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dna template  (Thermo Fisher)


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    Structured Review

    Thermo Fisher dna template
    A schematic representation of the RAPID-M technology. The modified T7Term primer was mixed with the immobilization beads in <t>a</t> <t>PCR</t> microwell plate ( a ) to create beads-immobilized T7Term primer ( b ). The target <t>DNA</t> is directly immobilized to the beads by PCR amplification using beads-immobilized T7Term and soluble <t>T7Prom</t> to create high density immobilized DNA (HDID) in each well ( c ). The beads-immobilized DNA is translated to protein with the addition of cell-free reagents ( d , e ) and the protein is arrayed onto Ni–NTA slides using a microarray printer to produce high density protein microarray slides (HDS) ( f )
    Dna Template, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/microarray+bead+plate/DNA/pmc04642736-62-6-41
    Average 99 stars, based on 1 article reviews
    dna template - by Bioz Stars, 2026-10
    99/100 stars

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    1) Product Images from "Development of repeatable arrays of proteins using immobilized DNA microplate (RAPID-M) technology"

    Article Title: Development of repeatable arrays of proteins using immobilized DNA microplate (RAPID-M) technology

    Journal: BMC Research Notes

    doi: 10.1186/s13104-015-1637-3

    A schematic representation of the RAPID-M technology. The modified T7Term primer was mixed with the immobilization beads in a PCR microwell plate ( a ) to create beads-immobilized T7Term primer ( b ). The target DNA is directly immobilized to the beads by PCR amplification using beads-immobilized T7Term and soluble T7Prom to create high density immobilized DNA (HDID) in each well ( c ). The beads-immobilized DNA is translated to protein with the addition of cell-free reagents ( d , e ) and the protein is arrayed onto Ni–NTA slides using a microarray printer to produce high density protein microarray slides (HDS) ( f )
    Figure Legend Snippet: A schematic representation of the RAPID-M technology. The modified T7Term primer was mixed with the immobilization beads in a PCR microwell plate ( a ) to create beads-immobilized T7Term primer ( b ). The target DNA is directly immobilized to the beads by PCR amplification using beads-immobilized T7Term and soluble T7Prom to create high density immobilized DNA (HDID) in each well ( c ). The beads-immobilized DNA is translated to protein with the addition of cell-free reagents ( d , e ) and the protein is arrayed onto Ni–NTA slides using a microarray printer to produce high density protein microarray slides (HDS) ( f )

    Techniques Used: Modification, Amplification, Microarray

    Western blot analysis of GFP ( a ) and OmpA ( b ) proteins using beads-immobilized DNA template. Proteins were detected using peroxidase-conjugated anti-polyHistidine monoclonal antibody. The calculated protein sizes for GFP and OmpA are 30 and 27 kDa, respectively. DNA templates used for cell-free expression were as follows: a Lane 1 , gfp -SA beads template; lane 2 , gfp -CA beads template; lane 3 , soluble DNA coding for GFP (as positive control); lane 4 , no DNA template (as negative control). b Lane 1 , no DNA template (as negative control); lane 2 , ompA -CA beads template; lane 3 , ompA -SA beads template; lane 4 , soluble ompA protein coding DNA (as positive control)
    Figure Legend Snippet: Western blot analysis of GFP ( a ) and OmpA ( b ) proteins using beads-immobilized DNA template. Proteins were detected using peroxidase-conjugated anti-polyHistidine monoclonal antibody. The calculated protein sizes for GFP and OmpA are 30 and 27 kDa, respectively. DNA templates used for cell-free expression were as follows: a Lane 1 , gfp -SA beads template; lane 2 , gfp -CA beads template; lane 3 , soluble DNA coding for GFP (as positive control); lane 4 , no DNA template (as negative control). b Lane 1 , no DNA template (as negative control); lane 2 , ompA -CA beads template; lane 3 , ompA -SA beads template; lane 4 , soluble ompA protein coding DNA (as positive control)

    Techniques Used: Western Blot, Expressing, Positive Control, Negative Control

    Repetitive cell-free expression of GFP and OmpA proteins using immobilized DNA templates. a Lane 1 , GFP from soluble DNA (as positive control); lanes 2–5 , GFP protein from the first, second, third and fourth sequential rounds of cell-free expression using gfp -CA beads template; lanes 6-9 , GFP protein from the first, second, third and fourth sequential rounds of cell-free expression using gfp -SA beads template; lane 10 , no DNA template (as negative control). b Lanes 1–4 , OmpA protein from the first, second, third and fourth sequential rounds of cell-free expression using ompA -CA beads template; lane 5 , OmpA protein from soluble DNA (as positive control); lane 6 , no DNA template (as negative control)
    Figure Legend Snippet: Repetitive cell-free expression of GFP and OmpA proteins using immobilized DNA templates. a Lane 1 , GFP from soluble DNA (as positive control); lanes 2–5 , GFP protein from the first, second, third and fourth sequential rounds of cell-free expression using gfp -CA beads template; lanes 6-9 , GFP protein from the first, second, third and fourth sequential rounds of cell-free expression using gfp -SA beads template; lane 10 , no DNA template (as negative control). b Lanes 1–4 , OmpA protein from the first, second, third and fourth sequential rounds of cell-free expression using ompA -CA beads template; lane 5 , OmpA protein from soluble DNA (as positive control); lane 6 , no DNA template (as negative control)

    Techniques Used: Expressing, Positive Control, Negative Control

    Application of the RAPID-M method for generation of protein arrays. The proteins were printed using the Nano-Plotter™ NP 2.1. Immobilized proteins were in situ purified on Ni–NTA chip and subjected to detection using peroxidase-conjugated anti-polyHistidine antibody followed by addition of TSA-Cy5. Lane 1–4 , proteins from repetitive cycles of first, second, third and fourth rounds of cell-free expression using immobilized DNA template. Proteins are printed in 3 × 3 blocks and each block represents one cycle of cell-free expression using beads-immobilized DNA
    Figure Legend Snippet: Application of the RAPID-M method for generation of protein arrays. The proteins were printed using the Nano-Plotter™ NP 2.1. Immobilized proteins were in situ purified on Ni–NTA chip and subjected to detection using peroxidase-conjugated anti-polyHistidine antibody followed by addition of TSA-Cy5. Lane 1–4 , proteins from repetitive cycles of first, second, third and fourth rounds of cell-free expression using immobilized DNA template. Proteins are printed in 3 × 3 blocks and each block represents one cycle of cell-free expression using beads-immobilized DNA

    Techniques Used: In Situ, Purification, Expressing, Blocking Assay

    Related Articles

    other:

    Article Title: A national study confirms a low occurrence of antimicrobial resistance amongst Escherichia coli isolates from the caecae of Australian meat chickens
    Article Snippet: DNA was extracted using the MagMAX Multi-Sample DNA Extraction Kit (Thermo Fisher Scientific, USA), following the manufacturer’s instructions.

    Article Title: Integrative genomic analysis and gene expression patterns reveal a cardio-neuroendocrine signaling network for heat adaptation in geographically diverse chickens
    Article Snippet: DNA extraction was performed, checked for DNA quality using 1% agarose gel electrophoresis and NanoDrop 2000 (A260/280 ratio), and finally libraries were sequenced on the DNBSEQ-T7 platform.

    Concentration Assay:

    Article Title: Development of a high-resolution multiplex qPCR method to profile microbial consortia in spaceflight water recovery systems
    Article Snippet: 3 mL of broth culture from each strain was harvested by centrifugation and the genomic DNA was extracted using the DNeasy Blood & Tissue Kit (Qiagen), following the manufacturer's protocol for cultured cells. .. DNA concentration and purity were assessed using a NanoDrop spectrophotometer. ..

    Article Title: Integrated genomic, transcriptomic, and metabolomic profile analysis reveals molecular mechanism underlying meat quality traits in Chinese Kangle chickens
    Article Snippet: .. We extracted genomic DNA from blood samples using the phenol/chloroform method and quantified DNA concentration/quality using a Nanodrop-2000 spectrophotometer (Thermo Fisher Scientific, MA, USA). .. In total, 273 Chinese Kangle chickens were genotyped for 52,180 SNPs using the “Jingxin NO.1” 55 K Beadchip by following the manufacturer's protocol (Chinese Academy of Agricultural Sciences, Beijing, China) ( ).

    Spectrophotometry:

    Article Title: Development of a high-resolution multiplex qPCR method to profile microbial consortia in spaceflight water recovery systems
    Article Snippet: 3 mL of broth culture from each strain was harvested by centrifugation and the genomic DNA was extracted using the DNeasy Blood & Tissue Kit (Qiagen), following the manufacturer's protocol for cultured cells. .. DNA concentration and purity were assessed using a NanoDrop spectrophotometer. ..

    Article Title: Integrated genomic, transcriptomic, and metabolomic profile analysis reveals molecular mechanism underlying meat quality traits in Chinese Kangle chickens
    Article Snippet: .. We extracted genomic DNA from blood samples using the phenol/chloroform method and quantified DNA concentration/quality using a Nanodrop-2000 spectrophotometer (Thermo Fisher Scientific, MA, USA). .. In total, 273 Chinese Kangle chickens were genotyped for 52,180 SNPs using the “Jingxin NO.1” 55 K Beadchip by following the manufacturer's protocol (Chinese Academy of Agricultural Sciences, Beijing, China) ( ).

    Polymerase Chain Reaction:

    Article Title: Combinatorial engineering of enzyme and pathway for efficient β-farnesene bioproduction in Yarrowia lipolytica
    Article Snippet: The codon-optimized exogenous AaFS gene and its mutant variants synthesized by GenScript (Nanjing, China) were tailored for Y. lipolytica expression. .. PCR amplification was performed using primers listed in (Phusion® High-Fidelity DNA Polymerase, Thermo Fisher Scientific). ..

    Amplification:

    Article Title: Combinatorial engineering of enzyme and pathway for efficient β-farnesene bioproduction in Yarrowia lipolytica
    Article Snippet: The codon-optimized exogenous AaFS gene and its mutant variants synthesized by GenScript (Nanjing, China) were tailored for Y. lipolytica expression. .. PCR amplification was performed using primers listed in (Phusion® High-Fidelity DNA Polymerase, Thermo Fisher Scientific). ..

    Viscosity:

    Article Title: Protocol for the assessment of the impact of mycotoxins and glyphosate residues on the gut microbiome and resistome of European fallow deer
    Article Snippet: .. Qubit quantification indicated acceptable DNA concentrations; however, NanoDrop measurements showed low 260/230 ratios (e.g., 0.3–1.2), and the DNA exhibited a brown coloration and increased viscosity. ..

    Modification:

    Article Title: Amino acid starvation and iron limitation facilitate the biofilm formation of Klebsiella pneumoniae within urine
    Article Snippet: .. All enzymes required for restriction digestion and DNA modification were sourced from Thermo Fisher Scientific (Waltham, MA, USA) and handled in accordance with the supplier's protocols. ..

    Purification:

    Article Title: Identification of biofilm-associated genes in Arcobacter butzleri
    Article Snippet: For that, the DNA of the P8 strain was extracted using Lysing Matrix E tubes (MP Biomedicals, France) and a Bead Mill 4 Mini Homogenizer (Fisher Scientific, USA). .. After purification with AMPure XP beads (Beckman Coulter, USA), DNA quantification was performed by a Qubit fluorometer (Invitrogen, USA) using the Qubit 1X dsDNA HS assay kit (Invitrogen, USA). .. DNA libraries were then prepared using the Rapid Sequencing Kit V14 (Oxford Nanopore Technologies, UK) and loaded into a Flonge flow cell (Oxford Nanopore Technologies, UK) for sequencing.



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