afl iii  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 94

    Structured Review

    New England Biolabs afl iii
    Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI <t>III</t> for Pfmdr1 gene (86Y) in chloroquine resistant Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is <t>Afl</t> III and (R1- R4) are chloroquine resistant P. falciparum isolates.
    Afl Iii, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 17452 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/afl iii/product/New England Biolabs
    Average 94 stars, based on 17452 article reviews
    Price from $9.99 to $1999.99
    afl iii - by Bioz Stars, 2020-09
    94/100 stars

    Images

    1) Product Images from "Correlation of Molecular Markers, Pfmdr1-N86Y and Pfcrt-K76T, with In Vitro Chloroquine Resistant Plasmodium falciparum, Isolated in the Malaria Endemic States of Assam and Arunachal Pradesh, Northeast India"

    Article Title: Correlation of Molecular Markers, Pfmdr1-N86Y and Pfcrt-K76T, with In Vitro Chloroquine Resistant Plasmodium falciparum, Isolated in the Malaria Endemic States of Assam and Arunachal Pradesh, Northeast India

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0103848

    Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (86Y) in chloroquine resistant Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (R1- R4) are chloroquine resistant P. falciparum isolates.
    Figure Legend Snippet: Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (86Y) in chloroquine resistant Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (R1- R4) are chloroquine resistant P. falciparum isolates.

    Techniques Used: Polymerase Chain Reaction, Amplification

    Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (N86) in chloroquine sensitive Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (ST1-ST4) are chloroquine sensitive P. falciparum isolates.
    Figure Legend Snippet: Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (N86) in chloroquine sensitive Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (ST1-ST4) are chloroquine sensitive P. falciparum isolates.

    Techniques Used: Polymerase Chain Reaction, Amplification

    2) Product Images from "Isolation, nucleotide sequencing and genomic comparison of a Novel SXT/R391 ICE mobile genetic element isolated from a municipal wastewater environment"

    Article Title: Isolation, nucleotide sequencing and genomic comparison of a Novel SXT/R391 ICE mobile genetic element isolated from a municipal wastewater environment

    Journal: Scientific Reports

    doi: 10.1038/s41598-020-65216-5

    Restriction Fragment length polymorphism of the Proteus isolate, ULP014 (integrase positive), M:100 bp NEB Molecular weight marker, 1: Uncut DNA, 2: ULP014 ( Hpa II), 3: ULP014 ( Apo II), 4: ULP014 ( Tau I), 5: ICER391 ( Hpa II), 6: ICER391 ( Apo I), 7: ICER391 ( Tau I), 8: Control no enzyme “mock digest”.
    Figure Legend Snippet: Restriction Fragment length polymorphism of the Proteus isolate, ULP014 (integrase positive), M:100 bp NEB Molecular weight marker, 1: Uncut DNA, 2: ULP014 ( Hpa II), 3: ULP014 ( Apo II), 4: ULP014 ( Tau I), 5: ICER391 ( Hpa II), 6: ICER391 ( Apo I), 7: ICER391 ( Tau I), 8: Control no enzyme “mock digest”.

    Techniques Used: Molecular Weight, Marker

    3) Product Images from "An ovine hepatorenal fibrocystic model of a Meckel-like syndrome associated with dysmorphic primary cilia and TMEM67 mutations"

    Article Title: An ovine hepatorenal fibrocystic model of a Meckel-like syndrome associated with dysmorphic primary cilia and TMEM67 mutations

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-01519-4

    Identification of two missense mutations in TMEM67 . ( a ) Sequence analysis of TMEM67 showing sequence variants in exon 20 (indicated by asterisks above the sequence tracks) in a carrier, and in an affected lamb, compared to an unaffected lamb. Below the unaffected sequence, the Apo I restriction site is indicated (black bar) ( b ) Apo I restriction fragment length polymorphism generated by the sequence variants caused different restriction digestion patterns for the affected and carrier lambs, compared to unaffected lambs; M, marker; U, unaffected pattern; C, carrier pattern; A, affected pattern. ( c ) Alignment of mutant with wild type partial sequences of meckelin from multiple species. The diagram shows the isoleucine to asparagine amino acid substitution at position 681 (I681N), and isoleucine to serine substitution at position 687 (I687S) in an affected lamb (MKS sheep), compared to the unaffected ( Ovis aries ) meckelin sequence (boxed). The partial meckelin sequence is aligned with ten orthologous sequences from other species. The boxes show the affected amino acids, and conservation of an isoleucine amino acid at these positions in several vertebrate species, including humans and zebrafish. The amino acids in the grey portion mark the beginning of a transmembrane domain in meckelin.
    Figure Legend Snippet: Identification of two missense mutations in TMEM67 . ( a ) Sequence analysis of TMEM67 showing sequence variants in exon 20 (indicated by asterisks above the sequence tracks) in a carrier, and in an affected lamb, compared to an unaffected lamb. Below the unaffected sequence, the Apo I restriction site is indicated (black bar) ( b ) Apo I restriction fragment length polymorphism generated by the sequence variants caused different restriction digestion patterns for the affected and carrier lambs, compared to unaffected lambs; M, marker; U, unaffected pattern; C, carrier pattern; A, affected pattern. ( c ) Alignment of mutant with wild type partial sequences of meckelin from multiple species. The diagram shows the isoleucine to asparagine amino acid substitution at position 681 (I681N), and isoleucine to serine substitution at position 687 (I687S) in an affected lamb (MKS sheep), compared to the unaffected ( Ovis aries ) meckelin sequence (boxed). The partial meckelin sequence is aligned with ten orthologous sequences from other species. The boxes show the affected amino acids, and conservation of an isoleucine amino acid at these positions in several vertebrate species, including humans and zebrafish. The amino acids in the grey portion mark the beginning of a transmembrane domain in meckelin.

    Techniques Used: Sequencing, Generated, Marker, Mutagenesis

    4) Product Images from "Copper stress in Staphylococcus aureus leads to adaptive changes in central carbon metabolism leads to adaptive changes in central carbon metabolism †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8mt00239h"

    Article Title: Copper stress in Staphylococcus aureus leads to adaptive changes in central carbon metabolism leads to adaptive changes in central carbon metabolism †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8mt00239h

    Journal: Metallomics

    doi: 10.1039/c8mt00239h

    The GapA-associated copper pool is absent in the Δ gapA mutant strain. The S. aureus SH1000 wild type and the Δ gapA mutant strain were cultured in TM medium (0.5 L) with no added glucose but containing 50 μM CuSO 4 . Extracts were prepared and resolved under anaerobic conditions by AEC, and the fraction eluted by 400 mM NaCl from the wild type extract was found to contain most of the GAPDH activity. Aliquots (500 μL) of the 400 mM NaCl AEC fractions from each strain were further resolved by SEC on a Superdex 200 Increase column in 10 mM Tris, 150 mM NaCl, pH 7.5. SEC fractions were analysed for copper (blue circles: closed = WT, open = Δ gapA mutant) by ICP-MS and for GAPDH activity using an enzyme assay (black triangles) (A). Note that the SEC fractions from the Δ gapA mutant strain were devoid of GAPDH activity (data not shown). SDS-PAGE analysis of selected SEC fractions from both the wild type (B) and the Δ gapA mutant (C) confirmed that the protein distribution was essentially unchanged between the two chromatographs, with the exception of the presence of the ∼36 kDa GapA band (highlighted by a red asterisk) in the wild type fractions that was absent in the Δ gapA mutant samples (also indicated with a red asterisk).
    Figure Legend Snippet: The GapA-associated copper pool is absent in the Δ gapA mutant strain. The S. aureus SH1000 wild type and the Δ gapA mutant strain were cultured in TM medium (0.5 L) with no added glucose but containing 50 μM CuSO 4 . Extracts were prepared and resolved under anaerobic conditions by AEC, and the fraction eluted by 400 mM NaCl from the wild type extract was found to contain most of the GAPDH activity. Aliquots (500 μL) of the 400 mM NaCl AEC fractions from each strain were further resolved by SEC on a Superdex 200 Increase column in 10 mM Tris, 150 mM NaCl, pH 7.5. SEC fractions were analysed for copper (blue circles: closed = WT, open = Δ gapA mutant) by ICP-MS and for GAPDH activity using an enzyme assay (black triangles) (A). Note that the SEC fractions from the Δ gapA mutant strain were devoid of GAPDH activity (data not shown). SDS-PAGE analysis of selected SEC fractions from both the wild type (B) and the Δ gapA mutant (C) confirmed that the protein distribution was essentially unchanged between the two chromatographs, with the exception of the presence of the ∼36 kDa GapA band (highlighted by a red asterisk) in the wild type fractions that was absent in the Δ gapA mutant samples (also indicated with a red asterisk).

    Techniques Used: Mutagenesis, Cell Culture, Activity Assay, Size-exclusion Chromatography, Mass Spectrometry, Enzymatic Assay, SDS Page

    S. aureus cells cultured in the presence of copper exhibit reduced GAPDH activity. S. aureus SH1000 cells were cultured in TSB medium in the absence (control sample – 1, black) or presence (high [Cu] sample – 2, dark blue) of 0.5 mM CuSO 4 . The cells were washed extensively in EDTA, and then lysed in the absence of EDTA, and the extracts assayed for GAPDH activity, demonstrating a reduction in enzymatic activity in cells cultured in the presence of elevated copper. The lysate that was prepared from cells cultured in the presence of copper was subsequently treated in vitro with a copper chelator, through anaerobic incubation of the extract for 10 min in the presence of 100 μM BCS (light blue), which resulted in increased GAPDH activity, implying Cu( i ) chelation had alleviated GAPDH inhibition. Likewise, anaerobic incubation of the control lysate with 10 μM Cu( i ) (dark grey) reduced the activity, which was reversed on subsequent addition of BCS (light grey).
    Figure Legend Snippet: S. aureus cells cultured in the presence of copper exhibit reduced GAPDH activity. S. aureus SH1000 cells were cultured in TSB medium in the absence (control sample – 1, black) or presence (high [Cu] sample – 2, dark blue) of 0.5 mM CuSO 4 . The cells were washed extensively in EDTA, and then lysed in the absence of EDTA, and the extracts assayed for GAPDH activity, demonstrating a reduction in enzymatic activity in cells cultured in the presence of elevated copper. The lysate that was prepared from cells cultured in the presence of copper was subsequently treated in vitro with a copper chelator, through anaerobic incubation of the extract for 10 min in the presence of 100 μM BCS (light blue), which resulted in increased GAPDH activity, implying Cu( i ) chelation had alleviated GAPDH inhibition. Likewise, anaerobic incubation of the control lysate with 10 μM Cu( i ) (dark grey) reduced the activity, which was reversed on subsequent addition of BCS (light grey).

    Techniques Used: Cell Culture, Activity Assay, In Vitro, Incubation, Inhibition

    High concentrations of copper inhibit the growth of S. aureus . Wild type S. aureus SH1000 were inoculated to a starting OD 595nm of 0.03 into (A) two types of rich media, tryptic soy broth (TSB – black bars) or LB (grey bars), or (B) two types of minimal media, glucose-containing chemically defined medium (CDM – black bars) or Tris-minimal (TM) medium lacking glucose (grey bars), each supplemented with increasing concentrations of CuSO 4 . The cultures were incubated for 5 h at 37 °C with orbital shaking (180 rpm), and the final OD 595nm values were recorded. Growth is inhibited by high levels of copper in all media, but this toxicity effect is greatest in the minimal media. The symbols represent statistical significance based on a Student's t -test, where ns = not significant, * = p
    Figure Legend Snippet: High concentrations of copper inhibit the growth of S. aureus . Wild type S. aureus SH1000 were inoculated to a starting OD 595nm of 0.03 into (A) two types of rich media, tryptic soy broth (TSB – black bars) or LB (grey bars), or (B) two types of minimal media, glucose-containing chemically defined medium (CDM – black bars) or Tris-minimal (TM) medium lacking glucose (grey bars), each supplemented with increasing concentrations of CuSO 4 . The cultures were incubated for 5 h at 37 °C with orbital shaking (180 rpm), and the final OD 595nm values were recorded. Growth is inhibited by high levels of copper in all media, but this toxicity effect is greatest in the minimal media. The symbols represent statistical significance based on a Student's t -test, where ns = not significant, * = p

    Techniques Used: Incubation

    S. aureus cells accumulate additional copper when cultured in high concentrations of copper. Wild type S. aureus SH1000 were inoculated to a starting OD 595nm of 0.05 into TM media (containing glucose) either with (Cu-treated) or without (control) the addition of 1 mM CuSO 4 , and incubated for 6 h at 37 °C with 180 rpm orbital shaking. Cell densities were determined by OD 595nm , and equal cell numbers were harvested, washed to remove surface-bound metals, digested in concentrated HNO 3 , and elemental composition of the resulting acid lysates was determined by ICP-MS. The symbols represent statistical significance, based on a Student's t -test, where *** = p
    Figure Legend Snippet: S. aureus cells accumulate additional copper when cultured in high concentrations of copper. Wild type S. aureus SH1000 were inoculated to a starting OD 595nm of 0.05 into TM media (containing glucose) either with (Cu-treated) or without (control) the addition of 1 mM CuSO 4 , and incubated for 6 h at 37 °C with 180 rpm orbital shaking. Cell densities were determined by OD 595nm , and equal cell numbers were harvested, washed to remove surface-bound metals, digested in concentrated HNO 3 , and elemental composition of the resulting acid lysates was determined by ICP-MS. The symbols represent statistical significance, based on a Student's t -test, where *** = p

    Techniques Used: Cell Culture, Incubation, Mass Spectrometry

    Purification of copper-associated GapA from extracts of copper-exposed S. aureus cells. S. aureus SH1000 cells (biomass from a total of 2.5 L culture) were cultured in TSB medium containing 50 μM CuSO 4 , harvested and washed as described (see Methods). Cell extract was prepared and resolved by liquid chromatography under anaerobic conditions. The soluble cell fraction was initially passed through a hydroxyapatite column in 5 mM sodium phosphate, pH 6.8 (data not shown), and then the unbound flow-through fraction was buffer exchanged into 10 mM Tris, pH 7.5. (A) This flow-through was subsequently resolved by anion exchange chromatography (AEC) at pH 7.5 on a 1 mL AEC column, eluted with a linear [NaCl] gradient (grey dashed line, 0–1 M NaCl), and fractions analysed for protein content by A 280nm (black triangles) and for copper (blue circles) by ICP-MS. (B) An aliquot (500 μL) of the peak copper-containing fraction from AEC was subsequently resolved by SEC on a Superdex 200 Increase column in 20 mM Tris, pH 7.5, 150 mM NaCl, analysed for protein by A 280nm (black) and for copper by ICP-MS (blue). (C) Fractions around the copper peak were analysed by SDS-PAGE, and the protein band identified by peptide mass fingerprinting as GapA is indicated by an arrow. (D) Selected fractions were also assayed for GAPDH activity (red squares), which co-migrated with the copper.
    Figure Legend Snippet: Purification of copper-associated GapA from extracts of copper-exposed S. aureus cells. S. aureus SH1000 cells (biomass from a total of 2.5 L culture) were cultured in TSB medium containing 50 μM CuSO 4 , harvested and washed as described (see Methods). Cell extract was prepared and resolved by liquid chromatography under anaerobic conditions. The soluble cell fraction was initially passed through a hydroxyapatite column in 5 mM sodium phosphate, pH 6.8 (data not shown), and then the unbound flow-through fraction was buffer exchanged into 10 mM Tris, pH 7.5. (A) This flow-through was subsequently resolved by anion exchange chromatography (AEC) at pH 7.5 on a 1 mL AEC column, eluted with a linear [NaCl] gradient (grey dashed line, 0–1 M NaCl), and fractions analysed for protein content by A 280nm (black triangles) and for copper (blue circles) by ICP-MS. (B) An aliquot (500 μL) of the peak copper-containing fraction from AEC was subsequently resolved by SEC on a Superdex 200 Increase column in 20 mM Tris, pH 7.5, 150 mM NaCl, analysed for protein by A 280nm (black) and for copper by ICP-MS (blue). (C) Fractions around the copper peak were analysed by SDS-PAGE, and the protein band identified by peptide mass fingerprinting as GapA is indicated by an arrow. (D) Selected fractions were also assayed for GAPDH activity (red squares), which co-migrated with the copper.

    Techniques Used: Purification, Cell Culture, Liquid Chromatography, Flow Cytometry, Chromatography, Mass Spectrometry, Size-exclusion Chromatography, SDS Page, Peptide Mass Fingerprinting, Activity Assay

    Metal distribution in S. aureus cytosolic extracts. Cytosolic extracts were prepared from S. aureus SH1000 cells, cultured in TSB medium either (A) without or (B) with addition of 500 μM CuSO 4 . Extracts were resolved by anion exchange chromatography (1 mL HiTrap Q HP column) in 20 mM Hepes, pH 8.0, and eluted with stepwise increases in NaCl concentration. Resulting fractions were subjected to a second dimension of separation by HPLC size exclusion chromatography (SW3000 column) in 5 mM Hepes, 50 mM NaCl, pH 7.5. Elemental composition of the resulting fractions were determined by ICP-MS, shown by the height of the peaks on the z -axis. Accumulation of copper in one major pool was observed in cells cultured in excess copper, whereas the accumulation of zinc was decreased in high molecular weight pools. Manganese accumulation was unchanged. All lysate preparation and chromatography steps were performed under anaerobic conditions.
    Figure Legend Snippet: Metal distribution in S. aureus cytosolic extracts. Cytosolic extracts were prepared from S. aureus SH1000 cells, cultured in TSB medium either (A) without or (B) with addition of 500 μM CuSO 4 . Extracts were resolved by anion exchange chromatography (1 mL HiTrap Q HP column) in 20 mM Hepes, pH 8.0, and eluted with stepwise increases in NaCl concentration. Resulting fractions were subjected to a second dimension of separation by HPLC size exclusion chromatography (SW3000 column) in 5 mM Hepes, 50 mM NaCl, pH 7.5. Elemental composition of the resulting fractions were determined by ICP-MS, shown by the height of the peaks on the z -axis. Accumulation of copper in one major pool was observed in cells cultured in excess copper, whereas the accumulation of zinc was decreased in high molecular weight pools. Manganese accumulation was unchanged. All lysate preparation and chromatography steps were performed under anaerobic conditions.

    Techniques Used: Cell Culture, Chromatography, Concentration Assay, High Performance Liquid Chromatography, Size-exclusion Chromatography, Mass Spectrometry, Molecular Weight

    5) Product Images from "Characterization and Expression Analysis of a Fiber Differentially Expressed Fasciclin-like Arabinogalactan Protein Gene in Sea Island Cotton Fibers"

    Article Title: Characterization and Expression Analysis of a Fiber Differentially Expressed Fasciclin-like Arabinogalactan Protein Gene in Sea Island Cotton Fibers

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0070185

    Visualized differentially expressed TDFs between Sea Island cotton fibers and Upland cotton fibers in cDNA-AFLP analyses. Lane 1 to 3 show Upland cotton ( G. hirsutum cv. CRI 8) fibers and Lane 4 to 6 show Sea Island cotton ( G . barbadense cv. Pima90-53) fibers. Eco RI/ Mse I and Apo I/ Taq I are the restriction enzyme combinations used in cDNA-AFLP analyses. Arrowheads show the differentially expressed FLA TDFs.
    Figure Legend Snippet: Visualized differentially expressed TDFs between Sea Island cotton fibers and Upland cotton fibers in cDNA-AFLP analyses. Lane 1 to 3 show Upland cotton ( G. hirsutum cv. CRI 8) fibers and Lane 4 to 6 show Sea Island cotton ( G . barbadense cv. Pima90-53) fibers. Eco RI/ Mse I and Apo I/ Taq I are the restriction enzyme combinations used in cDNA-AFLP analyses. Arrowheads show the differentially expressed FLA TDFs.

    Techniques Used: cDNA-AFLP Assay

    6) Product Images from "Characterization and Expression Analysis of a Fiber Differentially Expressed Fasciclin-like Arabinogalactan Protein Gene in Sea Island Cotton Fibers"

    Article Title: Characterization and Expression Analysis of a Fiber Differentially Expressed Fasciclin-like Arabinogalactan Protein Gene in Sea Island Cotton Fibers

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0070185

    Visualized differentially expressed TDFs between Sea Island cotton fibers and Upland cotton fibers in cDNA-AFLP analyses. Lane 1 to 3 show Upland cotton ( G. hirsutum cv. CRI 8) fibers and Lane 4 to 6 show Sea Island cotton ( G . barbadense cv. Pima90-53) fibers. Eco RI/ Mse I and Apo I/ Taq I are the restriction enzyme combinations used in cDNA-AFLP analyses. Arrowheads show the differentially expressed FLA TDFs.
    Figure Legend Snippet: Visualized differentially expressed TDFs between Sea Island cotton fibers and Upland cotton fibers in cDNA-AFLP analyses. Lane 1 to 3 show Upland cotton ( G. hirsutum cv. CRI 8) fibers and Lane 4 to 6 show Sea Island cotton ( G . barbadense cv. Pima90-53) fibers. Eco RI/ Mse I and Apo I/ Taq I are the restriction enzyme combinations used in cDNA-AFLP analyses. Arrowheads show the differentially expressed FLA TDFs.

    Techniques Used: cDNA-AFLP Assay

    Full length cDNA sequence of GbFLA5 and its deduced amino acid residues. Nucleotides underlined indicate the start codon of “ATG”, the effectively restriction site in cDNA-AFLP analysis (GAATTC for Eco RI and Apo I, TTAA for Mse I and TCGA for Taq I), and the stop codon of “TGA”, respectively; three conserved regions (H1, H2 and [YA] H) of smart00554 motif were ordinal characterized by wavy line; AGP-like domains are shown by the dashed line.
    Figure Legend Snippet: Full length cDNA sequence of GbFLA5 and its deduced amino acid residues. Nucleotides underlined indicate the start codon of “ATG”, the effectively restriction site in cDNA-AFLP analysis (GAATTC for Eco RI and Apo I, TTAA for Mse I and TCGA for Taq I), and the stop codon of “TGA”, respectively; three conserved regions (H1, H2 and [YA] H) of smart00554 motif were ordinal characterized by wavy line; AGP-like domains are shown by the dashed line.

    Techniques Used: Sequencing, cDNA-AFLP Assay

    7) Product Images from "Sequence analysis of pfcrt and pfmdr1 genes and its association with chloroquine resistance in Southeast Indian Plasmodium falciparum isolates"

    Article Title: Sequence analysis of pfcrt and pfmdr1 genes and its association with chloroquine resistance in Southeast Indian Plasmodium falciparum isolates

    Journal: Genomics Data

    doi: 10.1016/j.gdata.2016.04.010

    Linkage disequilibrium plot between the SNPs pairs of pfcrt and pfmdr1 gene in Indian P. falciparum . The intergenic and intragenic association between the genes were illustrated using the LD plot for isolates collected from (a) Puducherry and (b) Odisha regions. The strength of LD between the SNPs is determined by the association of statistical significance by calculating the r 2 values and represented by the darkness of the boxes.
    Figure Legend Snippet: Linkage disequilibrium plot between the SNPs pairs of pfcrt and pfmdr1 gene in Indian P. falciparum . The intergenic and intragenic association between the genes were illustrated using the LD plot for isolates collected from (a) Puducherry and (b) Odisha regions. The strength of LD between the SNPs is determined by the association of statistical significance by calculating the r 2 values and represented by the darkness of the boxes.

    Techniques Used:

    Distribution of pfcrt and pfmdr1 alleles P. falciparum isolates collected from Puducherry and Odisha, India. K76T mutation in the pfcrt gene showed higher frequency associated with CQ-resistance. However, in the pfmdr1 gene, the Y184F mutation showed a higher distribution of frequency.
    Figure Legend Snippet: Distribution of pfcrt and pfmdr1 alleles P. falciparum isolates collected from Puducherry and Odisha, India. K76T mutation in the pfcrt gene showed higher frequency associated with CQ-resistance. However, in the pfmdr1 gene, the Y184F mutation showed a higher distribution of frequency.

    Techniques Used: Mutagenesis

    8) Product Images from "Correlation of Molecular Markers, Pfmdr1-N86Y and Pfcrt-K76T, with In Vitro Chloroquine Resistant Plasmodium falciparum, Isolated in the Malaria Endemic States of Assam and Arunachal Pradesh, Northeast India"

    Article Title: Correlation of Molecular Markers, Pfmdr1-N86Y and Pfcrt-K76T, with In Vitro Chloroquine Resistant Plasmodium falciparum, Isolated in the Malaria Endemic States of Assam and Arunachal Pradesh, Northeast India

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0103848

    Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (86Y) in chloroquine resistant Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (R1- R4) are chloroquine resistant P. falciparum isolates.
    Figure Legend Snippet: Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (86Y) in chloroquine resistant Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (R1- R4) are chloroquine resistant P. falciparum isolates.

    Techniques Used: Polymerase Chain Reaction, Amplification

    Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (N86) in chloroquine sensitive Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (ST1-ST4) are chloroquine sensitive P. falciparum isolates.
    Figure Legend Snippet: Representative photomicrograph showing the results of RFLP after digestion of PCR amplified product with endonucleases, Apo1 and AfI III for Pfmdr1 gene (N86) in chloroquine sensitive Plasmodium falciparum isolates. In photograph, (M) is 100 bp DNA ladder; (C) is undigested product as control; (P) is Apo1; (F) is Afl III and (ST1-ST4) are chloroquine sensitive P. falciparum isolates.

    Techniques Used: Polymerase Chain Reaction, Amplification

    9) Product Images from "Sequence analysis of pfcrt and pfmdr1 genes and its association with chloroquine resistance in Southeast Indian Plasmodium falciparum isolates"

    Article Title: Sequence analysis of pfcrt and pfmdr1 genes and its association with chloroquine resistance in Southeast Indian Plasmodium falciparum isolates

    Journal: Genomics Data

    doi: 10.1016/j.gdata.2016.04.010

    Linkage disequilibrium plot between the SNPs pairs of pfcrt and pfmdr1 gene in Indian P. falciparum . The intergenic and intragenic association between the genes were illustrated using the LD plot for isolates collected from (a) Puducherry and (b) Odisha regions. The strength of LD between the SNPs is determined by the association of statistical significance by calculating the r 2 values and represented by the darkness of the boxes.
    Figure Legend Snippet: Linkage disequilibrium plot between the SNPs pairs of pfcrt and pfmdr1 gene in Indian P. falciparum . The intergenic and intragenic association between the genes were illustrated using the LD plot for isolates collected from (a) Puducherry and (b) Odisha regions. The strength of LD between the SNPs is determined by the association of statistical significance by calculating the r 2 values and represented by the darkness of the boxes.

    Techniques Used:

    Distribution of pfcrt and pfmdr1 alleles P. falciparum isolates collected from Puducherry and Odisha, India. K76T mutation in the pfcrt gene showed higher frequency associated with CQ-resistance. However, in the pfmdr1 gene, the Y184F mutation showed a higher distribution of frequency.
    Figure Legend Snippet: Distribution of pfcrt and pfmdr1 alleles P. falciparum isolates collected from Puducherry and Odisha, India. K76T mutation in the pfcrt gene showed higher frequency associated with CQ-resistance. However, in the pfmdr1 gene, the Y184F mutation showed a higher distribution of frequency.

    Techniques Used: Mutagenesis

    Related Articles

    Amplification:

    Article Title: Correlation of Molecular Markers, Pfmdr1-N86Y and Pfcrt-K76T, with In Vitro Chloroquine Resistant Plasmodium falciparum, Isolated in the Malaria Endemic States of Assam and Arunachal Pradesh, Northeast India
    Article Snippet: .. Restriction Digestion with ApoI and Afl III The finally amplified product was subjected to restriction digestion with Afl III (mutational allele) and Apo I (wild type allele) (New England Biolabs, UK) by incubating at 37°C for one hour with the one unit of each enzyme. .. The digests were resolved on 3% agarose gel, stained with ethidium bromide, and results were recorded on the gel documentation system (UVITEC, UK).

    DNA Synthesis:

    Article Title: The mechanism of DNA replication termination in vertebrates
    Article Snippet: .. To monitor DNA synthesis within a lacO array , 0.25–1.0 ng/µl of purified DNA was incubated in Buffer 3.1 with 0.2 units/µl PvuII and 0.2 units/µl AflIII (New England BioLabs) at 37°C for 1 hour. ..

    Southern Blot:

    Article Title: Development and validation of a multiplex-PCR assay for X-linked intellectual disability
    Article Snippet: .. Southern blot genotyping was done using ~10 μg of gDNA double-digested with the restriction enzymes EcoRI and EagI for FMR1 gene or AflIII and NotI for AFF2 gene (New England Biolabs, Ipswich, MA, USA). .. Further, the digested gDNA products were electrophoresed in parallel with a 1:1 mixture of the standard size markers, DNA Molecular Weight Marker II and III digoxigenin-labeled (Roche Applied Science, Indianapolis, IN, USA), blotted and hybridized using the FMR1 or the AFF2 digoxigenin-labeled specific probes, GLFXDIG1 or AJ31Dig1, as appropriate (Gene Link™, Hawthorne, NY, USA).

    Purification:

    Article Title: The mechanism of DNA replication termination in vertebrates
    Article Snippet: .. To monitor DNA synthesis within a lacO array , 0.25–1.0 ng/µl of purified DNA was incubated in Buffer 3.1 with 0.2 units/µl PvuII and 0.2 units/µl AflIII (New England BioLabs) at 37°C for 1 hour. ..

    Transgenic Assay:

    Article Title: Low-cost production of proinsulin in tobacco and lettuce chloroplasts for injectable or oral delivery of functional insulin and C-peptide
    Article Snippet: .. Transgenic and untransformed tobacco DNA was digested using AflIII, and lettuce DNA was digested using BglII in a reaction mixture containing 2 μL 10× buffer (New England Biolabs, Ipswich, MA), 3 μg plant genomic DNA, 2 μL BSA and 1 μL enzyme made up to 20 μL with dH2 O. .. Southern analysis was performed according to laboratory protocol ( ).

    Incubation:

    Article Title: Clinically Relevant Outcome Measures for the I307N Rhodopsin Mouse: A Model of Inducible Autosomal Dominant Retinitis Pigmentosa
    Article Snippet: .. The I307N Rho PCR-fragment, when incubated with AflIII (New England Biolabs, Ipswich, MA, USA), liberates two fragments of approximately 150 and 110 base-pairs. .. The WT Rho PCR-fragment retina retains the full 260 base-pair length.

    Article Title: The mechanism of DNA replication termination in vertebrates
    Article Snippet: .. To monitor DNA synthesis within a lacO array , 0.25–1.0 ng/µl of purified DNA was incubated in Buffer 3.1 with 0.2 units/µl PvuII and 0.2 units/µl AflIII (New England BioLabs) at 37°C for 1 hour. ..

    Polymerase Chain Reaction:

    Article Title: Clinically Relevant Outcome Measures for the I307N Rhodopsin Mouse: A Model of Inducible Autosomal Dominant Retinitis Pigmentosa
    Article Snippet: .. The I307N Rho PCR-fragment, when incubated with AflIII (New England Biolabs, Ipswich, MA, USA), liberates two fragments of approximately 150 and 110 base-pairs. .. The WT Rho PCR-fragment retina retains the full 260 base-pair length.

    Article Title: A tale of two haplotype groups: Evaluating the New World Junonia ring species hypothesis using the distribution of divergent COI haplotypes
    Article Snippet: .. PCR products of the correct size were evaluated by a triple digest using BseYI, AflIII, and BamHI restriction endonucleases (New England Biolabs, Ipswich, MA, USA) ( ). .. A 10 µL aliquot of the PCR product was incubated with 10 µL of the triple digest cocktail (2 µL of NEB Buffer3, 2 µL of BSA (10×, 1 mg/mL), 4 µL of ddH2 O, 0.5 µL of BseYI, 0.5 µL of AflIII and 1 µL of BamHI) for 1 hour in a 37°C water bath.

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 85
    New England Biolabs restriction enzyme apo i
    Identification of two missense mutations in TMEM67 . ( a ) Sequence analysis of TMEM67 showing sequence variants in exon 20 (indicated by asterisks above the sequence tracks) in a carrier, and in an affected lamb, compared to an unaffected lamb. Below the unaffected sequence, the <t>Apo</t> I restriction site is indicated (black bar) ( b ) Apo I restriction fragment length polymorphism generated by the sequence variants caused different restriction digestion patterns for the affected and carrier lambs, compared to unaffected lambs; M, marker; U, unaffected pattern; C, carrier pattern; A, affected pattern. ( c ) Alignment of mutant with wild type partial sequences of meckelin from multiple species. The diagram shows the isoleucine to asparagine amino acid substitution at position 681 (I681N), and isoleucine to serine substitution at position 687 (I687S) in an affected lamb (MKS sheep), compared to the unaffected ( Ovis aries ) meckelin sequence (boxed). The partial meckelin sequence is aligned with ten orthologous sequences from other species. The boxes show the affected amino acids, and conservation of an isoleucine amino acid at these positions in several vertebrate species, including humans and zebrafish. The amino acids in the grey portion mark the beginning of a transmembrane domain in meckelin.
    Restriction Enzyme Apo I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 85/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/restriction enzyme apo i/product/New England Biolabs
    Average 85 stars, based on 3 article reviews
    Price from $9.99 to $1999.99
    restriction enzyme apo i - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

    85
    New England Biolabs restriction enzymes apo i
    Identification of two missense mutations in TMEM67 . ( a ) Sequence analysis of TMEM67 showing sequence variants in exon 20 (indicated by asterisks above the sequence tracks) in a carrier, and in an affected lamb, compared to an unaffected lamb. Below the unaffected sequence, the <t>Apo</t> I restriction site is indicated (black bar) ( b ) Apo I restriction fragment length polymorphism generated by the sequence variants caused different restriction digestion patterns for the affected and carrier lambs, compared to unaffected lambs; M, marker; U, unaffected pattern; C, carrier pattern; A, affected pattern. ( c ) Alignment of mutant with wild type partial sequences of meckelin from multiple species. The diagram shows the isoleucine to asparagine amino acid substitution at position 681 (I681N), and isoleucine to serine substitution at position 687 (I687S) in an affected lamb (MKS sheep), compared to the unaffected ( Ovis aries ) meckelin sequence (boxed). The partial meckelin sequence is aligned with ten orthologous sequences from other species. The boxes show the affected amino acids, and conservation of an isoleucine amino acid at these positions in several vertebrate species, including humans and zebrafish. The amino acids in the grey portion mark the beginning of a transmembrane domain in meckelin.
    Restriction Enzymes Apo I, supplied by New England Biolabs, 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/restriction enzymes apo i/product/New England Biolabs
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    restriction enzymes apo i - by Bioz Stars, 2020-09
    85/100 stars
      Buy from Supplier

    Image Search Results


    Identification of two missense mutations in TMEM67 . ( a ) Sequence analysis of TMEM67 showing sequence variants in exon 20 (indicated by asterisks above the sequence tracks) in a carrier, and in an affected lamb, compared to an unaffected lamb. Below the unaffected sequence, the Apo I restriction site is indicated (black bar) ( b ) Apo I restriction fragment length polymorphism generated by the sequence variants caused different restriction digestion patterns for the affected and carrier lambs, compared to unaffected lambs; M, marker; U, unaffected pattern; C, carrier pattern; A, affected pattern. ( c ) Alignment of mutant with wild type partial sequences of meckelin from multiple species. The diagram shows the isoleucine to asparagine amino acid substitution at position 681 (I681N), and isoleucine to serine substitution at position 687 (I687S) in an affected lamb (MKS sheep), compared to the unaffected ( Ovis aries ) meckelin sequence (boxed). The partial meckelin sequence is aligned with ten orthologous sequences from other species. The boxes show the affected amino acids, and conservation of an isoleucine amino acid at these positions in several vertebrate species, including humans and zebrafish. The amino acids in the grey portion mark the beginning of a transmembrane domain in meckelin.

    Journal: Scientific Reports

    Article Title: An ovine hepatorenal fibrocystic model of a Meckel-like syndrome associated with dysmorphic primary cilia and TMEM67 mutations

    doi: 10.1038/s41598-017-01519-4

    Figure Lengend Snippet: Identification of two missense mutations in TMEM67 . ( a ) Sequence analysis of TMEM67 showing sequence variants in exon 20 (indicated by asterisks above the sequence tracks) in a carrier, and in an affected lamb, compared to an unaffected lamb. Below the unaffected sequence, the Apo I restriction site is indicated (black bar) ( b ) Apo I restriction fragment length polymorphism generated by the sequence variants caused different restriction digestion patterns for the affected and carrier lambs, compared to unaffected lambs; M, marker; U, unaffected pattern; C, carrier pattern; A, affected pattern. ( c ) Alignment of mutant with wild type partial sequences of meckelin from multiple species. The diagram shows the isoleucine to asparagine amino acid substitution at position 681 (I681N), and isoleucine to serine substitution at position 687 (I687S) in an affected lamb (MKS sheep), compared to the unaffected ( Ovis aries ) meckelin sequence (boxed). The partial meckelin sequence is aligned with ten orthologous sequences from other species. The boxes show the affected amino acids, and conservation of an isoleucine amino acid at these positions in several vertebrate species, including humans and zebrafish. The amino acids in the grey portion mark the beginning of a transmembrane domain in meckelin.

    Article Snippet: Restriction enzyme digestion (PCR-restriction fragment length polymorphism (RFLP) genotyping) Genotyping was carried out following amplification of exon 20 of TMEM67 using PCR primers (refer to Supplementary Table ) for 30 cycles at 95 °C for 30 sec, 55 °C for 30 sec, 72 °C for 1 min, followed by digestion of the PCR product (612 bp) using the restriction enzyme Apo I (New England Biolabs Inc., Ipswich, MA, USA) at 50 °C.

    Techniques: Sequencing, Generated, Marker, Mutagenesis