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Bio-Rad rnase free ddh2 o qpcr
<t>qPCR</t> validation and <t>RNase</t> R resistance test. ( a ) Sequencing results. *P
Rnase Free Ddh2 O Qpcr, 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
https://www.bioz.com/result/rnase free ddh2 o qpcr/product/Bio-Rad
Average 90 stars, based on 1 article reviews
Price from $9.99 to $1999.99
rnase free ddh2 o qpcr - by Bioz Stars, 2022-10
90/100 stars

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1) Product Images from "Genome-wide analysis of RNAs associated with Populus euphratica Oliv. heterophyll morphogenesis"

Article Title: Genome-wide analysis of RNAs associated with Populus euphratica Oliv. heterophyll morphogenesis

Journal: Scientific Reports

doi: 10.1038/s41598-018-35371-x

qPCR validation and RNase R resistance test. ( a ) Sequencing results. *P
Figure Legend Snippet: qPCR validation and RNase R resistance test. ( a ) Sequencing results. *P

Techniques Used: Real-time Polymerase Chain Reaction, Sequencing

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    Bio-Rad rnase free ddh2 o qpcr
    <t>qPCR</t> validation and <t>RNase</t> R resistance test. ( a ) Sequencing results. *P
    Rnase Free Ddh2 O Qpcr, 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
    https://www.bioz.com/result/rnase free ddh2 o qpcr/product/Bio-Rad
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rnase free ddh2 o qpcr - by Bioz Stars, 2022-10
    90/100 stars
      Buy from Supplier

    99
    Bio-Rad chemidoc mp imaging system
    MUC5B oligosaccharide-rich regions do not aggregate in the presence of excess EGCG. MUC5B T-domains were generated by trypsin-digestion and made to 200 µg/mL (A) and 600 µg/mL (B) before rate-zonal centrifugation with PBS (black circles) or 4 mM EGCG (grey triangles), in 5–20% (w/v) sucrose gradients. EGCG was removed from fractions using a HiTrap desalting column, fractions were slot blotted and PAS stained to detect glycoprotein (inset). Blots were scanned using Biorad <t>ChemiDoc</t> MP Imaging System and intensities measured using ImageLab software.
    Chemidoc Mp Imaging System, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad ddh2 o
    MUC5B oligosaccharide-rich regions do not aggregate in the presence of excess EGCG. MUC5B T-domains were generated by trypsin-digestion and made to 200 µg/mL (A) and 600 µg/mL (B) before rate-zonal centrifugation with PBS (black circles) or 4 mM EGCG (grey triangles), in 5–20% (w/v) sucrose gradients. EGCG was removed from fractions using a HiTrap desalting column, fractions were slot blotted and PAS stained to detect glycoprotein (inset). Blots were scanned using Biorad <t>ChemiDoc</t> MP Imaging System and intensities measured using ImageLab software.
    Ddh2 O, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    qPCR validation and RNase R resistance test. ( a ) Sequencing results. *P

    Journal: Scientific Reports

    Article Title: Genome-wide analysis of RNAs associated with Populus euphratica Oliv. heterophyll morphogenesis

    doi: 10.1038/s41598-018-35371-x

    Figure Lengend Snippet: qPCR validation and RNase R resistance test. ( a ) Sequencing results. *P

    Article Snippet: The qPCR system was as follows: 10 µL of TB GreenTM Premix Ex TaqTM , 2 µL of cDNA, 0.8 µL each of the upstream and downstream primers, and 6.4 µL of RNase-free ddH2 O. qPCR was carried out with Bio-Rad conditions: denaturation at 95 °C for 30 s, followed by 40 cycles at 95 °C for 5 s, 59 °C for 30 s, and 72 °C for 60 s.

    Techniques: Real-time Polymerase Chain Reaction, Sequencing

    MUC5B oligosaccharide-rich regions do not aggregate in the presence of excess EGCG. MUC5B T-domains were generated by trypsin-digestion and made to 200 µg/mL (A) and 600 µg/mL (B) before rate-zonal centrifugation with PBS (black circles) or 4 mM EGCG (grey triangles), in 5–20% (w/v) sucrose gradients. EGCG was removed from fractions using a HiTrap desalting column, fractions were slot blotted and PAS stained to detect glycoprotein (inset). Blots were scanned using Biorad ChemiDoc MP Imaging System and intensities measured using ImageLab software.

    Journal: PLoS ONE

    Article Title: Reorganisation of the Salivary Mucin Network by Dietary Components: Insights from Green Tea Polyphenols

    doi: 10.1371/journal.pone.0108372

    Figure Lengend Snippet: MUC5B oligosaccharide-rich regions do not aggregate in the presence of excess EGCG. MUC5B T-domains were generated by trypsin-digestion and made to 200 µg/mL (A) and 600 µg/mL (B) before rate-zonal centrifugation with PBS (black circles) or 4 mM EGCG (grey triangles), in 5–20% (w/v) sucrose gradients. EGCG was removed from fractions using a HiTrap desalting column, fractions were slot blotted and PAS stained to detect glycoprotein (inset). Blots were scanned using Biorad ChemiDoc MP Imaging System and intensities measured using ImageLab software.

    Article Snippet: Blots were then rinsed with ddH2 O, dried and scanned images were captured using a Biorad ChemiDoc MP Imaging System with Image Lab software (version 4.1).

    Techniques: Generated, Centrifugation, Staining, Imaging, Software

    Aggregation of MUC5B protein domains by EGCG. (A) Rate-zonal centrifugation of 380 µg/mL NT5B recombinant protein (D1-D2-D′-D3 domains of MUC5B) in PBS (black circles) or 4 mM EGCG (grey triangles) in 5–20% (w/v) sucrose gradients (n = 2). Sucrose gradients were fractionated into 21 fractions and pelleted material was solubilised in urea. Fractions were run on SDS-PAGE gels and silver stained. NT5B is expressed as a monomer and a dimer. Inset (i) shows the SDS-PAGE gel of the first 11 fractions of NT5B in PBS sucrose gradient, showing all NT5B was contained within the first 11 fractions. Inset (ii) shows the SDS-PAGE gel of fractions 12–21 and the pellet of an NT5B with EGCG gradient, showing that in the presence of EGCG all NT5B is pelleted to the bottom of the tube. (B) Rate-zonal centrifugation of 500 µg/mL CT5B recombinant protein (D4-B-C-CK domains of MUC5B) in PBS (black circles) or 4 mM EGCG (grey triangles) in 5–20% (w/v) sucrose gradients (n = 2). Gradients were fractionated into 19 fractions and pelleted material was solubilised in urea. Fractions were run on SDS-PAGE gels and Coomassie stained. CT5B is expressed as a monomer and a dimer. Inset (i) shows the SDS-PAGE of the first 10 fractions of a sucrose gradient of CT5B in PBS, showing all CT5B was present in the first 5 fractions. Insets (ii) and (iii) show the SDS-PAGE gels of fractions 1–10, and 11–19 and the pellet, respectively, showing that in the presence of EGCG, there is faster sedimentation of CT5B but not full aggregation. Stained SDS-PAGE gels were imaged on a Biorad ChemiDoc MP Imaging System to measure band intensities. Pel. = pelleted material.

    Journal: PLoS ONE

    Article Title: Reorganisation of the Salivary Mucin Network by Dietary Components: Insights from Green Tea Polyphenols

    doi: 10.1371/journal.pone.0108372

    Figure Lengend Snippet: Aggregation of MUC5B protein domains by EGCG. (A) Rate-zonal centrifugation of 380 µg/mL NT5B recombinant protein (D1-D2-D′-D3 domains of MUC5B) in PBS (black circles) or 4 mM EGCG (grey triangles) in 5–20% (w/v) sucrose gradients (n = 2). Sucrose gradients were fractionated into 21 fractions and pelleted material was solubilised in urea. Fractions were run on SDS-PAGE gels and silver stained. NT5B is expressed as a monomer and a dimer. Inset (i) shows the SDS-PAGE gel of the first 11 fractions of NT5B in PBS sucrose gradient, showing all NT5B was contained within the first 11 fractions. Inset (ii) shows the SDS-PAGE gel of fractions 12–21 and the pellet of an NT5B with EGCG gradient, showing that in the presence of EGCG all NT5B is pelleted to the bottom of the tube. (B) Rate-zonal centrifugation of 500 µg/mL CT5B recombinant protein (D4-B-C-CK domains of MUC5B) in PBS (black circles) or 4 mM EGCG (grey triangles) in 5–20% (w/v) sucrose gradients (n = 2). Gradients were fractionated into 19 fractions and pelleted material was solubilised in urea. Fractions were run on SDS-PAGE gels and Coomassie stained. CT5B is expressed as a monomer and a dimer. Inset (i) shows the SDS-PAGE of the first 10 fractions of a sucrose gradient of CT5B in PBS, showing all CT5B was present in the first 5 fractions. Insets (ii) and (iii) show the SDS-PAGE gels of fractions 1–10, and 11–19 and the pellet, respectively, showing that in the presence of EGCG, there is faster sedimentation of CT5B but not full aggregation. Stained SDS-PAGE gels were imaged on a Biorad ChemiDoc MP Imaging System to measure band intensities. Pel. = pelleted material.

    Article Snippet: Blots were then rinsed with ddH2 O, dried and scanned images were captured using a Biorad ChemiDoc MP Imaging System with Image Lab software (version 4.1).

    Techniques: Centrifugation, Recombinant, SDS Page, Staining, Sedimentation, Imaging