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Agilent technologies preparative hplc
<t>HPLC</t> chromatogram of <t>T65</t> embedded SBA-15 for sustainable control release test. ( a ) 0 day, ( b ) first day, ( c ) second day, and ( d ) third day.
Preparative Hplc, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 96/100, based on 285 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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preparative hplc - by Bioz Stars, 2020-11
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1) Product Images from "Development of Multifunctional Cosmetic Cream Using Bioactive Materials from Streptomyces sp. T65 with Synthesized Mesoporous Silica Particles SBA-15"

Article Title: Development of Multifunctional Cosmetic Cream Using Bioactive Materials from Streptomyces sp. T65 with Synthesized Mesoporous Silica Particles SBA-15

Journal: Antioxidants

doi: 10.3390/antiox9040278

HPLC chromatogram of T65 embedded SBA-15 for sustainable control release test. ( a ) 0 day, ( b ) first day, ( c ) second day, and ( d ) third day.
Figure Legend Snippet: HPLC chromatogram of T65 embedded SBA-15 for sustainable control release test. ( a ) 0 day, ( b ) first day, ( c ) second day, and ( d ) third day.

Techniques Used: High Performance Liquid Chromatography

2) Product Images from "Identification, Characterization and Synthesis of Walterospermin, a Sperm Motility Activator from the Egyptian Black Snake Walterinnesia aegyptia Venom"

Article Title: Identification, Characterization and Synthesis of Walterospermin, a Sperm Motility Activator from the Egyptian Black Snake Walterinnesia aegyptia Venom

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms21207786

Coelution of synthetic and natural walterospermin and disulfide bridge assignment. ( A ) Coelution experiment. Natural (blue) and synthetic (red) walterospermin elution profiles are shown after separation on analytical RP-HPLC (AdvanceBio Peptide Map 2.1 × 250 mm, 2.7 µm from Agilent Technologies). The ACN gradient is shown as dashed line. ( B ) HPLC-UV (214 nm) trace of walterospermin after partial reduction and alkylation. Peak 1: folded walterospermin; peak 2-4: walterospermin with one reduced/alkylated bridge; peak 5–7: walterospermin with two reduced/alkylated bridge; peak 8: fully reduced/alkylated peptides. ( C ) Sequence coverage obtained by LC-ESI-MS(/MS) analyses of (a) tryptic and (b) chymotryptic digests of intermediates 2-4 containing N-propyl-maleimide (NPM) and N-ethyl-maleimide (NEM). Blue lines indicate peptide sequences analyzed. Yellow and red labels indicate NPM and NEM derivates, respectively. ( D ) Disulfide bridge arrangement of synthetic walterospermin. Cysteines were numbered by their order of appearance in the sequence. Underlined sequence corresponds to the active site of Kunitz-type protease inhibitors.
Figure Legend Snippet: Coelution of synthetic and natural walterospermin and disulfide bridge assignment. ( A ) Coelution experiment. Natural (blue) and synthetic (red) walterospermin elution profiles are shown after separation on analytical RP-HPLC (AdvanceBio Peptide Map 2.1 × 250 mm, 2.7 µm from Agilent Technologies). The ACN gradient is shown as dashed line. ( B ) HPLC-UV (214 nm) trace of walterospermin after partial reduction and alkylation. Peak 1: folded walterospermin; peak 2-4: walterospermin with one reduced/alkylated bridge; peak 5–7: walterospermin with two reduced/alkylated bridge; peak 8: fully reduced/alkylated peptides. ( C ) Sequence coverage obtained by LC-ESI-MS(/MS) analyses of (a) tryptic and (b) chymotryptic digests of intermediates 2-4 containing N-propyl-maleimide (NPM) and N-ethyl-maleimide (NEM). Blue lines indicate peptide sequences analyzed. Yellow and red labels indicate NPM and NEM derivates, respectively. ( D ) Disulfide bridge arrangement of synthetic walterospermin. Cysteines were numbered by their order of appearance in the sequence. Underlined sequence corresponds to the active site of Kunitz-type protease inhibitors.

Techniques Used: High Performance Liquid Chromatography, Sequencing, Tandem Mass Spectroscopy

3) Product Images from "Culture-independent discovery of the malacidins as calcium-dependent antibiotics with activity against multidrug-resistant Gram-positive pathogens"

Article Title: Culture-independent discovery of the malacidins as calcium-dependent antibiotics with activity against multidrug-resistant Gram-positive pathogens

Journal: Nature microbiology

doi: 10.1038/s41564-018-0110-1

Maladicin biosynthesis, heterologous expression and structure (a) The malacidin biosynthetic gene cluster was recovered on three overlapping cosmid clones and (b) assembled from these three overlapping clones in yeast using transformation-associated recombination (TAR). The resulting bacterial artificial chromosome (BAC) was integrated into S. albus genome for heterologous expression studies. (c) A representative HPLC analysis of crude extracts derived from cultures of S. albus transformed with the malacidin biosynthetic gene cluster (BGC) shows the presence of BGC-specific small molecules. The two primary malacidin peaks are highlighted with an asterisk. (d) Unlike crude extracts of the S. albus host strain alone, only extracts from the S. albus harboring the malacidin BGC showed antibacterial activity when applied to a lawn of S. aureus USA300. Both the (c) HPLC analysis and (d) antibacterial activity are representative of 4 independent fermentations. (e) Malacidin A and B are cyclic lipopeptides containing 8 amino acid macrocycles and polyunsaturated lipids. The malacidins do not contain the conserved DXDG motif seen in all known calcium-dependent antibiotics – incorporating a rare 3-hydroxyl aspartic acid (HyAsp, highlighted in violet) and lacking the spacer residue. Biosynthetic enzymes predicted to be involved in the production of non-proteinogenic amino acid [3-methyl aspartic acid (MeAsp), 4-methyl proline (MePro), and 2,3-diamino 3-methyl propanoic acid (MeDap)] and fatty acid substrates required for the biosynthesis of the maladicins are shown and colored coded according to their activities. Stereocenters in malacidin that were predicted bioinformatically as opposed to through chemical and spectroscopic analysis are denoted with an asterisk.
Figure Legend Snippet: Maladicin biosynthesis, heterologous expression and structure (a) The malacidin biosynthetic gene cluster was recovered on three overlapping cosmid clones and (b) assembled from these three overlapping clones in yeast using transformation-associated recombination (TAR). The resulting bacterial artificial chromosome (BAC) was integrated into S. albus genome for heterologous expression studies. (c) A representative HPLC analysis of crude extracts derived from cultures of S. albus transformed with the malacidin biosynthetic gene cluster (BGC) shows the presence of BGC-specific small molecules. The two primary malacidin peaks are highlighted with an asterisk. (d) Unlike crude extracts of the S. albus host strain alone, only extracts from the S. albus harboring the malacidin BGC showed antibacterial activity when applied to a lawn of S. aureus USA300. Both the (c) HPLC analysis and (d) antibacterial activity are representative of 4 independent fermentations. (e) Malacidin A and B are cyclic lipopeptides containing 8 amino acid macrocycles and polyunsaturated lipids. The malacidins do not contain the conserved DXDG motif seen in all known calcium-dependent antibiotics – incorporating a rare 3-hydroxyl aspartic acid (HyAsp, highlighted in violet) and lacking the spacer residue. Biosynthetic enzymes predicted to be involved in the production of non-proteinogenic amino acid [3-methyl aspartic acid (MeAsp), 4-methyl proline (MePro), and 2,3-diamino 3-methyl propanoic acid (MeDap)] and fatty acid substrates required for the biosynthesis of the maladicins are shown and colored coded according to their activities. Stereocenters in malacidin that were predicted bioinformatically as opposed to through chemical and spectroscopic analysis are denoted with an asterisk.

Techniques Used: Expressing, Clone Assay, Transformation Assay, BAC Assay, High Performance Liquid Chromatography, Derivative Assay, Activity Assay

4) Product Images from "Morphogenesis guided by 3D patterning of growth factors in biological matrices"

Article Title: Morphogenesis guided by 3D patterning of growth factors in biological matrices

Journal: bioRxiv

doi: 10.1101/828947

Characterization of SAT and fluorescein-substituted avidin (Avidin-SAT-F) and biotinylated NGF (NGF-Biotin). ( a, b ) Matrix-assisted laser desorption and ionization time-of-flight mass spectroscopy (MALDI-TOF) of avidin and SAT-substituted avidin, showing approximately 1.5 substitutions on average per monomer, i.e. 6 substitutions per avidin tetramer. ( c,d ) MALDI-TOF of NGF-Biotin, showing approximately two thirds of the NGF monomer bear a biotin (with PEG spacer), i.e. ≈1.3 per NGF dimer. ( e ) Confirmation of the substitution of NGF with biotin on C18 analytical HPLC. ( f ) Confirmation of NGF-Biotin binding to modified avidin by gel permeation chromatography (GPC).
Figure Legend Snippet: Characterization of SAT and fluorescein-substituted avidin (Avidin-SAT-F) and biotinylated NGF (NGF-Biotin). ( a, b ) Matrix-assisted laser desorption and ionization time-of-flight mass spectroscopy (MALDI-TOF) of avidin and SAT-substituted avidin, showing approximately 1.5 substitutions on average per monomer, i.e. 6 substitutions per avidin tetramer. ( c,d ) MALDI-TOF of NGF-Biotin, showing approximately two thirds of the NGF monomer bear a biotin (with PEG spacer), i.e. ≈1.3 per NGF dimer. ( e ) Confirmation of the substitution of NGF with biotin on C18 analytical HPLC. ( f ) Confirmation of NGF-Biotin binding to modified avidin by gel permeation chromatography (GPC).

Techniques Used: Avidin-Biotin Assay, Mass Spectrometry, High Performance Liquid Chromatography, Binding Assay, Modification, GPC Assay, Gel Permeation Chromatography

5) Product Images from "Targeted Metabolomic Analysis of Polyphenols with Antioxidant Activity in Sour Guava (Psidium friedrichsthalianum Nied.) Fruit"

Article Title: Targeted Metabolomic Analysis of Polyphenols with Antioxidant Activity in Sour Guava (Psidium friedrichsthalianum Nied.) Fruit

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

doi: 10.3390/molecules22010011

HPLC analysis of F.EtOAc.2 fraction of P. friedrichsthalianum fruit (C 18 -column, λ = 370 nm). Compounds: 1 : procyanidin B1; 2 : procyanidin B2; 3 : unidentified; and 4 : ellagic acid.
Figure Legend Snippet: HPLC analysis of F.EtOAc.2 fraction of P. friedrichsthalianum fruit (C 18 -column, λ = 370 nm). Compounds: 1 : procyanidin B1; 2 : procyanidin B2; 3 : unidentified; and 4 : ellagic acid.

Techniques Used: High Performance Liquid Chromatography

6) Product Images from "Development of Multifunctional Cosmetic Cream Using Bioactive Materials from Streptomyces sp. T65 with Synthesized Mesoporous Silica Particles SBA-15"

Article Title: Development of Multifunctional Cosmetic Cream Using Bioactive Materials from Streptomyces sp. T65 with Synthesized Mesoporous Silica Particles SBA-15

Journal: Antioxidants

doi: 10.3390/antiox9040278

HPLC chromatogram of T65 embedded SBA-15 for sustainable control release test. ( a ) 0 day, ( b ) first day, ( c ) second day, and ( d ) third day.
Figure Legend Snippet: HPLC chromatogram of T65 embedded SBA-15 for sustainable control release test. ( a ) 0 day, ( b ) first day, ( c ) second day, and ( d ) third day.

Techniques Used: High Performance Liquid Chromatography

7) Product Images from "A Novel Antioxidant Phenyl Disaccharide from Populus tremula Knotwood"

Article Title: A Novel Antioxidant Phenyl Disaccharide from Populus tremula Knotwood

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

doi: 10.3390/12020205

Analytical HPLC chromatogram of Populus tremula knotwood extract recorded at 314 nm. Inserts represent the chromatograms of the fractions F1 and F2 isolated using preparative HPLC.
Figure Legend Snippet: Analytical HPLC chromatogram of Populus tremula knotwood extract recorded at 314 nm. Inserts represent the chromatograms of the fractions F1 and F2 isolated using preparative HPLC.

Techniques Used: High Performance Liquid Chromatography, Isolation

8) Product Images from "Bacillomycin D Produced by Bacillus amyloliquefaciens Is Involved in the Antagonistic Interaction with the Plant-Pathogenic Fungus Fusarium graminearum"

Article Title: Bacillomycin D Produced by Bacillus amyloliquefaciens Is Involved in the Antagonistic Interaction with the Plant-Pathogenic Fungus Fusarium graminearum

Journal: Applied and Environmental Microbiology

doi: 10.1128/AEM.01075-17

Purification and characterization of bacillomycin D from B. amyloliquefaciens CH02. (A) Bacillomycin D was purified from B. amyloliquefaciens CH02 using reverse-phase HPLC. (B) Five fractions (I to V) were separated and collected by reverse-phase HPLC and were used for the analysis of antagonistic activity. 45% acetonitrile (vol/vol) served as the control (CK). (C) The purity of bacillomycin D collected from peak I was analyzed by HPLC.
Figure Legend Snippet: Purification and characterization of bacillomycin D from B. amyloliquefaciens CH02. (A) Bacillomycin D was purified from B. amyloliquefaciens CH02 using reverse-phase HPLC. (B) Five fractions (I to V) were separated and collected by reverse-phase HPLC and were used for the analysis of antagonistic activity. 45% acetonitrile (vol/vol) served as the control (CK). (C) The purity of bacillomycin D collected from peak I was analyzed by HPLC.

Techniques Used: Purification, High Performance Liquid Chromatography, Activity Assay

9) Product Images from "Culture-independent discovery of the malacidins as calcium-dependent antibiotics with activity against multidrug-resistant Gram-positive pathogens"

Article Title: Culture-independent discovery of the malacidins as calcium-dependent antibiotics with activity against multidrug-resistant Gram-positive pathogens

Journal: Nature microbiology

doi: 10.1038/s41564-018-0110-1

Maladicin biosynthesis, heterologous expression and structure (a) The malacidin biosynthetic gene cluster was recovered on three overlapping cosmid clones and (b) assembled from these three overlapping clones in yeast using transformation-associated recombination (TAR). The resulting bacterial artificial chromosome (BAC) was integrated into S. albus genome for heterologous expression studies. (c) A representative HPLC analysis of crude extracts derived from cultures of S. albus transformed with the malacidin biosynthetic gene cluster (BGC) shows the presence of BGC-specific small molecules. The two primary malacidin peaks are highlighted with an asterisk. (d) Unlike crude extracts of the S. albus host strain alone, only extracts from the S. albus harboring the malacidin BGC showed antibacterial activity when applied to a lawn of S. aureus USA300. Both the (c) HPLC analysis and (d) antibacterial activity are representative of 4 independent fermentations. (e) Malacidin A and B are cyclic lipopeptides containing 8 amino acid macrocycles and polyunsaturated lipids. The malacidins do not contain the conserved DXDG motif seen in all known calcium-dependent antibiotics – incorporating a rare 3-hydroxyl aspartic acid (HyAsp, highlighted in violet) and lacking the spacer residue. Biosynthetic enzymes predicted to be involved in the production of non-proteinogenic amino acid [3-methyl aspartic acid (MeAsp), 4-methyl proline (MePro), and 2,3-diamino 3-methyl propanoic acid (MeDap)] and fatty acid substrates required for the biosynthesis of the maladicins are shown and colored coded according to their activities. Stereocenters in malacidin that were predicted bioinformatically as opposed to through chemical and spectroscopic analysis are denoted with an asterisk.
Figure Legend Snippet: Maladicin biosynthesis, heterologous expression and structure (a) The malacidin biosynthetic gene cluster was recovered on three overlapping cosmid clones and (b) assembled from these three overlapping clones in yeast using transformation-associated recombination (TAR). The resulting bacterial artificial chromosome (BAC) was integrated into S. albus genome for heterologous expression studies. (c) A representative HPLC analysis of crude extracts derived from cultures of S. albus transformed with the malacidin biosynthetic gene cluster (BGC) shows the presence of BGC-specific small molecules. The two primary malacidin peaks are highlighted with an asterisk. (d) Unlike crude extracts of the S. albus host strain alone, only extracts from the S. albus harboring the malacidin BGC showed antibacterial activity when applied to a lawn of S. aureus USA300. Both the (c) HPLC analysis and (d) antibacterial activity are representative of 4 independent fermentations. (e) Malacidin A and B are cyclic lipopeptides containing 8 amino acid macrocycles and polyunsaturated lipids. The malacidins do not contain the conserved DXDG motif seen in all known calcium-dependent antibiotics – incorporating a rare 3-hydroxyl aspartic acid (HyAsp, highlighted in violet) and lacking the spacer residue. Biosynthetic enzymes predicted to be involved in the production of non-proteinogenic amino acid [3-methyl aspartic acid (MeAsp), 4-methyl proline (MePro), and 2,3-diamino 3-methyl propanoic acid (MeDap)] and fatty acid substrates required for the biosynthesis of the maladicins are shown and colored coded according to their activities. Stereocenters in malacidin that were predicted bioinformatically as opposed to through chemical and spectroscopic analysis are denoted with an asterisk.

Techniques Used: Expressing, Clone Assay, Transformation Assay, BAC Assay, High Performance Liquid Chromatography, Derivative Assay, Activity Assay

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Concentration Assay:

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Purification:

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In Vitro:

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Size-exclusion Chromatography:

Article Title: Structural organization of a major neuronal G protein regulator, the RGS7-Gβ5-R7BP complex
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    Agilent technologies semi preparativerp hplc column
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