ngc fplc system Search Results


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Bio-Rad fast protein liquid chromatography fplc system
Fast Protein Liquid Chromatography Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ngc fplc system
Ngc Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ngc quest 10plus fast protein liquid chromatography system
Yields and purities of individual BERAs produced on a large scale using the nCAR platform and isolated by <t> FPLC </t> method
Ngc Quest 10plus Fast Protein Liquid Chromatography System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ngc quest plus fplc system
Yields and purities of individual BERAs produced on a large scale using the nCAR platform and isolated by <t> FPLC </t> method
Ngc Quest Plus Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad bio rad ngc fplc system
Yields and purities of individual BERAs produced on a large scale using the nCAR platform and isolated by <t> FPLC </t> method
Bio Rad Ngc Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad fplc system
Yields and purities of individual BERAs produced on a large scale using the nCAR platform and isolated by <t> FPLC </t> method
Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Chrom Tech fplc chromatography system
Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by <t>RP-FPLC</t> resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange <t>chromatography</t> into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.
Fplc Chromatography System, supplied by Chrom Tech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ngc discovery tm 10 fplc system
Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by <t>RP-FPLC</t> resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange <t>chromatography</t> into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.
Ngc Discovery Tm 10 Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad 278 ngc fplc
Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by <t>RP-FPLC</t> resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange <t>chromatography</t> into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.
278 Ngc Fplc, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ngc scout fplc system
Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by <t>RP-FPLC</t> resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange <t>chromatography</t> into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.
Ngc Scout Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ngc questtm 10 fplc system
Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by <t>RP-FPLC</t> resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange <t>chromatography</t> into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.
Ngc Questtm 10 Fplc System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Bio-Rad ngc chromatography system quest 10
Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by <t>RP-FPLC</t> resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange <t>chromatography</t> into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.
Ngc Chromatography System Quest 10, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Yields and purities of individual BERAs produced on a large scale using the nCAR platform and isolated by  FPLC  method

Journal: The Journal of Pharmacology and Experimental Therapeutics

Article Title: Bioengineered Noncoding RNAs Selectively Change Cellular miRNome Profiles for Cancer Therapy

doi: 10.1124/jpet.118.247775

Figure Lengend Snippet: Yields and purities of individual BERAs produced on a large scale using the nCAR platform and isolated by FPLC method

Article Snippet: Large-scale purification of target BERA was performed with a NGC QUEST 10PLUS fast protein liquid chromatography system (Bio-Rad) equipped with an anion exchange Enrich-Q 10 × 100 column (Bio-Rad).

Techniques: Produced, Isolation

Three-step strategy to bioengineer ncRNA agents using nCAR. (A) In step 1, the ncRNAs of interest are cloned into the target vector (Supplemental Fig. S2), where the miR-34a duplex (red/green) is replaced by target sRNAs (e.g., miRNA, siRNA or antisense RNA, RNA aptamers, etc.) of interest. (B) In step 2, the verified plasmid is transformed into E. coli and total RNAs are isolated postfermentation for urea-PAGE analysis of target BERA expression. Among 42 target ncRNAs, 33 showed remarkable high-level expression (40%–80% of total RNAs). Total RNAs from untransformed wild-type bacteria (WT) are used for comparison. (C) Finally, in step 3, ncRNAs are isolated either on small scale using spin columns or large scale using fast protein liquid chromatography (FPLC) methods to offer micrograms or milligrams of BERAs, respectively. B, blank nontransformed E. coli; E, eluate; FT, flow through; T, total RNA; W1-2, washes. Fractions 1–11 were collected at various times during FPLC isolation. RNA purity was verified by high-performance liquid chromatography (HPLC) analysis (Supplemental Fig. S3), and both methods could offer >98% pure, ready-to-use BERAs.

Journal: The Journal of Pharmacology and Experimental Therapeutics

Article Title: Bioengineered Noncoding RNAs Selectively Change Cellular miRNome Profiles for Cancer Therapy

doi: 10.1124/jpet.118.247775

Figure Lengend Snippet: Three-step strategy to bioengineer ncRNA agents using nCAR. (A) In step 1, the ncRNAs of interest are cloned into the target vector (Supplemental Fig. S2), where the miR-34a duplex (red/green) is replaced by target sRNAs (e.g., miRNA, siRNA or antisense RNA, RNA aptamers, etc.) of interest. (B) In step 2, the verified plasmid is transformed into E. coli and total RNAs are isolated postfermentation for urea-PAGE analysis of target BERA expression. Among 42 target ncRNAs, 33 showed remarkable high-level expression (40%–80% of total RNAs). Total RNAs from untransformed wild-type bacteria (WT) are used for comparison. (C) Finally, in step 3, ncRNAs are isolated either on small scale using spin columns or large scale using fast protein liquid chromatography (FPLC) methods to offer micrograms or milligrams of BERAs, respectively. B, blank nontransformed E. coli; E, eluate; FT, flow through; T, total RNA; W1-2, washes. Fractions 1–11 were collected at various times during FPLC isolation. RNA purity was verified by high-performance liquid chromatography (HPLC) analysis (Supplemental Fig. S3), and both methods could offer >98% pure, ready-to-use BERAs.

Article Snippet: Large-scale purification of target BERA was performed with a NGC QUEST 10PLUS fast protein liquid chromatography system (Bio-Rad) equipped with an anion exchange Enrich-Q 10 × 100 column (Bio-Rad).

Techniques: Clone Assay, Plasmid Preparation, Transformation Assay, Isolation, Expressing, Bacteria, Comparison, Fast Protein Liquid Chromatography, High Performance Liquid Chromatography

Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by RP-FPLC resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange chromatography into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.

Journal: Toxins

Article Title: Colombian Scorpion Centruroides margaritatus : Purification and Characterization of a Gamma Potassium Toxin with Full-Block Activity on the hERG1 Channel

doi: 10.3390/toxins13060407

Figure Lengend Snippet: Purification of potassium channel toxins from the venom of Centruroides margaritatus . ( A ) Venom separation by RP-FPLC resulting in 41 fractions. Fraction F23 is active on hERG1 channels and is indicated by the red arrow. The inset shows an example of the hERG1 current (black line) and the blocking effect of F23 (red line). ( B ) Re-purification of the fraction F23; the pure peptide active on hERG1 is indicated by the asterisk and corresponds to the one with MW 4792.88 Da and called CmERG1. ( C – E ) Isolation of CmERG1 by means of a three-step protocol. First, gel filtration leads to three principal fractions FI, FII and FIII ( C ). From these, fraction FII was further separated by cation-exchange chromatography into 10 sub-fractions ( D ). Toxin CmERG1 was isolated by RP-HPLC from fractions FII.6 with a retention time of 27.4 min (indicated with a star in E). In C and D, the red arrow indicates the fraction separated in the subsequent step.

Article Snippet: The venom was fractionated by means of FPLC high performance liquid chromatography model NGC chromatography System, Chrom lab Model software, and Bio Frac automatic fraction collector (Bio Rad, Hercules, CA, USA).

Techniques: Purification, Blocking Assay, Isolation, Filtration, Chromatography

Mass-spectrometry analysis of the most abundant peaks obtained by  RP-FPLC.

Journal: Toxins

Article Title: Colombian Scorpion Centruroides margaritatus : Purification and Characterization of a Gamma Potassium Toxin with Full-Block Activity on the hERG1 Channel

doi: 10.3390/toxins13060407

Figure Lengend Snippet: Mass-spectrometry analysis of the most abundant peaks obtained by RP-FPLC.

Article Snippet: The venom was fractionated by means of FPLC high performance liquid chromatography model NGC chromatography System, Chrom lab Model software, and Bio Frac automatic fraction collector (Bio Rad, Hercules, CA, USA).

Techniques: