 3 , pH 7.8. Reactions were initiated by the addition of 2 mM MgCl 2 ± 100 nM fesselin and centrifuged immediately in an Airfuge. The supernatants and pellets were analyzed by electrophoresis. (a) Actin standard, (b) fesselin standard, (c) supernatant from MgCl 2 alone, (d) pellet from MgCl 2 alone, (e) supernatant from MgCl 2 + fesselin, (f) pellet from MgCl 2 + fesselin. (B) The two fesselin polypeptides seen in panel A were separated by HPLC and tested for the ability to polymerize 5 μM pyrene-labeled smooth muscle actin. Four reactions were monitored simultaneously in a microplate fluorometer. All reactions were initiated by the addition of 2 mM MgCl 2 ) 0.25 μM of both polypeptides. The cation bound to actin was Mg 2+ in all reactions.
Figure Legend Snippet: Both fesselin polypeptides have actin polymerization activity. (A) SDS–polyacrylamide (7%) gel electrophoresis showing that fesselin promotes actin polymerization. Each assay contained 5 μM skeletal muscle G-actin in 5 mM Tris-HCl, 0.2 mM ATP, 0.5 mM DTT, 0.1 mM CaCl 2 , and 0.01% NaN 3 , pH 7.8. Reactions were initiated by the addition of 2 mM MgCl 2 ± 100 nM fesselin and centrifuged immediately in an Airfuge. The supernatants and pellets were analyzed by electrophoresis. (a) Actin standard, (b) fesselin standard, (c) supernatant from MgCl 2 alone, (d) pellet from MgCl 2 alone, (e) supernatant from MgCl 2 + fesselin, (f) pellet from MgCl 2 + fesselin. (B) The two fesselin polypeptides seen in panel A were separated by HPLC and tested for the ability to polymerize 5 μM pyrene-labeled smooth muscle actin. Four reactions were monitored simultaneously in a microplate fluorometer. All reactions were initiated by the addition of 2 mM MgCl 2 ) 0.25 μM of both polypeptides. The cation bound to actin was Mg 2+ in all reactions.

Techniques Used: Activity Assay, Nucleic Acid Electrophoresis, Electrophoresis, High Performance Liquid Chromatography, Labeling

5) Product Images from "An [18F]-Positron-Emitting, Fluorescent, Cerebrospinal Fluid Probe for Imaging Damage to the Brain and Spine"

Article Title: An [18F]-Positron-Emitting, Fluorescent, Cerebrospinal Fluid Probe for Imaging Damage to the Brain and Spine

Journal: Theranostics

doi: 10.7150/thno.19408

Spectral and radioactive properties of [ 18/19 F]- 2. (A) Excitation and emission spectra of 5-6 μM solutions of fluorescein (black) and [ 18/19 F]- 2 (green) in 1x PBS, pH 7.4 measured on a Cary Eclipse spectrophotometer, with 5 nm slit widths, and excitation at 490 nm. (B) In vitro cell viability tests performed with compound 2 (red line) and fluorescein (control) 24 hour on U87, Hela, MDA-MB-231, and A549 immortal cell lines using a CellTiter 96® AQueous One Solution Cell Proliferation Assay (MTS, G3582, Promega). Toxicity is not observed. (C) UV-Vis (280, 350, and 450 nm) UPLC-MS of 2 on a waters Acuity UPLC and a Phenomenex Luna Kinetex 1.7 µm EVO C18 50 x 2.1 mm column (00B-4726-AN), with a 1.5 min, a10-90% H 2 O:ACN (0.05% TFA) elution gradient indicating a pure synthesis of 2 . (D) Reverse phase HPLC of radiolabeled [ 18 F]- 2 on a Varian HPLC, using an Waters SunfireTM C18 3.5 μm 4.6 x 50 mm column (186002551), a10-90% H 2 O:ACN (0.05% TFA) elution gradient and a flow rate of 2 mL/min. (E) 10 µL 3x dilution series of [ 18/19 F]- 2 beginning at 70 µM (1.7 pmols) and 170 µCi of [ 18/19 F]- 2 (first spot). A 10 µl volume was plated onto glass-backed TLC plate model. Imaging was performed using (i) bright-field; (ii) a UV-sight hand-held 4.5 volt LED black-light (fluorescence); (iii) a Bruker Xtreme optical imaging device (fluorescence: 1 sec acquisition using excitation and emission filters set at λex= 450 nm and λem= 535 nm); (iv) and a phosphorimager.
Figure Legend Snippet: Spectral and radioactive properties of [ 18/19 F]- 2. (A) Excitation and emission spectra of 5-6 μM solutions of fluorescein (black) and [ 18/19 F]- 2 (green) in 1x PBS, pH 7.4 measured on a Cary Eclipse spectrophotometer, with 5 nm slit widths, and excitation at 490 nm. (B) In vitro cell viability tests performed with compound 2 (red line) and fluorescein (control) 24 hour on U87, Hela, MDA-MB-231, and A549 immortal cell lines using a CellTiter 96® AQueous One Solution Cell Proliferation Assay (MTS, G3582, Promega). Toxicity is not observed. (C) UV-Vis (280, 350, and 450 nm) UPLC-MS of 2 on a waters Acuity UPLC and a Phenomenex Luna Kinetex 1.7 µm EVO C18 50 x 2.1 mm column (00B-4726-AN), with a 1.5 min, a10-90% H 2 O:ACN (0.05% TFA) elution gradient indicating a pure synthesis of 2 . (D) Reverse phase HPLC of radiolabeled [ 18 F]- 2 on a Varian HPLC, using an Waters SunfireTM C18 3.5 μm 4.6 x 50 mm column (186002551), a10-90% H 2 O:ACN (0.05% TFA) elution gradient and a flow rate of 2 mL/min. (E) 10 µL 3x dilution series of [ 18/19 F]- 2 beginning at 70 µM (1.7 pmols) and 170 µCi of [ 18/19 F]- 2 (first spot). A 10 µl volume was plated onto glass-backed TLC plate model. Imaging was performed using (i) bright-field; (ii) a UV-sight hand-held 4.5 volt LED black-light (fluorescence); (iii) a Bruker Xtreme optical imaging device (fluorescence: 1 sec acquisition using excitation and emission filters set at λex= 450 nm and λem= 535 nm); (iv) and a phosphorimager.

Techniques Used: Spectrophotometry, In Vitro, Multiple Displacement Amplification, Proliferation Assay, Mass Spectrometry, High Performance Liquid Chromatography, Flow Cytometry, Thin Layer Chromatography, Imaging, Fluorescence, Optical Imaging, Size-exclusion Chromatography

6) Product Images from "Rat heart: A site of oxytocin production and action"

Article Title: Rat heart: A site of oxytocin production and action

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

doi:

Reverse-phase HPLC elution profile of oxytocin immunoreactivity in rat tissues. Tissue extracts, lyophilized and reconstituted in 20% acetonitrile in 0.1% TFA, were applied to a C 18 Bondapak column and were eluted with acetonitrile gradient (20–50%) in 0.1% TFA. ( A ) The extract from the right atrium. ( B ) The extract from the heart perfusates. ( C ) The HPLC profile of OT synthetic standard. ( D ) The extract from the pituitary gland.
Figure Legend Snippet: Reverse-phase HPLC elution profile of oxytocin immunoreactivity in rat tissues. Tissue extracts, lyophilized and reconstituted in 20% acetonitrile in 0.1% TFA, were applied to a C 18 Bondapak column and were eluted with acetonitrile gradient (20–50%) in 0.1% TFA. ( A ) The extract from the right atrium. ( B ) The extract from the heart perfusates. ( C ) The HPLC profile of OT synthetic standard. ( D ) The extract from the pituitary gland.

Techniques Used: High Performance Liquid Chromatography

7) Product Images from "Hydrophobicity drives the systemic distribution of lipid-conjugated siRNAs via lipid transport pathways"

Article Title: Hydrophobicity drives the systemic distribution of lipid-conjugated siRNAs via lipid transport pathways

Journal: Nucleic Acids Research

doi: 10.1093/nar/gky1232

Synthesis and biophysical characterization of lipid-hsiRNA conjugates. ( A ) Chemical structures of lipid-hsiRNA conjugates. ( B ) Modification pattern and molecular model of lipid-hsiRNAs. ( C ) HPLC traces of lipid-hsiRNAs following reverse phase column chromatography. ( D ) HeLa cells were incubated with PPIB -targeting hsiRNAs at concentrations shown for 72 h. PPIB mRNA levels were measured using QuantiGene (Affymetrix), normalized to housekeeping HPRT1 (hypoxanthine phosphoribosyltransferase 1) mRNA levels, and presented as percent of untreated control ( n = 3, mean ± SD). UNT – untreated cells. ( E ) Plotted IC 50 values determined from the best-fit curves in (D).
Figure Legend Snippet: Synthesis and biophysical characterization of lipid-hsiRNA conjugates. ( A ) Chemical structures of lipid-hsiRNA conjugates. ( B ) Modification pattern and molecular model of lipid-hsiRNAs. ( C ) HPLC traces of lipid-hsiRNAs following reverse phase column chromatography. ( D ) HeLa cells were incubated with PPIB -targeting hsiRNAs at concentrations shown for 72 h. PPIB mRNA levels were measured using QuantiGene (Affymetrix), normalized to housekeeping HPRT1 (hypoxanthine phosphoribosyltransferase 1) mRNA levels, and presented as percent of untreated control ( n = 3, mean ± SD). UNT – untreated cells. ( E ) Plotted IC 50 values determined from the best-fit curves in (D).

Techniques Used: Modification, High Performance Liquid Chromatography, Column Chromatography, Incubation

8) Product Images from "Photocrosslinking of G-Quadruplex Forming Sequences found in Human Promoters"

Article Title: Photocrosslinking of G-Quadruplex Forming Sequences found in Human Promoters

Journal: Photochemistry and photobiology

doi: 10.1111/php.12991

NP1-HPLC assay of CALU and the U-substituted sequences after 2.5 h of UVB irradiation at pH 7.5. A) NP1-HPLC trace for parent CALU sequence in 150 mM NaCl and sequences containing site-specific uracil substitutions. MALDI confirmed the assignment of pT(G)=pT(G) and pT(G)=pU(G) photoproducts. B) Sequences used in mapping of CALU G-quadruplex photoproduct sites.
Figure Legend Snippet: NP1-HPLC assay of CALU and the U-substituted sequences after 2.5 h of UVB irradiation at pH 7.5. A) NP1-HPLC trace for parent CALU sequence in 150 mM NaCl and sequences containing site-specific uracil substitutions. MALDI confirmed the assignment of pT(G)=pT(G) and pT(G)=pU(G) photoproducts. B) Sequences used in mapping of CALU G-quadruplex photoproduct sites.

Techniques Used: High Performance Liquid Chromatography, Irradiation, Sequencing

9) Product Images from "The Subunit Composition of Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) From Pichia pastoris"

Article Title: The Subunit Composition of Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) From Pichia pastoris

Journal: Molecular & Cellular Proteomics : MCP

doi: 10.1074/mcp.M110.001255

Reverse-phase HPLC trace showing the separation of the subunits of complex I from P. pastoris . Proteins were eluted from a reverse-phase HPLC column, at 50 μl min −1 , in a 100-min linear gradient of 0-70% propan-2-ol and 15-20% trifluoroethanol, in 1% hexafluoroisopropanol and 50 m m ammonium formate (pH 3.1). The eluant was analyzed by an online ESI mass spectrometer (see Experimental Methods), so the elution trace is described by the total ion current. The labels denote detected molecular masses that could be assigned to subunits of P. pastoris complex I; the numbers refer to the subunits as listed in Table II .
Figure Legend Snippet: Reverse-phase HPLC trace showing the separation of the subunits of complex I from P. pastoris . Proteins were eluted from a reverse-phase HPLC column, at 50 μl min −1 , in a 100-min linear gradient of 0-70% propan-2-ol and 15-20% trifluoroethanol, in 1% hexafluoroisopropanol and 50 m m ammonium formate (pH 3.1). The eluant was analyzed by an online ESI mass spectrometer (see Experimental Methods), so the elution trace is described by the total ion current. The labels denote detected molecular masses that could be assigned to subunits of P. pastoris complex I; the numbers refer to the subunits as listed in Table II .

Techniques Used: High Performance Liquid Chromatography, Mass Spectrometry

10) Product Images from "CONSTITUTIVE ANDROSTANE RECEPTOR MEDIATES PCB-INDUCED DISRUPTION OF RETINOID HOMEOSTASIS"

Article Title: CONSTITUTIVE ANDROSTANE RECEPTOR MEDIATES PCB-INDUCED DISRUPTION OF RETINOID HOMEOSTASIS

Journal: Toxicology and applied pharmacology

doi: 10.1016/j.taap.2019.114731

Hepatic and plasma retinoid concentrations in wild type and Car −/− mice after PCB153 administration. Panels A and B – Retinyl ester (RE) and retinol (ROH) concentrations determined by HPLC in wild type and Car −/− livers of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel C – Plasma retinol concentrations determined by HPLC in wild type and Car −/− mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel D – Relative levels of plasma RBP4 in wild type and Car −/− mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel E – all- trans -Retinoic acid (atRA) concentrations were determined by UPLC/MS/MS in wild type and Car −/− livers of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel F – 4-hydroxy-all- trans -Retinoic acid (4-OH-atRA) concentrations were determined by UPLC/MS/MS for wild type and Car −/− livers of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration. Values marked with different letters (a, b, c, d) are statistically different, P
Figure Legend Snippet: Hepatic and plasma retinoid concentrations in wild type and Car −/− mice after PCB153 administration. Panels A and B – Retinyl ester (RE) and retinol (ROH) concentrations determined by HPLC in wild type and Car −/− livers of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel C – Plasma retinol concentrations determined by HPLC in wild type and Car −/− mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel D – Relative levels of plasma RBP4 in wild type and Car −/− mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel E – all- trans -Retinoic acid (atRA) concentrations were determined by UPLC/MS/MS in wild type and Car −/− livers of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel F – 4-hydroxy-all- trans -Retinoic acid (4-OH-atRA) concentrations were determined by UPLC/MS/MS for wild type and Car −/− livers of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration. Values marked with different letters (a, b, c, d) are statistically different, P

Techniques Used: Mouse Assay, High Performance Liquid Chromatography, Tandem Mass Spectroscopy

Retinoid concentrations and Rarβ mRNA expression in white adipose tissue of wild type and Car −/− mice after PCB153 administration. Panels A and B – Retinyl ester (RE) and retinol (ROH) concentrations determined by HPLC in wild type and Car −/− adipose tissues of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel C – all- trans -Retinoic acid (atRA) concentrations were determined by UPLC/MS/MS in wild type and Car −/− adipose tissues of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks); Panel D – Gene expression values (normalized to 18S rRNA levels) were determined by qRT-PCR for RNA obtained from adipose tissues of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration. Values marked with different letters (a, b, c, d) are statistically different, P
Figure Legend Snippet: Retinoid concentrations and Rarβ mRNA expression in white adipose tissue of wild type and Car −/− mice after PCB153 administration. Panels A and B – Retinyl ester (RE) and retinol (ROH) concentrations determined by HPLC in wild type and Car −/− adipose tissues of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration; Panel C – all- trans -Retinoic acid (atRA) concentrations were determined by UPLC/MS/MS in wild type and Car −/− adipose tissues of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks); Panel D – Gene expression values (normalized to 18S rRNA levels) were determined by qRT-PCR for RNA obtained from adipose tissues of mice after administration of PCB153 (50 mg/kg body weight weekly for 4 weeks), either with or without oral retinyl acetate (Rac, 300 IU daily for 4 weeks) administration. Values marked with different letters (a, b, c, d) are statistically different, P

Techniques Used: Expressing, Mouse Assay, High Performance Liquid Chromatography, Tandem Mass Spectroscopy, Quantitative RT-PCR

11) Product Images from "The Effect of Plasma Pretreatment and Cross-Linking Degree on the Physical and Antimicrobial Properties of Nisin-Coated PVA Films"

Article Title: The Effect of Plasma Pretreatment and Cross-Linking Degree on the Physical and Antimicrobial Properties of Nisin-Coated PVA Films

Journal: Materials

doi: 10.3390/ma11081451

Nisin release from the PVA films after immersion in physiological solution, analysed by RP-HPLC: ( a ) cumulative concentration in µg/mm 2 and ( b ) related to total released amount.
Figure Legend Snippet: Nisin release from the PVA films after immersion in physiological solution, analysed by RP-HPLC: ( a ) cumulative concentration in µg/mm 2 and ( b ) related to total released amount.

Techniques Used: High Performance Liquid Chromatography, Concentration Assay

12) Product Images from "Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation"

Article Title: Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation

Journal: eLife

doi: 10.7554/eLife.15598

Supporting data for the 2HF labelling. ( A ) HPLC traces of SecA G793C ( Figure 7A ), the peptide AWCWA, and SecA G793C crosslinked to AWCWA, either with or without 20 min pre-incubation 100 mM DTT to break the disulphide bond. HPLC with DTT confirms that AWCWA is present on the crosslinked protein, while HPLC without DTT confirms that they are indeed connected by a disulphide bond. Dividing the peak integrals by the extinction coefficients of the components (ε = 99,000 M -1 .cm -1 for SecA, determined experimentally; and ε = 11,380 M -1 .cm -1 for AWCWA, calculated) gives an estimated labelling efficiency of 82%. Note that incomplete reduction of the disulphide bond would lead us to underestimate this value. Because only the tryptophan-containing (AWCWA) peptide has an appreciable UV absorption signal, we were unable to quantify labelling with the other two peptides. However, as the peptide labelling experiments were performed in parallel, and AWCWA is the least soluble of the three, AGCGA and AFCFA are likely to have crosslinked with the same or better efficiencies. ( B ) Stopped flow time traces for the data shown in Figure 7D and panel C . For ease of comparison, data were fitted to a single exponential, then normalised to an amplitude of 1. Note that SecA R20C was not tested with AGCGA or AFCFA, and SecA ∆cys was not tested with any peptide, as it has no cross-linking site. ( C ) Rates of ADP release for SecA R20C alone; with excess SecYEG; and crosslinked to the peptide AWCWA (and in the presence of excess SecYEG). For this position, which is not near the entrance to SecY ( Figure 7A ), the crosslinked peptide has no effect on the rate of ADP release. DOI: http://dx.doi.org/10.7554/eLife.15598.021
Figure Legend Snippet: Supporting data for the 2HF labelling. ( A ) HPLC traces of SecA G793C ( Figure 7A ), the peptide AWCWA, and SecA G793C crosslinked to AWCWA, either with or without 20 min pre-incubation 100 mM DTT to break the disulphide bond. HPLC with DTT confirms that AWCWA is present on the crosslinked protein, while HPLC without DTT confirms that they are indeed connected by a disulphide bond. Dividing the peak integrals by the extinction coefficients of the components (ε = 99,000 M -1 .cm -1 for SecA, determined experimentally; and ε = 11,380 M -1 .cm -1 for AWCWA, calculated) gives an estimated labelling efficiency of 82%. Note that incomplete reduction of the disulphide bond would lead us to underestimate this value. Because only the tryptophan-containing (AWCWA) peptide has an appreciable UV absorption signal, we were unable to quantify labelling with the other two peptides. However, as the peptide labelling experiments were performed in parallel, and AWCWA is the least soluble of the three, AGCGA and AFCFA are likely to have crosslinked with the same or better efficiencies. ( B ) Stopped flow time traces for the data shown in Figure 7D and panel C . For ease of comparison, data were fitted to a single exponential, then normalised to an amplitude of 1. Note that SecA R20C was not tested with AGCGA or AFCFA, and SecA ∆cys was not tested with any peptide, as it has no cross-linking site. ( C ) Rates of ADP release for SecA R20C alone; with excess SecYEG; and crosslinked to the peptide AWCWA (and in the presence of excess SecYEG). For this position, which is not near the entrance to SecY ( Figure 7A ), the crosslinked peptide has no effect on the rate of ADP release. DOI: http://dx.doi.org/10.7554/eLife.15598.021

Techniques Used: High Performance Liquid Chromatography, Incubation, Flow Cytometry

13) Product Images from "Synthesis and Characterization of Thermoresponsive Hydrogels Based on N-Isopropylacrylamide Crosslinked with 4,4′-Dihydroxybiphenyl Diacrylate"

Article Title: Synthesis and Characterization of Thermoresponsive Hydrogels Based on N-Isopropylacrylamide Crosslinked with 4,4′-Dihydroxybiphenyl Diacrylate

Journal: ACS Omega

doi: 10.1021/acsomega.7b01247

HPLC chromatograms for 4,4′-dihydroxybiphenyl and 44BDA.
Figure Legend Snippet: HPLC chromatograms for 4,4′-dihydroxybiphenyl and 44BDA.

Techniques Used: High Performance Liquid Chromatography

14) Product Images from "Interacting Targets of the Farnesyl of Transducin ?-Subunit "

Article Title: Interacting Targets of the Farnesyl of Transducin ?-Subunit

Journal: Biochemistry

doi: 10.1021/bi800359h

Isolation of Tγ−X product from ROS membranes. (A) Immunoblot patterns of the extracted Tγ−X species. The GTPγS-wash and phosducin-extraction procedures were repeated three and two times, respectively. These aliquots of supernatants (s) and pellets (p) were electrophoresed and transferred to a PVDF membrane for immunostaining. Shown is the clipped image of the anti-Tγ blot at the gel front region. (B) Immunoblot patterns of the fractions eluted from the reverse-phase HPLC as described in Experimental Procedures. Each fraction was subjected to SDS−polyacrylamide gel (12.5%) electrophoresis and immunostaining by anti-Tγ antibody. The fractions containing the Tγ−X product (fractions 25−34) are shown.
Figure Legend Snippet: Isolation of Tγ−X product from ROS membranes. (A) Immunoblot patterns of the extracted Tγ−X species. The GTPγS-wash and phosducin-extraction procedures were repeated three and two times, respectively. These aliquots of supernatants (s) and pellets (p) were electrophoresed and transferred to a PVDF membrane for immunostaining. Shown is the clipped image of the anti-Tγ blot at the gel front region. (B) Immunoblot patterns of the fractions eluted from the reverse-phase HPLC as described in Experimental Procedures. Each fraction was subjected to SDS−polyacrylamide gel (12.5%) electrophoresis and immunostaining by anti-Tγ antibody. The fractions containing the Tγ−X product (fractions 25−34) are shown.

Techniques Used: Isolation, Immunostaining, High Performance Liquid Chromatography, Electrophoresis

(A) Structures of POG-PP [(3-azidophenoxy)geranyl pyrophosphate] and farnesyl pyrophosphate. (B) HPLC analysis of Tγ in each modification step. Unmodified Tβγ-VIS was incubated with yeast FTase in the presence of POG-PP, and aliquots of the reaction mixtures were subjected to reverse-phase HPLC analysis before (trace a) and after (trace b) the POG-transfer reaction. The analysis was also performed following Rce1 treatment (trace c) and Icmt treatment in the presence of AdoMet (trace d). Retinal Tγ was analyzed as a standard (trace e). HPLC analysis was performed as described in Experimental Procedures. Each peak fraction detected by the absorbance at 214 nm was collected and analyzed by MALDI-TOF mass spectrometry with the Voyager-DE (Applied Biosystems) spectrometer. The singly and doubly protonated ion signals of cytochrome c (from horse heart, M r = 12359.7) were used as an internal standard of mass calibration. The observed [M + H] + values of the peak fractions were 8411.0 (trace a), 8681.1 (trace b), 8381.6 (trace c), and 8395.4 (trace d), in good agreement with the calculated [M + H] + values of Tγ-VIS (8411.4), POG-Tγ-VIS (8680.8), POG-Tγ (8381.4), and POG-Tγ-OMe (8395.4), respectively. Due to adsorption, Tβ was not eluted from the column. (C) Time courses of prenyl transfer (panel a), VIS cleavage (panel b), and carboxyl methylation (panel c) reactions catalyzed by FTase, Rce1, and Icmt, respectively.
Figure Legend Snippet: (A) Structures of POG-PP [(3-azidophenoxy)geranyl pyrophosphate] and farnesyl pyrophosphate. (B) HPLC analysis of Tγ in each modification step. Unmodified Tβγ-VIS was incubated with yeast FTase in the presence of POG-PP, and aliquots of the reaction mixtures were subjected to reverse-phase HPLC analysis before (trace a) and after (trace b) the POG-transfer reaction. The analysis was also performed following Rce1 treatment (trace c) and Icmt treatment in the presence of AdoMet (trace d). Retinal Tγ was analyzed as a standard (trace e). HPLC analysis was performed as described in Experimental Procedures. Each peak fraction detected by the absorbance at 214 nm was collected and analyzed by MALDI-TOF mass spectrometry with the Voyager-DE (Applied Biosystems) spectrometer. The singly and doubly protonated ion signals of cytochrome c (from horse heart, M r = 12359.7) were used as an internal standard of mass calibration. The observed [M + H] + values of the peak fractions were 8411.0 (trace a), 8681.1 (trace b), 8381.6 (trace c), and 8395.4 (trace d), in good agreement with the calculated [M + H] + values of Tγ-VIS (8411.4), POG-Tγ-VIS (8680.8), POG-Tγ (8381.4), and POG-Tγ-OMe (8395.4), respectively. Due to adsorption, Tβ was not eluted from the column. (C) Time courses of prenyl transfer (panel a), VIS cleavage (panel b), and carboxyl methylation (panel c) reactions catalyzed by FTase, Rce1, and Icmt, respectively.

Techniques Used: High Performance Liquid Chromatography, Modification, Incubation, Mass Spectrometry, Adsorption, Methylation

15) Product Images from "Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning"

Article Title: Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning

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

doi:

Subunit composition of CMO and M r of the monomer. ( A ) HPLC elution profile of a native CMO preparation (5.4 μg of protein). The cluster of small peaks eluting at ≈17–19 min contained no polypeptides detectable by MALDI-MS. Between analyses of the same preparation, the contaminant peak eluting at ≈15 min varied in size from
Figure Legend Snippet: Subunit composition of CMO and M r of the monomer. ( A ) HPLC elution profile of a native CMO preparation (5.4 μg of protein). The cluster of small peaks eluting at ≈17–19 min contained no polypeptides detectable by MALDI-MS. Between analyses of the same preparation, the contaminant peak eluting at ≈15 min varied in size from

Techniques Used: High Performance Liquid Chromatography, Mass Spectrometry

16) Product Images from "Serelaxin reduces oxidative stress and asymmetric dimethylarginine in angiotensin II-induced hypertension"

Article Title: Serelaxin reduces oxidative stress and asymmetric dimethylarginine in angiotensin II-induced hypertension

Journal: American Journal of Physiology - Renal Physiology

doi: 10.1152/ajprenal.00407.2014

Relaxin reduces plasma asymmetric dimethylarginine (ADMA) levels during high-dose ANG II hypertension. Plasma concentrations of ADMA ( A ) and l -arginine ( B ) as measured by HPLC and the ratio of plasma l -arginine-to-plasma ADMA ( C ) in CON, RLX, ANG, and
Figure Legend Snippet: Relaxin reduces plasma asymmetric dimethylarginine (ADMA) levels during high-dose ANG II hypertension. Plasma concentrations of ADMA ( A ) and l -arginine ( B ) as measured by HPLC and the ratio of plasma l -arginine-to-plasma ADMA ( C ) in CON, RLX, ANG, and

Techniques Used: High Performance Liquid Chromatography

17) Product Images from "Oxytocin and its receptors are synthesized in the rat vasculature"

Article Title: Oxytocin and its receptors are synthesized in the rat vasculature

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

doi:

Reverse-phase HPLC elution of OT immunoreactivity in the rat aorta and vena cava. Tissue extracts, lyophilized and reconstituted in 20% acetonitrile in 0.1% TFA, were applied to a C 18 μBondapak column and eluted with acetonitrile gradient (20–50%) in 0.1% TFA.
Figure Legend Snippet: Reverse-phase HPLC elution of OT immunoreactivity in the rat aorta and vena cava. Tissue extracts, lyophilized and reconstituted in 20% acetonitrile in 0.1% TFA, were applied to a C 18 μBondapak column and eluted with acetonitrile gradient (20–50%) in 0.1% TFA.

Techniques Used: High Performance Liquid Chromatography

18) Product Images from "Proanthocyanidin synthesis in Theobroma cacao: genes encoding anthocyanidin synthase, anthocyanidin reductase, and leucoanthocyanidin reductase"

Article Title: Proanthocyanidin synthesis in Theobroma cacao: genes encoding anthocyanidin synthase, anthocyanidin reductase, and leucoanthocyanidin reductase

Journal: BMC Plant Biology

doi: 10.1186/1471-2229-13-202

Enzymatic assay of recombinant TcLAR. A , HPLC analysis of products from incubation of leucocyanidin with boiled protein as control, monitored by UV spectroscopy. B , as above, for incubation of purified recombinant TcLAR with 3 H-leucocyanidin. C , As in (A) , but monitoring radioactivity of fractions; D , As in (B) , but monitoring radioactivity of fractions; ( E ), UV spectrum of catechin product from (B) ; F , HPLC analysis of an authentic standard of (−)-catechin. mAU, milliabsorbance units; CPM, counts per minute.
Figure Legend Snippet: Enzymatic assay of recombinant TcLAR. A , HPLC analysis of products from incubation of leucocyanidin with boiled protein as control, monitored by UV spectroscopy. B , as above, for incubation of purified recombinant TcLAR with 3 H-leucocyanidin. C , As in (A) , but monitoring radioactivity of fractions; D , As in (B) , but monitoring radioactivity of fractions; ( E ), UV spectrum of catechin product from (B) ; F , HPLC analysis of an authentic standard of (−)-catechin. mAU, milliabsorbance units; CPM, counts per minute.

Techniques Used: Enzymatic Assay, Recombinant, High Performance Liquid Chromatography, Incubation, Spectroscopy, Purification, Radioactivity

Complementation of the Arabidopsis PA-deficient ldox mutant by constitutively expressing TcLAR . A , Catechin and epicatechin standards analyzed by HPLC. B , HPLC analysis of Col-0 young siliques. C , HPLC analysis of ldox 35S:TcLAR Line14 young siliques. D , HPLC analysis of ldox mutant young siliques. E . TcLAR and AtUbiquitin transcripts in total RNA from leaves of ldox 35S:TcLAR transgenic plants, (line 9, line 14 and line 36), Col-O and ldox muant plants by RT-PCR. PCR products from the TcLAR-PGEM plasmid were loaded on the last lane as a positive control for the TcLAR primer set and as a negative control for the AtUbiquitin primer set. F , Catechin and epicatechin levels in young siliques of plants that were the source of the total RNA used in (E) . Catechin and epicatechin levels were determined by extraction and HPLC analysis. The data are presented as means ± SE, n = 3. *P
Figure Legend Snippet: Complementation of the Arabidopsis PA-deficient ldox mutant by constitutively expressing TcLAR . A , Catechin and epicatechin standards analyzed by HPLC. B , HPLC analysis of Col-0 young siliques. C , HPLC analysis of ldox 35S:TcLAR Line14 young siliques. D , HPLC analysis of ldox mutant young siliques. E . TcLAR and AtUbiquitin transcripts in total RNA from leaves of ldox 35S:TcLAR transgenic plants, (line 9, line 14 and line 36), Col-O and ldox muant plants by RT-PCR. PCR products from the TcLAR-PGEM plasmid were loaded on the last lane as a positive control for the TcLAR primer set and as a negative control for the AtUbiquitin primer set. F , Catechin and epicatechin levels in young siliques of plants that were the source of the total RNA used in (E) . Catechin and epicatechin levels were determined by extraction and HPLC analysis. The data are presented as means ± SE, n = 3. *P

Techniques Used: Mutagenesis, Expressing, High Performance Liquid Chromatography, Transgenic Assay, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction, Plasmid Preparation, Positive Control, Negative Control

Expression analysis of key PA biosynthesis genes, and PA composition in various tissues of Theobroma cacao . A , Gene expression levels of TcANR , TcLAR1 and TcLAR1 . Expression was determined by semi-quantitative RT-PCR normalized relative to the expression of TcActin in each sample. B , Levels of soluble PAs expressed as mg PA per g of dry weight. C , Levels of insoluble PAs expressed as mg PA per g of dry weight. D , Catechin and epicatechin standards analyzed by HPLC. E , Representative HPLC analysis of flavan-3-ols extracted from cacao leaves. F , Flavan-3-ol accumulation and composition analyzed by HPLC. All data are presented as means ± SE, for gene expression data, n ≥ 3, for PA level data, n ≥ 5. DW, dry weight.
Figure Legend Snippet: Expression analysis of key PA biosynthesis genes, and PA composition in various tissues of Theobroma cacao . A , Gene expression levels of TcANR , TcLAR1 and TcLAR1 . Expression was determined by semi-quantitative RT-PCR normalized relative to the expression of TcActin in each sample. B , Levels of soluble PAs expressed as mg PA per g of dry weight. C , Levels of insoluble PAs expressed as mg PA per g of dry weight. D , Catechin and epicatechin standards analyzed by HPLC. E , Representative HPLC analysis of flavan-3-ols extracted from cacao leaves. F , Flavan-3-ol accumulation and composition analyzed by HPLC. All data are presented as means ± SE, for gene expression data, n ≥ 3, for PA level data, n ≥ 5. DW, dry weight.

Techniques Used: Expressing, Quantitative RT-PCR, High Performance Liquid Chromatography

19) Product Images from "Killing cancer cells by targeted drug-carrying phage nanomedicines"

Article Title: Killing cancer cells by targeted drug-carrying phage nanomedicines

Journal: BMC Biotechnology

doi: 10.1186/1472-6750-8-37

Controlled release of doxorubicin release from drug-carrying phages . A. The sequence amino-acid sequence (single-letter code) of the g8p coat protein of fUSE5-ZZ-(p8)DFK phages (top) and native fUSE5 (bottom). The mutated residues are marked by black arrows. B. Drawing (not to scale) of a single fUSE5-ZZ-(p8)DFK phage; In the phage scheme on the right, small turquoise spheres represent major coat protein g8p monomers. Purple spheres and sticks represent the 5 copies of minor coat protein g3p, which is fused to a three-color helix representing the IgG binding ZZ domain. The Y shaped structure represents complexed IgG. An engineered g8p monomer is shown on the left. The helix represents a partial structure of a single major coat protein p8, conjugated through an amino terminal aspartate (D) of the sequence DFK carboxyl side chains a molecule of doxorubicin (red). C. A Photograph of the cathepsin-B release experiment tubes, on the right, doxorubicin carrying fUSE5-ZZ-(p8)DFK phages that was incubated with cathepsin-B, followed by PEG/NaCl precipitation, a reddish soluble D-DOX (verified by HPLC and MS in Fig. 5) is seen as well as a reddish pellet representing the drug conjugated through the internal glutamate residue. On the left is a tube containing fUSE5-ZZ phages that was incubated with cathepsin-B, followed by PEG/NaCl precipitation, the transparent colorless solution indicate no drug release.
Figure Legend Snippet: Controlled release of doxorubicin release from drug-carrying phages . A. The sequence amino-acid sequence (single-letter code) of the g8p coat protein of fUSE5-ZZ-(p8)DFK phages (top) and native fUSE5 (bottom). The mutated residues are marked by black arrows. B. Drawing (not to scale) of a single fUSE5-ZZ-(p8)DFK phage; In the phage scheme on the right, small turquoise spheres represent major coat protein g8p monomers. Purple spheres and sticks represent the 5 copies of minor coat protein g3p, which is fused to a three-color helix representing the IgG binding ZZ domain. The Y shaped structure represents complexed IgG. An engineered g8p monomer is shown on the left. The helix represents a partial structure of a single major coat protein p8, conjugated through an amino terminal aspartate (D) of the sequence DFK carboxyl side chains a molecule of doxorubicin (red). C. A Photograph of the cathepsin-B release experiment tubes, on the right, doxorubicin carrying fUSE5-ZZ-(p8)DFK phages that was incubated with cathepsin-B, followed by PEG/NaCl precipitation, a reddish soluble D-DOX (verified by HPLC and MS in Fig. 5) is seen as well as a reddish pellet representing the drug conjugated through the internal glutamate residue. On the left is a tube containing fUSE5-ZZ phages that was incubated with cathepsin-B, followed by PEG/NaCl precipitation, the transparent colorless solution indicate no drug release.

Techniques Used: Sequencing, Binding Assay, Incubation, High Performance Liquid Chromatography, Mass Spectrometry

analysis of the Cathepsin-B released material . A. The crude cathepsin-B released material from re-suspended, PEG-precipitated, cathepsin-B treated, doxorubicin-carrying fUSE5-ZZ-(p8)DFK phages was analysed using a gradient of acetonitrile in water on a Waters HPLC machine (RP; C-18 column) following the doxorubicin specific emission wavelength 480 nm. Cathepsin-B released material eluted at 24–25 minutes post injection. B. The crude cathepsin-B released material was analyzed by MALDI TOF MS . The theoretical mass of the aspartate-doxorubicin (shown in the insert) was observed by the mass spectrometry Analysis as a major peak 656.04 (marked by arrow – corresponding to the weight of aspartate-doxorubicin.
Figure Legend Snippet: analysis of the Cathepsin-B released material . A. The crude cathepsin-B released material from re-suspended, PEG-precipitated, cathepsin-B treated, doxorubicin-carrying fUSE5-ZZ-(p8)DFK phages was analysed using a gradient of acetonitrile in water on a Waters HPLC machine (RP; C-18 column) following the doxorubicin specific emission wavelength 480 nm. Cathepsin-B released material eluted at 24–25 minutes post injection. B. The crude cathepsin-B released material was analyzed by MALDI TOF MS . The theoretical mass of the aspartate-doxorubicin (shown in the insert) was observed by the mass spectrometry Analysis as a major peak 656.04 (marked by arrow – corresponding to the weight of aspartate-doxorubicin.

Techniques Used: High Performance Liquid Chromatography, Injection, Mass Spectrometry

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Article Title: Galloyl-RGD as a new cosmetic ingredient
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Article Title: Hydrophobicity drives the systemic distribution of lipid-conjugated siRNAs via lipid transport pathways
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Article Title: Rat heart: A site of oxytocin production and action
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Irradiation:

Article Title: Photocrosslinking of G-Quadruplex Forming Sequences found in Human Promoters
Article Snippet: .. One μL of 1 U/μL aqueous nuclease P1 from Penicillium citrinum (Sigma) and 1 μL 10 mM ZnCl2 were added to each 100 μL of 50 μM UVB irradiation sample and digested at 37 °C for > 36 h. Reverse-phase HPLC was carried out with an X-Bridge column (C18, 4.6 × 75 mm, 2.5 um, 135 à; Waters Corporation) on a System Gold BioEssential HPLC with a Model 125 binary gradient pump and a Model 168 diode array detector (Beckman Coulter). ..

Article Title: Photocrosslinking of G-Quadruplex Forming Sequences found in Human Promoters
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Flow Cytometry:

Article Title: An [18F]-Positron-Emitting, Fluorescent, Cerebrospinal Fluid Probe for Imaging Damage to the Brain and Spine
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Article Title: Determination of Ghrelin Structure in the Barfin Flounder (Verasper moseri) and Involvement of Ingested Fatty Acids in Ghrelin Acylation
Article Snippet: .. Fractions (1 ml/tube) were collected every minute for 80 min. Fractions showing ghrelin activity were separated by reverse-phase HPLC on a Symmetry300 C18 column (3.9 mm × 150 mm, Waters, Milford, MA, USA); the eluent was a linear gradient of acetonitrile containing 0.1% TFA (10–60% over 40 min; flow rate, 1 ml/min). ..

Radioactivity:

Article Title: An [18F]-Positron-Emitting, Fluorescent, Cerebrospinal Fluid Probe for Imaging Damage to the Brain and Spine
Article Snippet: .. Reverse phase HPLC on a Waters SunfireTM C18 3.5μm 4.6 x 50mm column (186002551), with a 10 min, a10-90% H2 O:ACN (0.05% TFA) gradient and a flow rate of 1 mL/min was used to confirm [18 F]- 2 radiolabeling and purity. .. Reverse phase HPLC analysis of [18 F]- 2 shows a single peak.

Conjugation Assay:

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Synthesized:

Article Title: Galloyl-RGD as a new cosmetic ingredient
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Purification:

Article Title: Galloyl-RGD as a new cosmetic ingredient
Article Snippet: .. Galloyl-RGD synthesis and purification Galloyl-RGD was synthesized with 9-fluorenylmethoxycarbonyl (as an amino acid protector against aminolysis) by solid-phase peptide synthesis, linked with amino acid residues using N-hydroxybenzotriazol-N,N-di-cyclohexylcarbodiimide, and then purified by reverse-phase HPLC (Waters, MA, USA; column: Gemini C18 110 Å 250 × 21.2 mm) (Figure a & b) in a gradient of acetonitrile in 0.1% trifluoroacetic acid. .. A MALDI-TOF mass spectrometry assay (linear mode, α-cyano-4-hydroxy-cinnamic acid matrix) was performed to ensure the synthetic quality of galloyl-RGD (molecular weight and chemical structure).

Activity Assay:

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    Waters Corporation phase high performance liquid chromatography rp hplc hplc analyses
    Reversed phase-high performance liquid chromatography <t>(RP-HPLC)</t> profile of SBP performed on a Waters <t>2545-2767-2489</t> HPLC system fitted with a Waters SunFire C18 column, 19×150 mm.
    Phase High Performance Liquid Chromatography Rp Hplc Hplc Analyses, supplied by Waters Corporation, 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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    <t>RP-HPLC-DAD</t> chromatograms of 7 major compounds. puerarin (1), daidzin (2), liquiritin (3), naringin (4), hesperidin (5), neohesperidin (6), and glycyrrhizin (7) in the standard mixture (A) and SSE sample (B) identified at wavelengths of 254 and 280 nm.
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    Reversed phase-high performance liquid chromatography (RP-HPLC) profile of SBP performed on a Waters 2545-2767-2489 HPLC system fitted with a Waters SunFire C18 column, 19×150 mm.

    Journal: PLoS ONE

    Article Title: Isolation and Characterization of Marine Brevibacillus sp. S-1 Collected from South China Sea and a Novel Antitumor Peptide Produced by the Strain

    doi: 10.1371/journal.pone.0111270

    Figure Lengend Snippet: Reversed phase-high performance liquid chromatography (RP-HPLC) profile of SBP performed on a Waters 2545-2767-2489 HPLC system fitted with a Waters SunFire C18 column, 19×150 mm.

    Article Snippet: Reversed phase-high performance liquid chromatography (RP-HPLC) HPLC analyses on a Waters 2545-2767-2489 HPLC system fitted with a WATERS SunFire C18 column, 19×150 mm. the elution solvent system was composed of water- trifluoroacetic acid (TFA) (solvent A, 100∶0.1, v/v) and acetonitrile (ACN)-TFA (Solvent B, 100∶0.1, v/v).

    Techniques: High Performance Liquid Chromatography

    RP-HPLC-DAD chromatograms of 7 major compounds. puerarin (1), daidzin (2), liquiritin (3), naringin (4), hesperidin (5), neohesperidin (6), and glycyrrhizin (7) in the standard mixture (A) and SSE sample (B) identified at wavelengths of 254 and 280 nm.

    Journal: BMC Complementary and Alternative Medicine

    Article Title: Samsoeum, a traditional herbal medicine, elicits apoptotic and autophagic cell death by inhibiting Akt/mTOR and activating the JNK pathway in cancer cells

    doi: 10.1186/1472-6882-13-233

    Figure Lengend Snippet: RP-HPLC-DAD chromatograms of 7 major compounds. puerarin (1), daidzin (2), liquiritin (3), naringin (4), hesperidin (5), neohesperidin (6), and glycyrrhizin (7) in the standard mixture (A) and SSE sample (B) identified at wavelengths of 254 and 280 nm.

    Article Snippet: Chromatographic conditions The experiments were carried out using RP-HPLC-DAD (reverse phase high-performance liquid chromatography-photoiodide array detector) system consisting of a Waters 2695 Alliance (Milford, MA) separation module and a 966 photodiode array detector.

    Techniques: High Performance Liquid Chromatography

    RP-HPLC analysis of the products in eLOX3 reactions. ( A )12 R -HPETE plus eLOX3. ( B )12 S -HPETE plus eLOX3. ( C )15 S -HPETE plus eLOX3. The products were analyzed by RP-HPLC with a Waters Symmetry C18 5-μm column (0.46 × 25 cm) eluted at a flow rate of 1 ml/min with methanol/water/acetic acid (80:20:0.01 by volume) and UV detection at 205 nm. In A and B , the 12 R -HPETE or 12 S -HPETE substrates (retention time, 18 min) were converted completely and do not appear on the chromatograms. KETE, ketoeicosatetraenoic acid.

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

    Article Title: The lipoxygenase gene ALOXE3 implicated in skin differentiation encodes a hydroperoxide isomerase

    doi: 10.1073/pnas.1633612100

    Figure Lengend Snippet: RP-HPLC analysis of the products in eLOX3 reactions. ( A )12 R -HPETE plus eLOX3. ( B )12 S -HPETE plus eLOX3. ( C )15 S -HPETE plus eLOX3. The products were analyzed by RP-HPLC with a Waters Symmetry C18 5-μm column (0.46 × 25 cm) eluted at a flow rate of 1 ml/min with methanol/water/acetic acid (80:20:0.01 by volume) and UV detection at 205 nm. In A and B , the 12 R -HPETE or 12 S -HPETE substrates (retention time, 18 min) were converted completely and do not appear on the chromatograms. KETE, ketoeicosatetraenoic acid.

    Article Snippet: Based on its chromatographic properties, it is a diastereomer (not the enantiomer) of the major 12 R -HPETE-derived epoxyalcohol; the two separate on RP-HPLC.

    Techniques: High Performance Liquid Chromatography, Flow Cytometry

    HPLC chromatograms of HEA standard solution and the water extract from mycelium of strain 351. Samples were eluted in the mobile phase, which consisted of acetonitrile: double-distilled H 2 O (0.1% acetic acid) (5:95), for 20 min at 25°C. The flow rate was 1 mL/min and the injection volume was 10 μL. HEA was monitored and quantified at 260 nm.

    Journal: Mycology

    Article Title: Beauveria bassiana: a new N6-(2-hydroxyethyl)-adenosine–producing fungus

    doi: 10.1080/21501203.2017.1375040

    Figure Lengend Snippet: HPLC chromatograms of HEA standard solution and the water extract from mycelium of strain 351. Samples were eluted in the mobile phase, which consisted of acetonitrile: double-distilled H 2 O (0.1% acetic acid) (5:95), for 20 min at 25°C. The flow rate was 1 mL/min and the injection volume was 10 μL. HEA was monitored and quantified at 260 nm.

    Article Snippet: The production of HEA was analysed by reversed-phase HPLC using a Waters 2695 Separations Module (Waters Corporation, Milford, CT, USA) equipped with a built-in quaternary pump, a 120 autosampler, the Waters 2998 Photodiode Array Detector and the Empower program for analysing data.

    Techniques: High Performance Liquid Chromatography, Flow Cytometry, Injection