Structured Review

Agilent technologies reverse phase hplc
In vitro drug release behaviors of LPNs and the solution depicted as the cumulative <t>RPV</t> release (%) vs time. Notes: Data represent mean ± SD, N=3. Release of RPV from the LPNs was studied following the dialysis bag method. The bags were placed in a glass beaker containing 0.2 L of PBS (pH 7.4) at 37.0°C±0.5°C and stirred at 100 rpm. At pre-set time intervals, 1 mL of the medium was collected and analyzed for RPV content by <t>HPLC.</t> Abbreviations: RPV, ropivacaine; LPNs, lipid-polymer hybrid nanoparticles.
Reverse Phase Hplc, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 94/100, based on 119 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/reverse phase hplc/product/Agilent technologies
Average 94 stars, based on 119 article reviews
Price from $9.99 to $1999.99
reverse phase hplc - by Bioz Stars, 2020-07
94/100 stars

Images

1) Product Images from "An efficient and long-acting local anesthetic: ropivacaine-loaded lipid-polymer hybrid nanoparticles for the control of pain"

Article Title: An efficient and long-acting local anesthetic: ropivacaine-loaded lipid-polymer hybrid nanoparticles for the control of pain

Journal: International Journal of Nanomedicine

doi: 10.2147/IJN.S190164

In vitro drug release behaviors of LPNs and the solution depicted as the cumulative RPV release (%) vs time. Notes: Data represent mean ± SD, N=3. Release of RPV from the LPNs was studied following the dialysis bag method. The bags were placed in a glass beaker containing 0.2 L of PBS (pH 7.4) at 37.0°C±0.5°C and stirred at 100 rpm. At pre-set time intervals, 1 mL of the medium was collected and analyzed for RPV content by HPLC. Abbreviations: RPV, ropivacaine; LPNs, lipid-polymer hybrid nanoparticles.
Figure Legend Snippet: In vitro drug release behaviors of LPNs and the solution depicted as the cumulative RPV release (%) vs time. Notes: Data represent mean ± SD, N=3. Release of RPV from the LPNs was studied following the dialysis bag method. The bags were placed in a glass beaker containing 0.2 L of PBS (pH 7.4) at 37.0°C±0.5°C and stirred at 100 rpm. At pre-set time intervals, 1 mL of the medium was collected and analyzed for RPV content by HPLC. Abbreviations: RPV, ropivacaine; LPNs, lipid-polymer hybrid nanoparticles.

Techniques Used: In Vitro, High Performance Liquid Chromatography

2) Product Images from "The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule"

Article Title: The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule

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

doi: 10.1073/pnas.1115623109

Two critical lysines in IRE1 are selectively targeted by 4μ8C. ( A ) Absorption traces of peptides eluting from a C18 reverse-phase HPLC. The column was loaded with a tryptic digest of baculovirus expressed IRE1 that had or had not been exposed
Figure Legend Snippet: Two critical lysines in IRE1 are selectively targeted by 4μ8C. ( A ) Absorption traces of peptides eluting from a C18 reverse-phase HPLC. The column was loaded with a tryptic digest of baculovirus expressed IRE1 that had or had not been exposed

Techniques Used: High Performance Liquid Chromatography

3) Product Images from "Indoleamine 2,3-dioxygenase 1 (IDO1) activity in leukemia blasts correlates with poor outcome in childhood acute myeloid leukemia"

Article Title: Indoleamine 2,3-dioxygenase 1 (IDO1) activity in leukemia blasts correlates with poor outcome in childhood acute myeloid leukemia

Journal: Oncotarget

doi:

Expression and Function of IDO1 in BM Samples from Children with AML BM samples from children with AML obtained at diagnosis were cryopreserved. After thawing, BM mononuclear cells (MNC) were either stimulated with 100 ng/ml IFN-γ for up to 72 hours or were maintained in culture medium alone. Supernatants were collected and used for the measurement of kynurenine and tryptophan levels by RP-HPLC. (A) Up-regulation of IDO protein by IFN-γ (+) in 2 representative AML samples; UPN = Unique Patient Number; Hsp-70 = heat shock protein-70; (B) Release of kynurenine and (C) Consumption of tryptophan by AML blasts maintained in culture for 72 hours with or without exogenous IFN-γ. Blasts from a cohort of 7 children with acute lymphoblastic leukemia (ALL) were also challenged with IFN-γ to detect any IDO-mediated tryptophan breakdown. Comparisons between groups were performed with the Mann-Whitney U test for paired determinations. HC = healthy controls. Medium = blast cells maintained with complete culture medium alone; (D) Time-course experiments with AML blasts from 4 randomly selected BM samples that were either activated with IFN-γ (red dots) or left untouched (black dots). Bars depict the median and interquartile range; (E) Commercially available AML cell lines (see main text for details) were either stimulated with IFN-γ for 72 hours (black columns) or were maintained in culture medium alone (empty columns), prior to HPLC studies. Bars are representative of mean values and standard deviation recorded in 3 independent experiments run in duplicate.
Figure Legend Snippet: Expression and Function of IDO1 in BM Samples from Children with AML BM samples from children with AML obtained at diagnosis were cryopreserved. After thawing, BM mononuclear cells (MNC) were either stimulated with 100 ng/ml IFN-γ for up to 72 hours or were maintained in culture medium alone. Supernatants were collected and used for the measurement of kynurenine and tryptophan levels by RP-HPLC. (A) Up-regulation of IDO protein by IFN-γ (+) in 2 representative AML samples; UPN = Unique Patient Number; Hsp-70 = heat shock protein-70; (B) Release of kynurenine and (C) Consumption of tryptophan by AML blasts maintained in culture for 72 hours with or without exogenous IFN-γ. Blasts from a cohort of 7 children with acute lymphoblastic leukemia (ALL) were also challenged with IFN-γ to detect any IDO-mediated tryptophan breakdown. Comparisons between groups were performed with the Mann-Whitney U test for paired determinations. HC = healthy controls. Medium = blast cells maintained with complete culture medium alone; (D) Time-course experiments with AML blasts from 4 randomly selected BM samples that were either activated with IFN-γ (red dots) or left untouched (black dots). Bars depict the median and interquartile range; (E) Commercially available AML cell lines (see main text for details) were either stimulated with IFN-γ for 72 hours (black columns) or were maintained in culture medium alone (empty columns), prior to HPLC studies. Bars are representative of mean values and standard deviation recorded in 3 independent experiments run in duplicate.

Techniques Used: Expressing, High Performance Liquid Chromatography, MANN-WHITNEY, Standard Deviation

4) Product Images from "Solenodon genome reveals convergent evolution of venom in eulipotyphlan mammals"

Article Title: Solenodon genome reveals convergent evolution of venom in eulipotyphlan mammals

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

doi: 10.1073/pnas.1906117116

Proteomic analyses of Hispaniolan solenodon ( S. paradoxus ) venom and saliva reveal KLK1 proteins as major venom components. ( A ) Reduced SDS-PAGE gel electrophoretic profiles of venom and saliva samples. ( B ) Gene ontology (GO) term analysis of proteins identified via shotgun proteomic-based annotation to the genome. GO term categories are only displayed for those with at least 2 matches. ( C ) Venn diagram displaying the number of proteins in the venom and saliva, and those identified in both samples via shotgun proteomic-based annotation to the genome. ( D ) Reverse-phase chromatographic separation of venom. Venom was separated by semipreparative reversed-phase HPLC (UV 214nm ) and manually collected. Peptides were directly submitted to LC-MS/MS, whereas protein fractions were analyzed by SDS-PAGE ( Inset ) under reducing conditions. Afterward, protein bands were subjected to in-gel trypsin digestion and identified by spectrum peptide matching against the translated S. paradoxus genome database. ( E and F ) LC-top-down MS analysis of saliva ( E ) and venom ( F ). The peak nomenclature is based on the chromatogram fractions, shown in D . ( E ) Total ion current (TIC) profile of native saliva separated by HPLC. ( F ) TIC profile of native venom separated by HPLC. ( G ) Summary table of the proteins identified via top-down and bottom-up proteomic analyses of solenodon venom, including their mass, corresponding identification in the genome (genome ID), and protein annotation. All identified proteins are annotated as KLK1 , with the exception of keratins, which are human contaminants. ( H ) Comparison of the relative abundance of main proteins present in chromatographic fractions of venom and saliva from top-down MS experiments. SI Appendix , Table S2 presents a summary of the protein matches identified in solenodon venom and saliva via the various proteomic approaches.
Figure Legend Snippet: Proteomic analyses of Hispaniolan solenodon ( S. paradoxus ) venom and saliva reveal KLK1 proteins as major venom components. ( A ) Reduced SDS-PAGE gel electrophoretic profiles of venom and saliva samples. ( B ) Gene ontology (GO) term analysis of proteins identified via shotgun proteomic-based annotation to the genome. GO term categories are only displayed for those with at least 2 matches. ( C ) Venn diagram displaying the number of proteins in the venom and saliva, and those identified in both samples via shotgun proteomic-based annotation to the genome. ( D ) Reverse-phase chromatographic separation of venom. Venom was separated by semipreparative reversed-phase HPLC (UV 214nm ) and manually collected. Peptides were directly submitted to LC-MS/MS, whereas protein fractions were analyzed by SDS-PAGE ( Inset ) under reducing conditions. Afterward, protein bands were subjected to in-gel trypsin digestion and identified by spectrum peptide matching against the translated S. paradoxus genome database. ( E and F ) LC-top-down MS analysis of saliva ( E ) and venom ( F ). The peak nomenclature is based on the chromatogram fractions, shown in D . ( E ) Total ion current (TIC) profile of native saliva separated by HPLC. ( F ) TIC profile of native venom separated by HPLC. ( G ) Summary table of the proteins identified via top-down and bottom-up proteomic analyses of solenodon venom, including their mass, corresponding identification in the genome (genome ID), and protein annotation. All identified proteins are annotated as KLK1 , with the exception of keratins, which are human contaminants. ( H ) Comparison of the relative abundance of main proteins present in chromatographic fractions of venom and saliva from top-down MS experiments. SI Appendix , Table S2 presents a summary of the protein matches identified in solenodon venom and saliva via the various proteomic approaches.

Techniques Used: SDS Page, High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

5) Product Images from "Metabolic Regulation as a Consequence of Anaerobic 5-Methylthioadenosine Recycling in Rhodospirillum rubrum"

Article Title: Metabolic Regulation as a Consequence of Anaerobic 5-Methylthioadenosine Recycling in Rhodospirillum rubrum

Journal: mBio

doi: 10.1128/mBio.00855-16

HPLC identification of purines resulting from MTA metabolism. The R. rubrum wild-type strain was grown anaerobically in the presence of sulfate and then fed with MTA for the indicated amount of time (minutes) before resolution of metabolites via 260-nm absorbance present in the medium after reverse-phase liquid chromatography. “Standard” (black line) is the retention time of known purine base and nucleoside standards (see Fig. S4A in the supplemental material). Ura, urate; Hyx, hypoxanthine; Xan, xanthine; Ino, inosine; Ade, adenine; Xao, xanthosine; Ado, adenosine; MTA, 5-methylthioadenosine.
Figure Legend Snippet: HPLC identification of purines resulting from MTA metabolism. The R. rubrum wild-type strain was grown anaerobically in the presence of sulfate and then fed with MTA for the indicated amount of time (minutes) before resolution of metabolites via 260-nm absorbance present in the medium after reverse-phase liquid chromatography. “Standard” (black line) is the retention time of known purine base and nucleoside standards (see Fig. S4A in the supplemental material). Ura, urate; Hyx, hypoxanthine; Xan, xanthine; Ino, inosine; Ade, adenine; Xao, xanthosine; Ado, adenosine; MTA, 5-methylthioadenosine.

Techniques Used: High Performance Liquid Chromatography, Liquid Chromatography

6) Product Images from "Anthocyanins Extracted from Oryza sativa L. Prevent Fluorouracil-Induced Nuclear Factor-κB Activation in Oral Mucositis: In Vitro and In Vivo Studies"

Article Title: Anthocyanins Extracted from Oryza sativa L. Prevent Fluorouracil-Induced Nuclear Factor-κB Activation in Oral Mucositis: In Vitro and In Vivo Studies

Journal: International Journal of Molecular Sciences

doi: 10.3390/ijms19102981

HPLC-electrospray ionization (ESI) mass spectrometry (MS) analysis of anthrocyanins (ANTs) in Oryza sativa L. ( A ) Representative HPLC chromatograms of Cyanidin-3-glucoside (C3G) and Pelargonidin-3-glucoside (P3G) in the extracts at 530 nm. Peaks were detected with a retention time at 31.0 and 37.0 min, identified as C3G and P3G, respectively; ( B ) Fragmentation patterns in the mass spectra of C3G and P3G in the ANT. The assay was performed in triplicate.
Figure Legend Snippet: HPLC-electrospray ionization (ESI) mass spectrometry (MS) analysis of anthrocyanins (ANTs) in Oryza sativa L. ( A ) Representative HPLC chromatograms of Cyanidin-3-glucoside (C3G) and Pelargonidin-3-glucoside (P3G) in the extracts at 530 nm. Peaks were detected with a retention time at 31.0 and 37.0 min, identified as C3G and P3G, respectively; ( B ) Fragmentation patterns in the mass spectra of C3G and P3G in the ANT. The assay was performed in triplicate.

Techniques Used: High Performance Liquid Chromatography, Mass Spectrometry

7) Product Images from "Anti-tumor activity of nanomicelles encapsulating CXCR4 peptide antagonist E5"

Article Title: Anti-tumor activity of nanomicelles encapsulating CXCR4 peptide antagonist E5

Journal: PLoS ONE

doi: 10.1371/journal.pone.0182697

Characterization of micelles in terms of particle size distribution, morphology and drug release kinetics. (a ) Particle sizes of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) were determined by DLS. ( b ) The morphology of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) was observed via TEM, and the samples were stained with 1% uranyl acetate for 1 min at room temperature. Scale bar = 100 nm. ( c ) The HPLC chromatogram of Dox, and physicochemical properties of the PEG-PE micelle (100 μM), M-E5 (PEG-PE: 100 μM, E5: 25 μM) and M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM). ( d ) Time course (0–72 h) release profiles of Dox and E5 from M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM) at 37°C and at pH 5.0 and 7.4. Data are presented as mean ± SD ( n = 3). The * represents significant difference between two groups (*p
Figure Legend Snippet: Characterization of micelles in terms of particle size distribution, morphology and drug release kinetics. (a ) Particle sizes of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) were determined by DLS. ( b ) The morphology of the PEG-PE micelle (50 μM), M-E5 (PEG-PE: 50 μM, E5: 12.5 μM) and M-E5-Dox (PEG-PE: 50 μM, E5: 12.5 μM, and Dox: 5 μM) was observed via TEM, and the samples were stained with 1% uranyl acetate for 1 min at room temperature. Scale bar = 100 nm. ( c ) The HPLC chromatogram of Dox, and physicochemical properties of the PEG-PE micelle (100 μM), M-E5 (PEG-PE: 100 μM, E5: 25 μM) and M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM). ( d ) Time course (0–72 h) release profiles of Dox and E5 from M-E5-Dox (PEG-PE: 100 μM, E5: 25 μM, and Dox: 10 μM) at 37°C and at pH 5.0 and 7.4. Data are presented as mean ± SD ( n = 3). The * represents significant difference between two groups (*p

Techniques Used: Transmission Electron Microscopy, Staining, High Performance Liquid Chromatography

8) Product Images from "Nitric Oxide Deficiency Accelerates Chlorophyll Breakdown and Stability Loss of Thylakoid Membranes during Dark-Induced Leaf Senescence in Arabidopsis"

Article Title: Nitric Oxide Deficiency Accelerates Chlorophyll Breakdown and Stability Loss of Thylakoid Membranes during Dark-Induced Leaf Senescence in Arabidopsis

Journal: PLoS ONE

doi: 10.1371/journal.pone.0056345

Activities of PAO in wild type and nos1/noa1 leaves during dark-induced leaf senescence. HPLC analysis of pFCC-1 generated by PAO-RCCR coupled assay with crude extracts of PAO and RCCR from wild type and nos1/noa1 leaves during a 4-d dark treatment. pFCC-1 was eluted after 9 min, as indicated by arrows. The experiment was repeated once with qualitatively identical results.
Figure Legend Snippet: Activities of PAO in wild type and nos1/noa1 leaves during dark-induced leaf senescence. HPLC analysis of pFCC-1 generated by PAO-RCCR coupled assay with crude extracts of PAO and RCCR from wild type and nos1/noa1 leaves during a 4-d dark treatment. pFCC-1 was eluted after 9 min, as indicated by arrows. The experiment was repeated once with qualitatively identical results.

Techniques Used: High Performance Liquid Chromatography, Generated

9) Product Images from "Substrate-Induced Inactivation of the Escherichia coli AmiD N-Acetylmuramoyl-l-Alanine Amidase Highlights a New Strategy To Inhibit This Class of Enzyme ▿"

Article Title: Substrate-Induced Inactivation of the Escherichia coli AmiD N-Acetylmuramoyl-l-Alanine Amidase Highlights a New Strategy To Inhibit This Class of Enzyme ▿

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.01520-07

Release of peptides from the peptidoglycan polymer by the purified AmiD-His 6 . Purified peptidoglycan from E. coli was digested overnight by AmiD-His 6 , and the reaction mixture was analyzed using HPLC and a Nucleosil 100C 18 column as described in Materials
Figure Legend Snippet: Release of peptides from the peptidoglycan polymer by the purified AmiD-His 6 . Purified peptidoglycan from E. coli was digested overnight by AmiD-His 6 , and the reaction mixture was analyzed using HPLC and a Nucleosil 100C 18 column as described in Materials

Techniques Used: Purification, High Performance Liquid Chromatography

10) Product Images from "Activation of 6-Alkoxy-Substituted Methylenecyclopropane Nucleoside Analogs Requires Enzymatic Modification by Adenosine Deaminase-Like Protein 1"

Article Title: Activation of 6-Alkoxy-Substituted Methylenecyclopropane Nucleoside Analogs Requires Enzymatic Modification by Adenosine Deaminase-Like Protein 1

Journal: Antimicrobial Agents and Chemotherapy

doi: 10.1128/AAC.01301-19

Metabolite identification assay. MBX-2168 was exposed to mouse liver microsomes (MLMS), and metabolites were identified by LC-MS/MS analysis. (a) HPLC traces, including UV absorbance at 254 nm and extracted ion chromatographs representing all major metabolites. (b) Structures of notable peaks and relevant MS fragments. HPLC peak 1, synguanol metabolite; HPLC peak 2, metabolic product of oxidation of the butyl chain, identified by the presence of a synguanol MS fragment (peak at m / z 308.3 is from an isotope with higher molecular weight); HPLC peak 3, metabolic product of hydration at the cyclopropylidine substituent, identified by the presence of a MS fragment ( m / z 208.2); HPLC peak 4, metabolic product of oxidation at the core or cyclopropylidine substituent, identified by the presence of an oxidized synguanol MS fragment; HPLC peak 5, parent, MBX-2168 accompanied by significant levels of a synguanol MS fragment.
Figure Legend Snippet: Metabolite identification assay. MBX-2168 was exposed to mouse liver microsomes (MLMS), and metabolites were identified by LC-MS/MS analysis. (a) HPLC traces, including UV absorbance at 254 nm and extracted ion chromatographs representing all major metabolites. (b) Structures of notable peaks and relevant MS fragments. HPLC peak 1, synguanol metabolite; HPLC peak 2, metabolic product of oxidation of the butyl chain, identified by the presence of a synguanol MS fragment (peak at m / z 308.3 is from an isotope with higher molecular weight); HPLC peak 3, metabolic product of hydration at the cyclopropylidine substituent, identified by the presence of a MS fragment ( m / z 208.2); HPLC peak 4, metabolic product of oxidation at the core or cyclopropylidine substituent, identified by the presence of an oxidized synguanol MS fragment; HPLC peak 5, parent, MBX-2168 accompanied by significant levels of a synguanol MS fragment.

Techniques Used: Liquid Chromatography with Mass Spectroscopy, High Performance Liquid Chromatography, Molecular Weight

Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 -methyl-AMP (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via HPLC. The values represent the mean ± standard deviation from at least three experiments.
Figure Legend Snippet: Enzymatic conversion of MBX-2168-MP to synguanol-MP by ADAL-1. The time-dependent formation of synguanol-MP (a) or IMP (b) was determined by incubating 100 μM MBX-2168-MP (a) or N 6 -methyl-AMP (NAMP) (b), respectively, with purified ADAL-1 and separating and quantifying the products via HPLC. The values represent the mean ± standard deviation from at least three experiments.

Techniques Used: Purification, High Performance Liquid Chromatography, Standard Deviation

11) Product Images from "Utility of Muropeptide Ligase for Identification of Inhibitors of the Cell Wall Biosynthesis Enzyme MurF"

Article Title: Utility of Muropeptide Ligase for Identification of Inhibitors of the Cell Wall Biosynthesis Enzyme MurF

Journal:

doi: 10.1128/AAC.50.1.230-236.2006

HPLC chromatograms of Mpl and MurF reactions. The HPLC profiles at 260 nM are displayed for the following reactions: l -Ala-γ- d -Glu-A 2 pm without enzyme (A) or incubated with Mpl (B) or with Mpl and MurF (F), l -Ala-γ- d -Glu- l -Lys incubated
Figure Legend Snippet: HPLC chromatograms of Mpl and MurF reactions. The HPLC profiles at 260 nM are displayed for the following reactions: l -Ala-γ- d -Glu-A 2 pm without enzyme (A) or incubated with Mpl (B) or with Mpl and MurF (F), l -Ala-γ- d -Glu- l -Lys incubated

Techniques Used: High Performance Liquid Chromatography, Incubation

12) Product Images from "Venomics and antivenomics of the poorly studied Brazil’s lancehead,Bothrops brazili (Hoge, 1954), from the Brazilian State of Pará"

Article Title: Venomics and antivenomics of the poorly studied Brazil’s lancehead,Bothrops brazili (Hoge, 1954), from the Brazilian State of Pará

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

doi: 10.1590/1678-9199-JVATITD-2019-0103

Comparative immunorecognition ability of the Brazilian SAB antivenom towards B. brazili and B. jararaca venom toxins. (A) Third-generation antivenomic analyses of B. brazili and (B) B. jararaca venom with the pentabothropic antivenom ( soro antibotrópico , SAB) produced at Butantan Institute. Reverse-phase chromatographic analysis of whole venom (panels a ) and of the non-retained and the immunoretained fractions recovered from affinity column [9 mg immobilized SAB antivenom F(ab’) 2 molecules] incubated with increasing amounts (300-3600 µg) of venom from ( A ) B. brazili (Pará, Brazil) and ( B ) B. jararaca (SE population) are displayed in panels b through i . Panels j-l show reverse-phase HPLC separations of the retained and non-retained venom fractions on mock matrix and naïve equine IgG affinity columns, respectively.
Figure Legend Snippet: Comparative immunorecognition ability of the Brazilian SAB antivenom towards B. brazili and B. jararaca venom toxins. (A) Third-generation antivenomic analyses of B. brazili and (B) B. jararaca venom with the pentabothropic antivenom ( soro antibotrópico , SAB) produced at Butantan Institute. Reverse-phase chromatographic analysis of whole venom (panels a ) and of the non-retained and the immunoretained fractions recovered from affinity column [9 mg immobilized SAB antivenom F(ab’) 2 molecules] incubated with increasing amounts (300-3600 µg) of venom from ( A ) B. brazili (Pará, Brazil) and ( B ) B. jararaca (SE population) are displayed in panels b through i . Panels j-l show reverse-phase HPLC separations of the retained and non-retained venom fractions on mock matrix and naïve equine IgG affinity columns, respectively.

Techniques Used: Produced, Affinity Column, Incubation, High Performance Liquid Chromatography

13) Product Images from "Purification and characterization of a novel lipopeptide from Streptomyces amritsarensis sp. nov. active against methicillin-resistant Staphylococcus aureus"

Article Title: Purification and characterization of a novel lipopeptide from Streptomyces amritsarensis sp. nov. active against methicillin-resistant Staphylococcus aureus

Journal: AMB Express

doi: 10.1186/s13568-014-0050-y

Elution profile of lipopeptide using HPLC reverse phase chromatography on ZORBAX 300-SB18 column monitoring by absorbance at 215 nm. Peak 3 corresponds to lipopeptide elution.
Figure Legend Snippet: Elution profile of lipopeptide using HPLC reverse phase chromatography on ZORBAX 300-SB18 column monitoring by absorbance at 215 nm. Peak 3 corresponds to lipopeptide elution.

Techniques Used: High Performance Liquid Chromatography, Reversed-phase Chromatography

Related Articles

High Performance Liquid Chromatography:

Article Title: Nitric Oxide Deficiency Accelerates Chlorophyll Breakdown and Stability Loss of Thylakoid Membranes during Dark-Induced Leaf Senescence in Arabidopsis
Article Snippet: .. The reaction mixture was centrifuged at 14,000 g for 10 min, and the supernatant was analyzed for pFCC-1 by reverse-phase HPLC with 0.1 M potassium phosphate (pH 7.0)/methanol (32.5%∶67.5%, V/V). pFCC-1 was analyzed by HPLC with an Agilent 1100 HPLC ChemStation coupled to a fluorescence detector equipped with a ZorbaxSB C-18 column (4.6 mm×25 cm, 5-µm particle diameter). ..

Article Title: Anti-tumor activity of nanomicelles encapsulating CXCR4 peptide antagonist E5
Article Snippet: .. The concentration of free Dox in filtrate was quantified by reverse-phase HPLC (RP-HPLC, Agilent 1206, USA) with a C18 % E n c a p s u l a t i o n e f f i c i e n c y o f D o x ( E 5 ) = [ i n c o r p o r a t e d D o x ( E 5 ) ] [ i n i t i a l D o x ( E 5 ) a d d e d ] * 100 (1) .. In vitro drug release In vitro release of Dox and E5 from M-E5-Dox (PEG-PE: 100 μM, FITC-E5: 25 μM, and Dox: 10 μM) was determined by dialysis using a 100,000 Da molecular weight cut-off membrane (Millipore).

Article Title: Indoleamine 2,3-dioxygenase 1 (IDO1) activity in leukemia blasts correlates with poor outcome in childhood acute myeloid leukemia
Article Snippet: .. IDO1 activity Tryptophan and kynurenine levels were measured with reverse-phase HPLC (Agilent Technologies 1200; Waldbronn, Germany). ..

Article Title: Anthocyanins Extracted from Oryza sativa L. Prevent Fluorouracil-Induced Nuclear Factor-κB Activation in Oral Mucositis: In Vitro and In Vivo Studies
Article Snippet: .. For HPLC-electrospray ionization (ESI) mass spectrometry (MS), ANT-rich extracts were separated and quantified by reverse-phase HPLC (Agilent model Model:1100 (Binary pump, Degasser, Autosample, DAD) using a Hypersil Gold C18 column (inner diameter, 3 μm; 4.6 × 150 mm; Thermo Fisher Scientific Inc., Waltham, MA, USA) following previous reporting [ ], with slight modifications. .. The column was eluted with a mobile phase consisting of formic acid (VWR International, Ltd., Leicestershire, UK) and methanol at a flow rate of 1 mL/min.

Article Title: An efficient and long-acting local anesthetic: ropivacaine-loaded lipid-polymer hybrid nanoparticles for the control of pain
Article Snippet: .. Drug loading and in vitro release RPV content in the LPNs was analyzed by reverse-phase HPLC (Agilent 1,100 Series, Agilent Technologies, Santa Clara, CA, USA). .. Specifically, 10 mL of sample was injected into a mobile phase of 50% PBS (pH 7.4) and 50% acetonitrile (0.1% TFA) at a flow rate of 1 mL/min and passed over a 5 µm reverse-phase column (Zorbax Eclipse SDB-C18, Agilent Technologies).

Article Title: The molecular basis for selective inhibition of unconventional mRNA splicing by an IRE1-binding small molecule
Article Snippet: .. Eluted peptides were dried and separated by reverse-phase HPLC on a poroshell 120 C18 column using a multistep acetonitrile gradient with 0.1% TFA on an Agilent LC1290 system with a diode array detection of absorbance from 180–400 nm. .. Two-drop (approximately 13 μL) fractions were collected, dried, and analyzed by MALDI-TOF mass spectrometry and nanoLC-ESI-MS/MS (see ).

Article Title: Metabolic Regulation as a Consequence of Anaerobic 5-Methylthioadenosine Recycling in Rhodospirillum rubrum
Article Snippet: .. Detection of R. rubrum metabolites due to MTA metabolism present in the spent medium was performed by reverse-phase HPLC on a Zorbax C18 (Agilent) column connected to a Shimadzu Prominence HPLC system with dual-wavelength detection (215 nm and 260 nm) and an inline β-RAM radiochromatography scintillation detector (IN/US Systems). .. Metabolites were eluted on a linear gradient from 0 to 50% acetonitrile (J. T. Baker) in 20 mM ammonium acetate over 30 min at 30°C.

Article Title: Solenodon genome reveals convergent evolution of venom in eulipotyphlan mammals
Article Snippet: .. Samples (1 mg) were separated via reverse-phase HPLC, then reduced and analyzed by SDS-PAGE, and protein bands subjected to in-gel tryptic digestion and analyzed by LC-MS/MS using an Orbitrap XL (Agilent, Germany). .. For top-down proteomics we used 0.2 mg of venom and saliva for reduced and nonreduced HPLC high-resolution (HR) MS/MS measurements.

In Vitro:

Article Title: An efficient and long-acting local anesthetic: ropivacaine-loaded lipid-polymer hybrid nanoparticles for the control of pain
Article Snippet: .. Drug loading and in vitro release RPV content in the LPNs was analyzed by reverse-phase HPLC (Agilent 1,100 Series, Agilent Technologies, Santa Clara, CA, USA). .. Specifically, 10 mL of sample was injected into a mobile phase of 50% PBS (pH 7.4) and 50% acetonitrile (0.1% TFA) at a flow rate of 1 mL/min and passed over a 5 µm reverse-phase column (Zorbax Eclipse SDB-C18, Agilent Technologies).

Fluorescence:

Article Title: Nitric Oxide Deficiency Accelerates Chlorophyll Breakdown and Stability Loss of Thylakoid Membranes during Dark-Induced Leaf Senescence in Arabidopsis
Article Snippet: .. The reaction mixture was centrifuged at 14,000 g for 10 min, and the supernatant was analyzed for pFCC-1 by reverse-phase HPLC with 0.1 M potassium phosphate (pH 7.0)/methanol (32.5%∶67.5%, V/V). pFCC-1 was analyzed by HPLC with an Agilent 1100 HPLC ChemStation coupled to a fluorescence detector equipped with a ZorbaxSB C-18 column (4.6 mm×25 cm, 5-µm particle diameter). ..

Concentration Assay:

Article Title: Anti-tumor activity of nanomicelles encapsulating CXCR4 peptide antagonist E5
Article Snippet: .. The concentration of free Dox in filtrate was quantified by reverse-phase HPLC (RP-HPLC, Agilent 1206, USA) with a C18 % E n c a p s u l a t i o n e f f i c i e n c y o f D o x ( E 5 ) = [ i n c o r p o r a t e d D o x ( E 5 ) ] [ i n i t i a l D o x ( E 5 ) a d d e d ] * 100 (1) .. In vitro drug release In vitro release of Dox and E5 from M-E5-Dox (PEG-PE: 100 μM, FITC-E5: 25 μM, and Dox: 10 μM) was determined by dialysis using a 100,000 Da molecular weight cut-off membrane (Millipore).

Activity Assay:

Article Title: Indoleamine 2,3-dioxygenase 1 (IDO1) activity in leukemia blasts correlates with poor outcome in childhood acute myeloid leukemia
Article Snippet: .. IDO1 activity Tryptophan and kynurenine levels were measured with reverse-phase HPLC (Agilent Technologies 1200; Waldbronn, Germany). ..

Mass Spectrometry:

Article Title: Anthocyanins Extracted from Oryza sativa L. Prevent Fluorouracil-Induced Nuclear Factor-κB Activation in Oral Mucositis: In Vitro and In Vivo Studies
Article Snippet: .. For HPLC-electrospray ionization (ESI) mass spectrometry (MS), ANT-rich extracts were separated and quantified by reverse-phase HPLC (Agilent model Model:1100 (Binary pump, Degasser, Autosample, DAD) using a Hypersil Gold C18 column (inner diameter, 3 μm; 4.6 × 150 mm; Thermo Fisher Scientific Inc., Waltham, MA, USA) following previous reporting [ ], with slight modifications. .. The column was eluted with a mobile phase consisting of formic acid (VWR International, Ltd., Leicestershire, UK) and methanol at a flow rate of 1 mL/min.

SDS Page:

Article Title: Solenodon genome reveals convergent evolution of venom in eulipotyphlan mammals
Article Snippet: .. Samples (1 mg) were separated via reverse-phase HPLC, then reduced and analyzed by SDS-PAGE, and protein bands subjected to in-gel tryptic digestion and analyzed by LC-MS/MS using an Orbitrap XL (Agilent, Germany). .. For top-down proteomics we used 0.2 mg of venom and saliva for reduced and nonreduced HPLC high-resolution (HR) MS/MS measurements.

Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 85
    Agilent technologies peptide elution reverse phase high performance liquid chromatography rp hplc purification
    Purification of MHC class II-associated peptides. A. <t>RP-HPLC</t> chromatogram of elution of the MHCII associated peptides. System: Agilent 1100, Column: Agilent ZORBAX 300SB-C18, Flow rate : 1 mL/min and a gradient was created by mixing Solvent A: 0.1% TFA (v/v) in CH3COOH(8.7%) and HCOOH(2.2%), pH1.9, and Solvent B: 0.08% TFA (v/v) in Acetonitrile; B. Dot blot of RP-HPLC fractions. 5 µL from each fraction was applied to a blotting membrane and I-A b molecules were detected as described in the text. C. Quantitative Imaging Analysis of MHCII positive fractions from <t>GILT-WT</t> and GILT−/− samples. MHC class II positive fractions from RP-HPLC were pooled for each sample and three different amounts (high: 25 µL, medium: 12.5 µL, and low: 6µL) from each pool were loaded onto SDS-PAGE gel for quantitative imaging. D. Flow cytometry analysis of GILT−/− and GILT-WT splenocytes. Spleens were isolated, ground and red blood cells lysed in hypertonic buffer. Washed and filtered splenocytes were incubated 30 min. on ice with anti-IA b M5/114–PE antibody.
    Peptide Elution Reverse Phase High Performance Liquid Chromatography Rp Hplc Purification, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/peptide elution reverse phase high performance liquid chromatography rp hplc purification/product/Agilent technologies
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    peptide elution reverse phase high performance liquid chromatography rp hplc purification - by Bioz Stars, 2020-07
    85/100 stars
      Buy from Supplier

    89
    Agilent technologies rp hplc purification
    Recombinant expression and characterization of <t>Tgu6.1</t> teretoxin. ( A ) Terebrid snail Terebra guttata from which the Tgu6.1 teretoxin was discovered. ( B ) Plasmid map of Tgu6.1 cloned into pET-32a Xa/ligation independent cloning (LIC) vector via LIC. ( C ) <t>RP-HPLC</t> purification of recombinant Tgu6.1 from its fusion tag after expression, purification and cleavage (top spectra); LC-MS analysis of Tgu6.1 (bottom spectra). ( D ) Characterization of Tgu6.1 bioactivity using the native prey polychaete worm assay (view the video in Supplemental Material ).
    Rp Hplc Purification, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 89/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rp hplc purification/product/Agilent technologies
    Average 89 stars, based on 15 article reviews
    Price from $9.99 to $1999.99
    rp hplc purification - by Bioz Stars, 2020-07
    89/100 stars
      Buy from Supplier

    93
    Agilent technologies agilent rp hplc system
    The purified rhMK was analyzed by SDS-PAGE with protein silver-staining and <t>RP-HPLC</t> (a) 1 μg of purified rhMK column fractions were load on SDS-PAGE and protein silver-staining; no other bands could be observed except the main band of rhMK. Lane M: low M w protein markers; Lanes 1~2: purified rhMK column fractions; (b) Reverse phase HPLC analysis of purified rhMK. Purified rhMK (5 μg) was analyzed by RP-HPLC, using <t>Agilent</t> ZORBAX StableBond-C18 column (150 mm×4.6 mm), which showed a single peak with a retention time of 6.533 min
    Agilent Rp Hplc System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/agilent rp hplc system/product/Agilent technologies
    Average 93 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    agilent rp hplc system - by Bioz Stars, 2020-07
    93/100 stars
      Buy from Supplier

    88
    Agilent technologies reverse phase high performance liquid chromatography hplc system
    Binding affinity assays of the selected phages encoding 7-mer peptides for human (HSA) and mouse (MSA) serium albumin, and preparation and identification of recombinant <t>RMP16.</t> ( A ) Selected phages encoding two 7-mer peptides were tested for binding HSA and MSA by ELISA. N12 represents the number of 10 12 phage particles, N11 ∼ N1 is the phage particles number by 4-fold serial dilution from 10 12 . ( B ) The construction map of the expression plasmid pKYB-RMP16. ( C ) The growth curve of the gene engineering E.coli pKYB-RMP16/ER2566. The SDS-PAGE ( D ) and ESI-MS ( E ) analysis of the prepared recombinant RMP16. ( F ) The HLPC analysis of the prepared recombinant RMP16. M: protein marker; 1: The prepared recombinant RMP16. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; <t>HPLC:</t> high-performance liquid chromatography; ESI-MS: electrospray ionization-mass spectrometry.
    Reverse Phase High Performance Liquid Chromatography Hplc System, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 88/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/reverse phase high performance liquid chromatography hplc system/product/Agilent technologies
    Average 88 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    reverse phase high performance liquid chromatography hplc system - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

    Image Search Results


    Purification of MHC class II-associated peptides. A. RP-HPLC chromatogram of elution of the MHCII associated peptides. System: Agilent 1100, Column: Agilent ZORBAX 300SB-C18, Flow rate : 1 mL/min and a gradient was created by mixing Solvent A: 0.1% TFA (v/v) in CH3COOH(8.7%) and HCOOH(2.2%), pH1.9, and Solvent B: 0.08% TFA (v/v) in Acetonitrile; B. Dot blot of RP-HPLC fractions. 5 µL from each fraction was applied to a blotting membrane and I-A b molecules were detected as described in the text. C. Quantitative Imaging Analysis of MHCII positive fractions from GILT-WT and GILT−/− samples. MHC class II positive fractions from RP-HPLC were pooled for each sample and three different amounts (high: 25 µL, medium: 12.5 µL, and low: 6µL) from each pool were loaded onto SDS-PAGE gel for quantitative imaging. D. Flow cytometry analysis of GILT−/− and GILT-WT splenocytes. Spleens were isolated, ground and red blood cells lysed in hypertonic buffer. Washed and filtered splenocytes were incubated 30 min. on ice with anti-IA b M5/114–PE antibody.

    Journal: PLoS ONE

    Article Title: Comparative Quantitative Mass Spectrometry Analysis of MHC Class II-Associated Peptides Reveals a Role of GILT in Formation of Self-Peptide Repertoire

    doi: 10.1371/journal.pone.0010599

    Figure Lengend Snippet: Purification of MHC class II-associated peptides. A. RP-HPLC chromatogram of elution of the MHCII associated peptides. System: Agilent 1100, Column: Agilent ZORBAX 300SB-C18, Flow rate : 1 mL/min and a gradient was created by mixing Solvent A: 0.1% TFA (v/v) in CH3COOH(8.7%) and HCOOH(2.2%), pH1.9, and Solvent B: 0.08% TFA (v/v) in Acetonitrile; B. Dot blot of RP-HPLC fractions. 5 µL from each fraction was applied to a blotting membrane and I-A b molecules were detected as described in the text. C. Quantitative Imaging Analysis of MHCII positive fractions from GILT-WT and GILT−/− samples. MHC class II positive fractions from RP-HPLC were pooled for each sample and three different amounts (high: 25 µL, medium: 12.5 µL, and low: 6µL) from each pool were loaded onto SDS-PAGE gel for quantitative imaging. D. Flow cytometry analysis of GILT−/− and GILT-WT splenocytes. Spleens were isolated, ground and red blood cells lysed in hypertonic buffer. Washed and filtered splenocytes were incubated 30 min. on ice with anti-IA b M5/114–PE antibody.

    Article Snippet: Peptide elution Reverse Phase High Performance Liquid Chromatography (RP-HPLC) purification of I-Ab containing GILT-WT and GILT−/− samples was performed on Agilent 1100 Chromatographic system (Agilent Technologies).

    Techniques: Purification, High Performance Liquid Chromatography, Flow Cytometry, Dot Blot, Imaging, SDS Page, Cytometry, Isolation, Incubation, IA

    Recombinant expression and characterization of Tgu6.1 teretoxin. ( A ) Terebrid snail Terebra guttata from which the Tgu6.1 teretoxin was discovered. ( B ) Plasmid map of Tgu6.1 cloned into pET-32a Xa/ligation independent cloning (LIC) vector via LIC. ( C ) RP-HPLC purification of recombinant Tgu6.1 from its fusion tag after expression, purification and cleavage (top spectra); LC-MS analysis of Tgu6.1 (bottom spectra). ( D ) Characterization of Tgu6.1 bioactivity using the native prey polychaete worm assay (view the video in Supplemental Material ).

    Journal: Toxins

    Article Title: Characterization and Recombinant Expression of Terebrid Venom Peptide from Terebra guttata

    doi: 10.3390/toxins8030063

    Figure Lengend Snippet: Recombinant expression and characterization of Tgu6.1 teretoxin. ( A ) Terebrid snail Terebra guttata from which the Tgu6.1 teretoxin was discovered. ( B ) Plasmid map of Tgu6.1 cloned into pET-32a Xa/ligation independent cloning (LIC) vector via LIC. ( C ) RP-HPLC purification of recombinant Tgu6.1 from its fusion tag after expression, purification and cleavage (top spectra); LC-MS analysis of Tgu6.1 (bottom spectra). ( D ) Characterization of Tgu6.1 bioactivity using the native prey polychaete worm assay (view the video in Supplemental Material ).

    Article Snippet: RP-HPLC Purification and Mass Spectrometry Cleaved Tgu6.1 was purified by RP-HPLC (Agilent, Santa Clara, CA, USA) using an X-Bridge C18 semi-preparative column (10 × 150 mm, 5-µm particle size, Waters Corporation, Milford, MA, USA) pre-equilibrated with 95% Buffer A (0.1% TFA).

    Techniques: Recombinant, Expressing, Plasmid Preparation, Clone Assay, Positron Emission Tomography, Ligation, High Performance Liquid Chromatography, Purification, Liquid Chromatography with Mass Spectroscopy

    Expression and purification of Tgu6.1. ( A ) 12% SDS-PAGE Coomassie-stained gel showing expression and purification of Tgu6.1 fusion protein by Ni-NTA affinity chromatography. M = protein molecular weight marker; Lane 1 = cell lysate; Lane 2 = supernatant post-binding to Ni-NTA resin; Lane 3 = Wash Buffer 1 supernatant; Lane 4 = Wash Buffer 2 supernatant; Lane 5 = imidazole eluted fraction. ( B ) Tris-tricine 16.5% SDS-PAGE Coomassie-stained gel showing Tgu6.1 cleavage by enterokinase. M = protein molecular weight marker; Lanes 1–3, enterokinase cleavage in 1:50, 1:20 and 1:10 dilutions. ( C ) Chromatogram of RP-HPLC purification of Tgu6.1 from TRX fusion tag. An X-Bridge C18 semi-preparative column was used with Buffer A (0.1% TFA) and Buffer B (80% ACN/0.1% TFA). The peptide was eluted with a linear gradient of 5%–75% Buffer B over 30 min at a flow rate of 5 mL/min. ( D ) LC-MS characterization of folded Tgu6.1. The +4, +5, +6 and +7 ion charge states are shown. Expected mass = 4758.58 Da. Observed mass = 4758.28 Da.

    Journal: Toxins

    Article Title: Characterization and Recombinant Expression of Terebrid Venom Peptide from Terebra guttata

    doi: 10.3390/toxins8030063

    Figure Lengend Snippet: Expression and purification of Tgu6.1. ( A ) 12% SDS-PAGE Coomassie-stained gel showing expression and purification of Tgu6.1 fusion protein by Ni-NTA affinity chromatography. M = protein molecular weight marker; Lane 1 = cell lysate; Lane 2 = supernatant post-binding to Ni-NTA resin; Lane 3 = Wash Buffer 1 supernatant; Lane 4 = Wash Buffer 2 supernatant; Lane 5 = imidazole eluted fraction. ( B ) Tris-tricine 16.5% SDS-PAGE Coomassie-stained gel showing Tgu6.1 cleavage by enterokinase. M = protein molecular weight marker; Lanes 1–3, enterokinase cleavage in 1:50, 1:20 and 1:10 dilutions. ( C ) Chromatogram of RP-HPLC purification of Tgu6.1 from TRX fusion tag. An X-Bridge C18 semi-preparative column was used with Buffer A (0.1% TFA) and Buffer B (80% ACN/0.1% TFA). The peptide was eluted with a linear gradient of 5%–75% Buffer B over 30 min at a flow rate of 5 mL/min. ( D ) LC-MS characterization of folded Tgu6.1. The +4, +5, +6 and +7 ion charge states are shown. Expected mass = 4758.58 Da. Observed mass = 4758.28 Da.

    Article Snippet: RP-HPLC Purification and Mass Spectrometry Cleaved Tgu6.1 was purified by RP-HPLC (Agilent, Santa Clara, CA, USA) using an X-Bridge C18 semi-preparative column (10 × 150 mm, 5-µm particle size, Waters Corporation, Milford, MA, USA) pre-equilibrated with 95% Buffer A (0.1% TFA).

    Techniques: Expressing, Purification, SDS Page, Staining, Affinity Chromatography, Molecular Weight, Marker, Binding Assay, High Performance Liquid Chromatography, Flow Cytometry, Liquid Chromatography with Mass Spectroscopy

    The purified rhMK was analyzed by SDS-PAGE with protein silver-staining and RP-HPLC (a) 1 μg of purified rhMK column fractions were load on SDS-PAGE and protein silver-staining; no other bands could be observed except the main band of rhMK. Lane M: low M w protein markers; Lanes 1~2: purified rhMK column fractions; (b) Reverse phase HPLC analysis of purified rhMK. Purified rhMK (5 μg) was analyzed by RP-HPLC, using Agilent ZORBAX StableBond-C18 column (150 mm×4.6 mm), which showed a single peak with a retention time of 6.533 min

    Journal: Journal of Zhejiang University. Science. B

    Article Title: Expression and purification of bioactive high-purity human midkine in Escherichia coli *

    doi: 10.1631/jzus.B0820385

    Figure Lengend Snippet: The purified rhMK was analyzed by SDS-PAGE with protein silver-staining and RP-HPLC (a) 1 μg of purified rhMK column fractions were load on SDS-PAGE and protein silver-staining; no other bands could be observed except the main band of rhMK. Lane M: low M w protein markers; Lanes 1~2: purified rhMK column fractions; (b) Reverse phase HPLC analysis of purified rhMK. Purified rhMK (5 μg) was analyzed by RP-HPLC, using Agilent ZORBAX StableBond-C18 column (150 mm×4.6 mm), which showed a single peak with a retention time of 6.533 min

    Article Snippet: The purity of the fractions was analyzed by an Agilent RP-HPLC system.

    Techniques: Purification, SDS Page, Silver Staining, High Performance Liquid Chromatography

    Binding affinity assays of the selected phages encoding 7-mer peptides for human (HSA) and mouse (MSA) serium albumin, and preparation and identification of recombinant RMP16. ( A ) Selected phages encoding two 7-mer peptides were tested for binding HSA and MSA by ELISA. N12 represents the number of 10 12 phage particles, N11 ∼ N1 is the phage particles number by 4-fold serial dilution from 10 12 . ( B ) The construction map of the expression plasmid pKYB-RMP16. ( C ) The growth curve of the gene engineering E.coli pKYB-RMP16/ER2566. The SDS-PAGE ( D ) and ESI-MS ( E ) analysis of the prepared recombinant RMP16. ( F ) The HLPC analysis of the prepared recombinant RMP16. M: protein marker; 1: The prepared recombinant RMP16. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; HPLC: high-performance liquid chromatography; ESI-MS: electrospray ionization-mass spectrometry.

    Journal: Scientific Reports

    Article Title: A novel recombinant slow-release TNF α-derived peptide effectively inhibits tumor growth and angiogensis

    doi: 10.1038/srep13595

    Figure Lengend Snippet: Binding affinity assays of the selected phages encoding 7-mer peptides for human (HSA) and mouse (MSA) serium albumin, and preparation and identification of recombinant RMP16. ( A ) Selected phages encoding two 7-mer peptides were tested for binding HSA and MSA by ELISA. N12 represents the number of 10 12 phage particles, N11 ∼ N1 is the phage particles number by 4-fold serial dilution from 10 12 . ( B ) The construction map of the expression plasmid pKYB-RMP16. ( C ) The growth curve of the gene engineering E.coli pKYB-RMP16/ER2566. The SDS-PAGE ( D ) and ESI-MS ( E ) analysis of the prepared recombinant RMP16. ( F ) The HLPC analysis of the prepared recombinant RMP16. M: protein marker; 1: The prepared recombinant RMP16. SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; HPLC: high-performance liquid chromatography; ESI-MS: electrospray ionization-mass spectrometry.

    Article Snippet: After chitin beads affinity chromatography purification for the cell lysate, RMP16 was purified and prepared by reverse-phase high-performance liquid chromatography (HPLC) system using 4.6 mm × 150 mm 300 SB-C18 Sep-Pak column (Agilent Technologies, Beijing, China) through gradient elution with increasing concentration of acetonitrile from 2% to 55% for 50 minutes at 1 ml/min.

    Techniques: Binding Assay, Recombinant, Enzyme-linked Immunosorbent Assay, Serial Dilution, Expressing, Plasmid Preparation, SDS Page, Mass Spectrometry, Marker, Polyacrylamide Gel Electrophoresis, High Performance Liquid Chromatography