Structured Review

Shimadzu Corporation c18 column
Rechromatography of the subfractions eluted from the fractions VIIIA and VIIIB. ( a ) Subfraction 7. ( b ) Subfraction 9. The <t>C18</t> column (2.1 mm × 250.0 mm, 3.6 μm particles, Phenomenex) was equilibrated with 0.1 % TFA and the proteins were eluted using a concentration gradient from 0 to 100 % of solution B (80 % ACN in 0.1 % TFA), represented by the dashed line. Absorbance was monitored at 214 nm, at 25 °C, using a FPLC Äkta Purifier UPC-10 system. Fractions of 0.3 mL/tube were collected at a flow rate of 0.4 mL/min
C18 Column, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 94/100, based on 131 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/c18 column/product/Shimadzu Corporation
Average 94 stars, based on 131 article reviews
Price from $9.99 to $1999.99
c18 column - by Bioz Stars, 2020-09
94/100 stars

Images

1) Product Images from "Partial purification and functional characterization of Ts19 Frag-I, a novel toxin from Tityus serrulatus scorpion venom"

Article Title: Partial purification and functional characterization of Ts19 Frag-I, a novel toxin from Tityus serrulatus scorpion venom

Journal: The Journal of Venomous Animals and Toxins Including Tropical Diseases

doi: 10.1186/s40409-015-0051-6

Rechromatography of the subfractions eluted from the fractions VIIIA and VIIIB. ( a ) Subfraction 7. ( b ) Subfraction 9. The C18 column (2.1 mm × 250.0 mm, 3.6 μm particles, Phenomenex) was equilibrated with 0.1 % TFA and the proteins were eluted using a concentration gradient from 0 to 100 % of solution B (80 % ACN in 0.1 % TFA), represented by the dashed line. Absorbance was monitored at 214 nm, at 25 °C, using a FPLC Äkta Purifier UPC-10 system. Fractions of 0.3 mL/tube were collected at a flow rate of 0.4 mL/min
Figure Legend Snippet: Rechromatography of the subfractions eluted from the fractions VIIIA and VIIIB. ( a ) Subfraction 7. ( b ) Subfraction 9. The C18 column (2.1 mm × 250.0 mm, 3.6 μm particles, Phenomenex) was equilibrated with 0.1 % TFA and the proteins were eluted using a concentration gradient from 0 to 100 % of solution B (80 % ACN in 0.1 % TFA), represented by the dashed line. Absorbance was monitored at 214 nm, at 25 °C, using a FPLC Äkta Purifier UPC-10 system. Fractions of 0.3 mL/tube were collected at a flow rate of 0.4 mL/min

Techniques Used: Concentration Assay, Fast Protein Liquid Chromatography, Flow Cytometry

Chromatographic profiles of fractions VIIIA and VIIIB from Tsv. ( a ) Fraction VIIIA. ( b ) Fraction VIIIB. Fractions (4 mg, eluted of the cation exchange chromatography from Tityus serrulatus venom) were submitted to RP-FPLC on a C18 column (4.6 mm × 250.0 mm, 5 μm particles, Shimadzu Corp.). The column was equilibrated with 0.1 % trifluoroacetic acid (TFA) and the proteins were eluted using a concentration gradient from 0 to 100 % of solution B (80 % acetonitrile (ACN) in 0.1 % TFA), represented by the dashed line. Absorbance was monitored at 214 nm, at 25 °C, using an FPLC Äkta Purifier UPC-10 system. Fractions of 0.3 mL/tube were collected at a flow rate of 0.7 mL/min
Figure Legend Snippet: Chromatographic profiles of fractions VIIIA and VIIIB from Tsv. ( a ) Fraction VIIIA. ( b ) Fraction VIIIB. Fractions (4 mg, eluted of the cation exchange chromatography from Tityus serrulatus venom) were submitted to RP-FPLC on a C18 column (4.6 mm × 250.0 mm, 5 μm particles, Shimadzu Corp.). The column was equilibrated with 0.1 % trifluoroacetic acid (TFA) and the proteins were eluted using a concentration gradient from 0 to 100 % of solution B (80 % acetonitrile (ACN) in 0.1 % TFA), represented by the dashed line. Absorbance was monitored at 214 nm, at 25 °C, using an FPLC Äkta Purifier UPC-10 system. Fractions of 0.3 mL/tube were collected at a flow rate of 0.7 mL/min

Techniques Used: Chromatography, Fast Protein Liquid Chromatography, Concentration Assay, Flow Cytometry

2) Product Images from "New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom"

Article Title: New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom

Journal: Toxins

doi: 10.3390/toxins10120500

Isolation of Moojase from Bothrops moojeni snake venom. ( A ) Chromatographic profile of B. moojeni crude venom (200 mg) on a CM-sepharose column, equilibrated and eluted with 50 mM ammonium bicarbonate buffer, pH 7.8, followed by a linear gradient of up to 500 mM (solution B). Fractions were collected at a flow rate of 20 mL/h and at room temperature. ( B ) Chromatographic profile of Moojase (2.2 mg) on a C18 reversed-phase column equilibrated and eluted with 0.1% trifluoroacetic acid (TFA), and 70% acetonitrile and 0.1% TFA (solution B). Protein elution was achieved at flow rate of 1 mL/min with a linear concentration gradient of solution B. Insert, 12% SDS-PAGE of the purified Moojase under denaturing and reducing conditions.
Figure Legend Snippet: Isolation of Moojase from Bothrops moojeni snake venom. ( A ) Chromatographic profile of B. moojeni crude venom (200 mg) on a CM-sepharose column, equilibrated and eluted with 50 mM ammonium bicarbonate buffer, pH 7.8, followed by a linear gradient of up to 500 mM (solution B). Fractions were collected at a flow rate of 20 mL/h and at room temperature. ( B ) Chromatographic profile of Moojase (2.2 mg) on a C18 reversed-phase column equilibrated and eluted with 0.1% trifluoroacetic acid (TFA), and 70% acetonitrile and 0.1% TFA (solution B). Protein elution was achieved at flow rate of 1 mL/min with a linear concentration gradient of solution B. Insert, 12% SDS-PAGE of the purified Moojase under denaturing and reducing conditions.

Techniques Used: Isolation, Flow Cytometry, Concentration Assay, SDS Page, Purification

3) Product Images from "Revealing the Function and the Structural Model of Ts4: Insights into the “Non-Toxic” Toxin from Tityus serrulatus Venom"

Article Title: Revealing the Function and the Structural Model of Ts4: Insights into the “Non-Toxic” Toxin from Tityus serrulatus Venom

Journal: Toxins

doi: 10.3390/toxins7072534

Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.
Figure Legend Snippet: Reversed-phase FPLC of fraction VIIIB resulting from the Ts venom fractionation procedure. The fraction VIIIB was submitted to a reversed-phase chromatography on a C18 column (4.6 mm × 250 mm, 5 μm particles) equilibrated with 0.1% ( v / v ) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C.

Techniques Used: Fast Protein Liquid Chromatography, Fractionation, Reversed-phase Chromatography, Concentration Assay, Flow Cytometry

4) Product Images from "Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria"

Article Title: Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria

Journal: Molecules : A Journal of Synthetic Chemistry and Natural Product Chemistry

doi: 10.3390/molecules22111898

Serum stability assays by analytical high-performance liquid chromatography (HPLC). ( A ) p-BthTX-I and ( B ) (p-BthTX-I) 2 were incubated with human serum for the indicated times. Analytical HPLC was performed on a Shimadzu (Kyoto, Japan) system using a C18 column (4.6 × 150 mm, Phenomenex) with a linear gradient of solvent B (5–95%) at 1 mL/min for 15 min (Solvent A: 0.045% trifluoroacetic acid (TFA) in water. Solvent B: 0.036% TFA in acetonitrile). Marked boxes in the figures show the same degradation product produced by both the peptides.
Figure Legend Snippet: Serum stability assays by analytical high-performance liquid chromatography (HPLC). ( A ) p-BthTX-I and ( B ) (p-BthTX-I) 2 were incubated with human serum for the indicated times. Analytical HPLC was performed on a Shimadzu (Kyoto, Japan) system using a C18 column (4.6 × 150 mm, Phenomenex) with a linear gradient of solvent B (5–95%) at 1 mL/min for 15 min (Solvent A: 0.045% trifluoroacetic acid (TFA) in water. Solvent B: 0.036% TFA in acetonitrile). Marked boxes in the figures show the same degradation product produced by both the peptides.

Techniques Used: High Performance Liquid Chromatography, Incubation, Produced

Analytical HPLC comparing the peaks of the peptides (p-BthTX-I) 2 , des-Lys 12 /Lys 13 -(p-BthTX-I) 2 , and des-Lys 1 /Lys 2 -(p-BthTX-I) 2 to the RT of peaks of the stable serum degradation product of (p-BthTX-I) 2 . Samples were eluted at 5 min and 3 h. Analytical HPLC was performed on a Shimadzu system using a C18 column (4.6 × 150 mm, Phenomenex) with a linear gradient of solvent B (5–95%) at 1 mL/min for 30 min (Solvent A: 0.045% trifluoroacetic acid (TFA) in water. Solvent B: 0.036% TFA in acetonitrile). Marked box indicates the peak of des-Lys 12 /Lys 13 -(p-BthTX-I) 2 and the stable degradation peptide produced.
Figure Legend Snippet: Analytical HPLC comparing the peaks of the peptides (p-BthTX-I) 2 , des-Lys 12 /Lys 13 -(p-BthTX-I) 2 , and des-Lys 1 /Lys 2 -(p-BthTX-I) 2 to the RT of peaks of the stable serum degradation product of (p-BthTX-I) 2 . Samples were eluted at 5 min and 3 h. Analytical HPLC was performed on a Shimadzu system using a C18 column (4.6 × 150 mm, Phenomenex) with a linear gradient of solvent B (5–95%) at 1 mL/min for 30 min (Solvent A: 0.045% trifluoroacetic acid (TFA) in water. Solvent B: 0.036% TFA in acetonitrile). Marked box indicates the peak of des-Lys 12 /Lys 13 -(p-BthTX-I) 2 and the stable degradation peptide produced.

Techniques Used: High Performance Liquid Chromatography, Produced

5) Product Images from "Vaccine Containing the Three Allelic Variants of the Plasmodium vivax Circumsporozoite Antigen Induces Protection in Mice after Challenge with a Transgenic Rodent Malaria Parasite"

Article Title: Vaccine Containing the Three Allelic Variants of the Plasmodium vivax Circumsporozoite Antigen Induces Protection in Mice after Challenge with a Transgenic Rodent Malaria Parasite

Journal: Frontiers in Immunology

doi: 10.3389/fimmu.2017.01275

Purification and biochemical characterization of the Plasmodium vivax circumsporozoite protein (CSP) recombinant proteins. (A) 13% SDS-PAGE under reduced conditions stained with Coomassie blue. Proteins migrate between 50 and 55 kDa. Fractions were 2 µg of: (1) yPvCSP-VK210, (2) yPvCSP-VK247, (3) yPvCSP- P. vivax -like, and (4) yPvCSP-All epitopes. (B) Western blot using 1 µg of the same fractions of proteins described above. Antibodies used were monoclonal antibody (MAb) anti-His, MAb VK210 (2F2), and MAb VK247 (2E10.E9). The secondary antibody used was anti-mouse IgG HRP-labeled, and detection was performed by ECL assay. (C) The purity of proteins, after the combination of chromatographic methods, was analyzed by reverse-phase high-performance liquid chromatography (RP-HPLC), in which the gradient elution was developed combining 0.1% trifluoroacetic acid (TFA) in water and 0.1% TFA in 90% acetonitrile, 24°C, 1 mL/min for 40 min, in a C18 column.
Figure Legend Snippet: Purification and biochemical characterization of the Plasmodium vivax circumsporozoite protein (CSP) recombinant proteins. (A) 13% SDS-PAGE under reduced conditions stained with Coomassie blue. Proteins migrate between 50 and 55 kDa. Fractions were 2 µg of: (1) yPvCSP-VK210, (2) yPvCSP-VK247, (3) yPvCSP- P. vivax -like, and (4) yPvCSP-All epitopes. (B) Western blot using 1 µg of the same fractions of proteins described above. Antibodies used were monoclonal antibody (MAb) anti-His, MAb VK210 (2F2), and MAb VK247 (2E10.E9). The secondary antibody used was anti-mouse IgG HRP-labeled, and detection was performed by ECL assay. (C) The purity of proteins, after the combination of chromatographic methods, was analyzed by reverse-phase high-performance liquid chromatography (RP-HPLC), in which the gradient elution was developed combining 0.1% trifluoroacetic acid (TFA) in water and 0.1% TFA in 90% acetonitrile, 24°C, 1 mL/min for 40 min, in a C18 column.

Techniques Used: Purification, Recombinant, SDS Page, Staining, Western Blot, Labeling, High Performance Liquid Chromatography

6) Product Images from "Purification and Characterization of a Novel Antiplatelet Peptide from Deinagkistrodon acutus Venom"

Article Title: Purification and Characterization of a Novel Antiplatelet Peptide from Deinagkistrodon acutus Venom

Journal: Toxins

doi: 10.3390/toxins10080332

Bioassay-directed chromatographic separation of anti-platelet aggregation peptide. ( a ) The lyophilized percolate ( D. acutus venom) was separated on a semi-preparative RP-HPLC column (Hedera ODS-2; 250 × 20 mm, 5 µm) in the BioLogic Duoflow system (Bio-Rad, Redmond, WA, USA) using acetonitrile as the organic modifier and trifluoroacetic acid (TFA) as the ion-pairing reagent. ( b ) Inhibitory activities of fractions 1–5 against thrombin-induced platelet aggregation. Platelet aggregation inhibition rate (%) = [(X−Y)/X]×100, where X represents the maximum aggregation rate of saline-treated gel-filtered platelet and Y represents the maximum aggregation rate of sample-treated gel-filtered platelet. ( c – e ) The Fractions 3, 4, and 5 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). ( f – h ) Inhibitory activities of fractions 3.1–3.5, 4.1–4.4, and 5.1–5.5 against thrombin-induced platelet aggregation. ( i – k ) The Fractions 3.5, 4.2, and 4.4 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). Data are presented as means ± SD ( n = 3).
Figure Legend Snippet: Bioassay-directed chromatographic separation of anti-platelet aggregation peptide. ( a ) The lyophilized percolate ( D. acutus venom) was separated on a semi-preparative RP-HPLC column (Hedera ODS-2; 250 × 20 mm, 5 µm) in the BioLogic Duoflow system (Bio-Rad, Redmond, WA, USA) using acetonitrile as the organic modifier and trifluoroacetic acid (TFA) as the ion-pairing reagent. ( b ) Inhibitory activities of fractions 1–5 against thrombin-induced platelet aggregation. Platelet aggregation inhibition rate (%) = [(X−Y)/X]×100, where X represents the maximum aggregation rate of saline-treated gel-filtered platelet and Y represents the maximum aggregation rate of sample-treated gel-filtered platelet. ( c – e ) The Fractions 3, 4, and 5 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). ( f – h ) Inhibitory activities of fractions 3.1–3.5, 4.1–4.4, and 5.1–5.5 against thrombin-induced platelet aggregation. ( i – k ) The Fractions 3.5, 4.2, and 4.4 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). Data are presented as means ± SD ( n = 3).

Techniques Used: High Performance Liquid Chromatography, Inhibition

7) Product Images from "Synergic effects between ocellatin-F1 and bufotenine on the inhibition of BHK-21 cellular infection by the rabies virus"

Article Title: Synergic effects between ocellatin-F1 and bufotenine on the inhibition of BHK-21 cellular infection by the rabies virus

Journal: The Journal of Venomous Animals and Toxins Including Tropical Diseases

doi: 10.1186/s40409-015-0048-1

Representative RP-HPLC profile of the pooled filtered skin secretion of L. labyrinthicus. RP-HPLC profile of L. labyrinthicus skin secretion in a C18 monolithic column monitored at 214 nm. Numbers 1–16 represent the sixteen fractions manually collected for the antiviral screening; the arrow indicates the active fraction. Inset: superimposed individual chromatographic profiles of the filtered skin secretions from three individuals, under the same chromatographic conditions
Figure Legend Snippet: Representative RP-HPLC profile of the pooled filtered skin secretion of L. labyrinthicus. RP-HPLC profile of L. labyrinthicus skin secretion in a C18 monolithic column monitored at 214 nm. Numbers 1–16 represent the sixteen fractions manually collected for the antiviral screening; the arrow indicates the active fraction. Inset: superimposed individual chromatographic profiles of the filtered skin secretions from three individuals, under the same chromatographic conditions

Techniques Used: High Performance Liquid Chromatography

8) Product Images from "Electrophysiological Characterization of Ts6 and Ts7, K+ Channel Toxins Isolated through an Improved Tityus serrulatus Venom Purification Procedure"

Article Title: Electrophysiological Characterization of Ts6 and Ts7, K+ Channel Toxins Isolated through an Improved Tityus serrulatus Venom Purification Procedure

Journal: Toxins

doi: 10.3390/toxins6030892

Reversed-phase FPLC of fractions X and XIIA resulting from the improved Ts venom fractionation procedure. The fractions were purified on a C18 column (4.6 mm × 250 mm, 5 µm particles) equilibrated with 0.1% (v/v) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C. ( A ) Fraction X; ( B ) Fraction XIIA.
Figure Legend Snippet: Reversed-phase FPLC of fractions X and XIIA resulting from the improved Ts venom fractionation procedure. The fractions were purified on a C18 column (4.6 mm × 250 mm, 5 µm particles) equilibrated with 0.1% (v/v) of trifluoroacetic acid (TFA). Adsorbed proteins were eluted using a concentration gradient from 0% to 100% of solution B (80% acetonitrile in 0.1% TFA), represented by the dotted line. Flow: 0.8 mL/min. Absorbance was monitored at 214 nm, at 25 °C. ( A ) Fraction X; ( B ) Fraction XIIA.

Techniques Used: Fast Protein Liquid Chromatography, Fractionation, Purification, Concentration Assay, Flow Cytometry

9) Product Images from "New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom"

Article Title: New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom

Journal: Toxins

doi: 10.3390/toxins10120500

Isolation of Moojase from Bothrops moojeni snake venom. ( A ) Chromatographic profile of B. moojeni crude venom (200 mg) on a CM-sepharose column, equilibrated and eluted with 50 mM ammonium bicarbonate buffer, pH 7.8, followed by a linear gradient of up to 500 mM (solution B). Fractions were collected at a flow rate of 20 mL/h and at room temperature. ( B ) Chromatographic profile of Moojase (2.2 mg) on a C18 reversed-phase column equilibrated and eluted with 0.1% trifluoroacetic acid (TFA), and 70% acetonitrile and 0.1% TFA (solution B). Protein elution was achieved at flow rate of 1 mL/min with a linear concentration gradient of solution B. Insert, 12% SDS-PAGE of the purified Moojase under denaturing and reducing conditions.
Figure Legend Snippet: Isolation of Moojase from Bothrops moojeni snake venom. ( A ) Chromatographic profile of B. moojeni crude venom (200 mg) on a CM-sepharose column, equilibrated and eluted with 50 mM ammonium bicarbonate buffer, pH 7.8, followed by a linear gradient of up to 500 mM (solution B). Fractions were collected at a flow rate of 20 mL/h and at room temperature. ( B ) Chromatographic profile of Moojase (2.2 mg) on a C18 reversed-phase column equilibrated and eluted with 0.1% trifluoroacetic acid (TFA), and 70% acetonitrile and 0.1% TFA (solution B). Protein elution was achieved at flow rate of 1 mL/min with a linear concentration gradient of solution B. Insert, 12% SDS-PAGE of the purified Moojase under denaturing and reducing conditions.

Techniques Used: Isolation, Flow Cytometry, Concentration Assay, SDS Page, Purification

10) Product Images from "Purification and Characterization of a Novel Antiplatelet Peptide from Deinagkistrodon acutus Venom"

Article Title: Purification and Characterization of a Novel Antiplatelet Peptide from Deinagkistrodon acutus Venom

Journal: Toxins

doi: 10.3390/toxins10080332

Bioassay-directed chromatographic separation of anti-platelet aggregation peptide. ( a ) The lyophilized percolate ( D. acutus venom) was separated on a semi-preparative RP-HPLC column (Hedera ODS-2; 250 × 20 mm, 5 µm) in the BioLogic Duoflow system (Bio-Rad, Redmond, WA, USA) using acetonitrile as the organic modifier and trifluoroacetic acid (TFA) as the ion-pairing reagent. ( b ) Inhibitory activities of fractions 1–5 against thrombin-induced platelet aggregation. Platelet aggregation inhibition rate (%) = [(X−Y)/X]×100, where X represents the maximum aggregation rate of saline-treated gel-filtered platelet and Y represents the maximum aggregation rate of sample-treated gel-filtered platelet. ( c – e ) The Fractions 3, 4, and 5 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). ( f – h ) Inhibitory activities of fractions 3.1–3.5, 4.1–4.4, and 5.1–5.5 against thrombin-induced platelet aggregation. ( i – k ) The Fractions 3.5, 4.2, and 4.4 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). Data are presented as means ± SD ( n = 3).
Figure Legend Snippet: Bioassay-directed chromatographic separation of anti-platelet aggregation peptide. ( a ) The lyophilized percolate ( D. acutus venom) was separated on a semi-preparative RP-HPLC column (Hedera ODS-2; 250 × 20 mm, 5 µm) in the BioLogic Duoflow system (Bio-Rad, Redmond, WA, USA) using acetonitrile as the organic modifier and trifluoroacetic acid (TFA) as the ion-pairing reagent. ( b ) Inhibitory activities of fractions 1–5 against thrombin-induced platelet aggregation. Platelet aggregation inhibition rate (%) = [(X−Y)/X]×100, where X represents the maximum aggregation rate of saline-treated gel-filtered platelet and Y represents the maximum aggregation rate of sample-treated gel-filtered platelet. ( c – e ) The Fractions 3, 4, and 5 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). ( f – h ) Inhibitory activities of fractions 3.1–3.5, 4.1–4.4, and 5.1–5.5 against thrombin-induced platelet aggregation. ( i – k ) The Fractions 3.5, 4.2, and 4.4 were separated on an analytical RP-HPLC column (Diamonsill C18; 4.6 × 250 mm, 5 µm). Data are presented as means ± SD ( n = 3).

Techniques Used: High Performance Liquid Chromatography, Inhibition

Related Articles

High Performance Liquid Chromatography:

Article Title: New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom
Article Snippet: .. The fraction of interest was then submitted to reverse-phase chromatography on a C18 column (CLC-ODS, 0.46 × 25 cm, Shimadzu, Kyoto, Japan) using a HPLC system (Shimadzu). .. The column was equilibrated with 0.1% trifluoroacetic acid (TFA, solvent A) and elution was carried out at a flow rate of 1 mL/min and a linear concentration gradient of 70% acetonitrile and 0.1% TFA (solvent B), as follows: 0% B for 0–10 min, 0–100% B for 10–70 min, and 100% B for 70–80 min. All peaks were monitored by measuring the absorbance at 280 nm.

Article Title: Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria
Article Snippet: .. Liquid chromatography-mass spectrometry (LC/MS) was performed using a C18 column (2.0 × 30 mm, Shimadzu) attached to analytical HPLC and an amaZon ion trap mass spectrometer (Bruker Daltonics) using ESI. ..

Article Title: Vaccine Containing the Three Allelic Variants of the Plasmodium vivax Circumsporozoite Antigen Induces Protection in Mice after Challenge with a Transgenic Rodent Malaria Parasite
Article Snippet: .. Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) Purified proteins were analyzed by RP-HPLC using a C18 column (4.6 × 250 mm; 300 µm particle size) coupled to an HPLC LCMS-2020 LC/MS system (Shimadzu, Kyoto, Japan). .. The HPLC procedure was performed at RT (≈25°C) using a binary gradient of 0.1% trifluoroacetic acid (TFA, Solvent A) and 0.1% TFA in a 9:1 (v/v) solution of acetonitrile:water (Solvent B) with a two-step solvent gradient starting at 0–20%, followed by 20–100%, at a rate of 1 mL/min for 40 min.

Article Title: Purification and Characterization of a Novel Antiplatelet Peptide from Deinagkistrodon acutus Venom
Article Snippet: .. They were further isolated by an analytical C18 column (4.6 × 250 mm) using a Shimadzu LC-20AT HPLC system ( c–e). .. Each fraction was collected and tested for antiplatelet aggregation activity ( f–h).

Flow Cytometry:

Article Title: Electrophysiological Characterization of Ts6 and Ts7, K+ Channel Toxins Isolated through an Improved Tityus serrulatus Venom Purification Procedure
Article Snippet: .. RP-FPLC of each fraction was performed in an Äkta Purifier UPC-10 system (GE Healthcare, Uppsala, Sweden), using a 4.6 mm × 250.0 mm C18 column (Shimadzu Corp., Kyoto, Japan) equilibrated with 0.1% (v/v) trifluoroacetic acid (TFA) at a flow rate of 0.8 mL/min. ..

Article Title: Revealing the Function and the Structural Model of Ts4: Insights into the “Non-Toxic” Toxin from Tityus serrulatus Venom
Article Snippet: .. RP-FPLC of the fraction VIIIB was performed in an Äkta Purifier UPC-10 system (GE Healthcare, Uppsala, Sweden), using a 4.6 mm × 250.0 mm C18 column (Shimadzu Corp., Kyoto, Kansai, Japan) equilibrated with 0.1% (v /v ) trifluoroacetic acid (TFA, Avantor Performance Materials Inc., Center Valley, PA, USA) at a flow rate of 0.8 mL/min. .. The samples were eluted with steps of concentration gradient from 0 to 100% of solution B (80% acetonitrile (Avantor Performance Materials Inc., Center Valley, PA, USA) in 0.1% TFA), at a flow rate of 0.8 mL/min.

Mass Spectrometry:

Article Title: Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria
Article Snippet: .. Liquid chromatography-mass spectrometry (LC/MS) was performed using a C18 column (2.0 × 30 mm, Shimadzu) attached to analytical HPLC and an amaZon ion trap mass spectrometer (Bruker Daltonics) using ESI. ..

Chromatography:

Article Title: Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria
Article Snippet: .. Liquid chromatography-mass spectrometry (LC/MS) was performed using a C18 column (2.0 × 30 mm, Shimadzu) attached to analytical HPLC and an amaZon ion trap mass spectrometer (Bruker Daltonics) using ESI. ..

Isolation:

Article Title: Purification and Characterization of a Novel Antiplatelet Peptide from Deinagkistrodon acutus Venom
Article Snippet: .. They were further isolated by an analytical C18 column (4.6 × 250 mm) using a Shimadzu LC-20AT HPLC system ( c–e). .. Each fraction was collected and tested for antiplatelet aggregation activity ( f–h).

Purification:

Article Title: Vaccine Containing the Three Allelic Variants of the Plasmodium vivax Circumsporozoite Antigen Induces Protection in Mice after Challenge with a Transgenic Rodent Malaria Parasite
Article Snippet: .. Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) Purified proteins were analyzed by RP-HPLC using a C18 column (4.6 × 250 mm; 300 µm particle size) coupled to an HPLC LCMS-2020 LC/MS system (Shimadzu, Kyoto, Japan). .. The HPLC procedure was performed at RT (≈25°C) using a binary gradient of 0.1% trifluoroacetic acid (TFA, Solvent A) and 0.1% TFA in a 9:1 (v/v) solution of acetonitrile:water (Solvent B) with a two-step solvent gradient starting at 0–20%, followed by 20–100%, at a rate of 1 mL/min for 40 min.

Liquid Chromatography with Mass Spectroscopy:

Article Title: Antibacterial Activity of the Non-Cytotoxic Peptide (p-BthTX-I)2 and Its Serum Degradation Product against Multidrug-Resistant Bacteria
Article Snippet: .. Liquid chromatography-mass spectrometry (LC/MS) was performed using a C18 column (2.0 × 30 mm, Shimadzu) attached to analytical HPLC and an amaZon ion trap mass spectrometer (Bruker Daltonics) using ESI. ..

Article Title: Vaccine Containing the Three Allelic Variants of the Plasmodium vivax Circumsporozoite Antigen Induces Protection in Mice after Challenge with a Transgenic Rodent Malaria Parasite
Article Snippet: .. Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) Purified proteins were analyzed by RP-HPLC using a C18 column (4.6 × 250 mm; 300 µm particle size) coupled to an HPLC LCMS-2020 LC/MS system (Shimadzu, Kyoto, Japan). .. The HPLC procedure was performed at RT (≈25°C) using a binary gradient of 0.1% trifluoroacetic acid (TFA, Solvent A) and 0.1% TFA in a 9:1 (v/v) solution of acetonitrile:water (Solvent B) with a two-step solvent gradient starting at 0–20%, followed by 20–100%, at a rate of 1 mL/min for 40 min.

Reversed-phase Chromatography:

Article Title: New Insights on Moojase, a Thrombin-Like Serine Protease from Bothrops moojeni Snake Venom
Article Snippet: .. The fraction of interest was then submitted to reverse-phase chromatography on a C18 column (CLC-ODS, 0.46 × 25 cm, Shimadzu, Kyoto, Japan) using a HPLC system (Shimadzu). .. The column was equilibrated with 0.1% trifluoroacetic acid (TFA, solvent A) and elution was carried out at a flow rate of 1 mL/min and a linear concentration gradient of 70% acetonitrile and 0.1% TFA (solvent B), as follows: 0% B for 0–10 min, 0–100% B for 10–70 min, and 100% B for 70–80 min. All peaks were monitored by measuring the absorbance at 280 nm.

Article Title: Partial purification and functional characterization of Ts19 Frag-I, a novel toxin from Tityus serrulatus scorpion venom
Article Snippet: .. The fractions VIIIA and VIIIB (4 mg) were submitted to reversed-phase chromatography using a 4.6 mm × 250.0 mm C18 column (5 μm particles, Shimadzu Corp., Japan); the eluted subfractions were rechromatographed on a 2.1 mm × 250.0 mm C18 column (3.6 μm particles, Phenomenex, USA). .. Both reversed-phase columns were equilibrated with 0.1 % (V/V) trifluoroacetic acid (TFA) and the subfractions were eluted using a concentration gradient from 0 to 100 % of solution B (80 % acetonitrile in 0.1% TFA).

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 84
    Shimadzu Corporation semi preparative c18 shim pak vp ods column
    Purification and purity of synthetic peptides PepTry and PepChy. (A,C) Reverse-phase chromatography of PepTry and PepChy, respectively, on a <t>C18</t> <t>Shim-pak</t> <t>VP-ODS</t> column using a linear gradient (5–95%) of acetonitrile. PepTry and PepChy were eluted at 10.5 minutes and 12.0 minutes and 50% and 55% ACN, respectively. (B , D) EIS-MS spectrometry analysis of PepTry (molecular mass of 974.5 Da) and PepChy (molecular mass of 967.35 Da), respectively. In sets : structures of PepTry and PepChy from crystal structure of BTCI 19 (PDB code 2G81).
    Semi Preparative C18 Shim Pak Vp Ods Column, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 84/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/semi preparative c18 shim pak vp ods column/product/Shimadzu Corporation
    Average 84 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    semi preparative c18 shim pak vp ods column - by Bioz Stars, 2020-09
    84/100 stars
      Buy from Supplier

    85
    Shimadzu Corporation vp ods c18 column
    HPLC analysis of ( A ) rosmarinic acid from Z. marina and ( B ) rosmarinic acid standard. The samples were passed through reversed phase column <t>VP-ODS</t> <t>C18</t> (150 × 4 mm) at 1 mL/min. Chromatograms were monitored at 330 nm, and the mobile phase was methanol/water/acetic acid (55:44.9:0.1, v:v:v). The experiment was carried out at 30 °C. The retention time of rosmarinic acid was approximately 8.9 min.
    Vp Ods C18 Column, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/vp ods c18 column/product/Shimadzu Corporation
    Average 85 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    vp ods c18 column - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

    90
    Shimadzu Corporation shim pack gis c18 preparative column
    Chromatography of A 1a separated by a Shim-pack <t>GIS</t> <t>C18.</t> Liner gradient was 5%–30% acetonitrile containing 0.1% TFA from 0 to 30 min.
    Shim Pack Gis C18 Preparative Column, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/shim pack gis c18 preparative column/product/Shimadzu Corporation
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    shim pack gis c18 preparative column - by Bioz Stars, 2020-09
    90/100 stars
      Buy from Supplier

    93
    Shimadzu Corporation hplc system
    <t>HPLC</t> monitoring of coupling reaction between 18 F-sugar and 5-Iodo-uracil, heated using microwave for 15 min. Method 1 (details in method section), <t>0.05%TFA</t> in water/AcCN as mobile phase. Red line: sample was from radiosynthesis; Black line: sample from
    Hplc System, supplied by Shimadzu Corporation, used in various techniques. Bioz Stars score: 93/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hplc system/product/Shimadzu Corporation
    Average 93 stars, based on 13 article reviews
    Price from $9.99 to $1999.99
    hplc system - by Bioz Stars, 2020-09
    93/100 stars
      Buy from Supplier

    Image Search Results


    Purification and purity of synthetic peptides PepTry and PepChy. (A,C) Reverse-phase chromatography of PepTry and PepChy, respectively, on a C18 Shim-pak VP-ODS column using a linear gradient (5–95%) of acetonitrile. PepTry and PepChy were eluted at 10.5 minutes and 12.0 minutes and 50% and 55% ACN, respectively. (B , D) EIS-MS spectrometry analysis of PepTry (molecular mass of 974.5 Da) and PepChy (molecular mass of 967.35 Da), respectively. In sets : structures of PepTry and PepChy from crystal structure of BTCI 19 (PDB code 2G81).

    Journal: Scientific Reports

    Article Title: Blood pressure-lowering effects of a Bowman-Birk inhibitor and its derived peptides in normotensive and hypertensive rats

    doi: 10.1038/s41598-020-66624-3

    Figure Lengend Snippet: Purification and purity of synthetic peptides PepTry and PepChy. (A,C) Reverse-phase chromatography of PepTry and PepChy, respectively, on a C18 Shim-pak VP-ODS column using a linear gradient (5–95%) of acetonitrile. PepTry and PepChy were eluted at 10.5 minutes and 12.0 minutes and 50% and 55% ACN, respectively. (B , D) EIS-MS spectrometry analysis of PepTry (molecular mass of 974.5 Da) and PepChy (molecular mass of 967.35 Da), respectively. In sets : structures of PepTry and PepChy from crystal structure of BTCI 19 (PDB code 2G81).

    Article Snippet: Peptides were purified by reverse-phase high performance liquid chromatography, RP-HPLC (Class LC-20A from Shimadzu Corp., Kyoto, Japan), using a semi-preparative C18 Shim-pak VP-ODS column (5 µm, 4.6 × 250 mm) (Shimadzu Corp., Kyoto, Japan) with a linear gradient (5–45%) of ACN.

    Techniques: Purification, Reversed-phase Chromatography, Impedance Spectroscopy

    HPLC analysis of ( A ) rosmarinic acid from Z. marina and ( B ) rosmarinic acid standard. The samples were passed through reversed phase column VP-ODS C18 (150 × 4 mm) at 1 mL/min. Chromatograms were monitored at 330 nm, and the mobile phase was methanol/water/acetic acid (55:44.9:0.1, v:v:v). The experiment was carried out at 30 °C. The retention time of rosmarinic acid was approximately 8.9 min.

    Journal: Marine Drugs

    Article Title: Rosmarinic Acid from Eelgrass Shows Nematicidal and Antibacterial Activities against Pine Wood Nematode and Its Carrying Bacteria

    doi: 10.3390/md10122729

    Figure Lengend Snippet: HPLC analysis of ( A ) rosmarinic acid from Z. marina and ( B ) rosmarinic acid standard. The samples were passed through reversed phase column VP-ODS C18 (150 × 4 mm) at 1 mL/min. Chromatograms were monitored at 330 nm, and the mobile phase was methanol/water/acetic acid (55:44.9:0.1, v:v:v). The experiment was carried out at 30 °C. The retention time of rosmarinic acid was approximately 8.9 min.

    Article Snippet: HPLC Analysis The light yellow crystal was dissolved in ethanol and analyzed by high-performance liquid chromatography on a VP-ODS C18 column (150 × 4 nm, Shimadzu) at 1 mL/min.

    Techniques: High Performance Liquid Chromatography

    Chromatography of A 1a separated by a Shim-pack GIS C18. Liner gradient was 5%–30% acetonitrile containing 0.1% TFA from 0 to 30 min.

    Journal: Marine Drugs

    Article Title: Purification of Antioxidant Peptides by High Resolution Mass Spectrometry from Simulated Gastrointestinal Digestion Hydrolysates of Alaska Pollock (Theragra chalcogramma) Skin Collagen

    doi: 10.3390/md14100186

    Figure Lengend Snippet: Chromatography of A 1a separated by a Shim-pack GIS C18. Liner gradient was 5%–30% acetonitrile containing 0.1% TFA from 0 to 30 min.

    Article Snippet: The highest active faction after Sephadex G-15 was further purified by preparative high performance liquid on a Shim-pack GIS C18 preparative column (Φ 20 mm × 250 mm, Shimadzu, Kyoto, Japan).

    Techniques: Chromatography

    HPLC monitoring of coupling reaction between 18 F-sugar and 5-Iodo-uracil, heated using microwave for 15 min. Method 1 (details in method section), 0.05%TFA in water/AcCN as mobile phase. Red line: sample was from radiosynthesis; Black line: sample from

    Journal: Nuclear medicine and biology

    Article Title: An improved strategy for the synthesis of [18F]-labeled arabinofuranosyl nuclosides

    doi: 10.1016/j.nucmedbio.2012.06.008

    Figure Lengend Snippet: HPLC monitoring of coupling reaction between 18 F-sugar and 5-Iodo-uracil, heated using microwave for 15 min. Method 1 (details in method section), 0.05%TFA in water/AcCN as mobile phase. Red line: sample was from radiosynthesis; Black line: sample from

    Article Snippet: An aliquot of the crude 4 or the purified [18 F]-FXAU was characterized with analytical HPLC system ( Method 3 , column: Alltima HP C18 (250 mm × 4.6 mm) flow rate: 1 mL/min; mobile phase: 0.1% TFA in water and AcCN; gradient: 0–2 min, 2–10% AcCN, 14 min, 10% AcCN, 14–16.5 min, 10–100% AcCN, 24 min, 100% AcCN, 25 min, 2% AcCN).

    Techniques: High Performance Liquid Chromatography