ph d 12 peptide library  (New England Biolabs)


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    Ph D 12 Phage Display Peptide Library
    Description:
    Ph D 12 Phage Display Peptide Library 50 panning exps
    Catalog Number:
    e8111l
    Price:
    2260
    Size:
    50 exps
    Category:
    Phage Display Systems
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    New England Biolabs ph d 12 peptide library
    Ph D 12 Phage Display Peptide Library
    Ph D 12 Phage Display Peptide Library 50 panning exps
    https://www.bioz.com/result/ph d 12 peptide library/product/New England Biolabs
    Average 96 stars, based on 40 article reviews
    Price from $9.99 to $1999.99
    ph d 12 peptide library - by Bioz Stars, 2020-05
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    Images

    1) Product Images from "Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization"

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-02891-x

    Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.
    Figure Legend Snippet: Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Clone Assay, Blocking Assay

    2) Product Images from "Targeting of Embryonic Stem Cells by Peptide-Conjugated Quantum Dots"

    Article Title: Targeting of Embryonic Stem Cells by Peptide-Conjugated Quantum Dots

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0012075

    Selection of Ph.D-12 phage pools against ES cells. (A) Subtraction efficiency with dES cells and PMEFs. The phage pool underwent three subtractions with dES cells and three subtractions with PMEFs in each round of biopanning. The efficiency is shown as the percentage of recovered phage numbers from subtraction to input phage numbers. (B) Selection efficiency with ES cells. The binding efficiency of phage pool is shown as the percentage of eluted phage numbers to input phage numbers in each round of biopanning. (C) Alignment of peptide sequences displayed by monoclonal M13 phages selected binding to ES cells. Identical sequences are shown in color. (D) Affinity and specificity of purified candidate M13 phages binding to indicated cell types using ELISA. The peptides displayed by selected phages are APWHLSSQYSRT, GYPHPWTLWHLN, LDVRPWYVTPLP, TPLINMNALTVT, and WAPEKDYMQLMK. The first three amino acid letters of these sequences are used to stand for the corresponding phages. Results are presented as absorption value (mean ± standard derivation) in ELISA assay. Each experiment was repeated three times independently. **: p
    Figure Legend Snippet: Selection of Ph.D-12 phage pools against ES cells. (A) Subtraction efficiency with dES cells and PMEFs. The phage pool underwent three subtractions with dES cells and three subtractions with PMEFs in each round of biopanning. The efficiency is shown as the percentage of recovered phage numbers from subtraction to input phage numbers. (B) Selection efficiency with ES cells. The binding efficiency of phage pool is shown as the percentage of eluted phage numbers to input phage numbers in each round of biopanning. (C) Alignment of peptide sequences displayed by monoclonal M13 phages selected binding to ES cells. Identical sequences are shown in color. (D) Affinity and specificity of purified candidate M13 phages binding to indicated cell types using ELISA. The peptides displayed by selected phages are APWHLSSQYSRT, GYPHPWTLWHLN, LDVRPWYVTPLP, TPLINMNALTVT, and WAPEKDYMQLMK. The first three amino acid letters of these sequences are used to stand for the corresponding phages. Results are presented as absorption value (mean ± standard derivation) in ELISA assay. Each experiment was repeated three times independently. **: p

    Techniques Used: Selection, Binding Assay, Purification, Enzyme-linked Immunosorbent Assay

    3) Product Images from "Targeting of Hepatoma Cell and Suppression of Tumor Growth by a Novel 12mer Peptide Fused to Superantigen TSST-1"

    Article Title: Targeting of Hepatoma Cell and Suppression of Tumor Growth by a Novel 12mer Peptide Fused to Superantigen TSST-1

    Journal:

    doi: 10.2119/2006-00011.Jiang

    Screening of HCC-specific peptides from 12-mer peptide libraries. (A) Output assay for each plaque selection round. The output ratio was calculated as output number/input number. (B) Binding assay of positive clones to the hepatoma cell lines (SMMC-7721
    Figure Legend Snippet: Screening of HCC-specific peptides from 12-mer peptide libraries. (A) Output assay for each plaque selection round. The output ratio was calculated as output number/input number. (B) Binding assay of positive clones to the hepatoma cell lines (SMMC-7721

    Techniques Used: Selection, Binding Assay, Clone Assay

    4) Product Images from "Prostaglandin D2 Receptor DP1 Antibodies Predict Vaccine-induced and Spontaneous Narcolepsy Type 1: Large-scale Study of Antibody Profiling"

    Article Title: Prostaglandin D2 Receptor DP1 Antibodies Predict Vaccine-induced and Spontaneous Narcolepsy Type 1: Large-scale Study of Antibody Profiling

    Journal: EBioMedicine

    doi: 10.1016/j.ebiom.2018.01.043

    Humoral immune response studied using the mimotope-variation analysis (MVA) method. A. Schematic drawing of the workflow in MVA. MVA is a high-throughput random peptide phage display analysis. A random peptide display library (PhD12) was used which contained 10^9 different 12-mer peptide sequences introduced to the N-terminus of the phage major coat protein pIII (NEB). For MVA, sample-specific IgG proteins (antibodies, Human IgG fraction ) present in human sera of interest are allowed to interact with the phage-displayed peptides and the IgG-phage complexes were captured to protein G magnetic beads, while the unbound phages were washed away ( Peptide library display ). Captured phages were lysed and DNA amplified with primer sequences containing a tag with a unique barcode sequence and the final amplicons were pooled for NGS analysis ( HTS sequencing ). The primer set homologous to the M13KE vector sequences that flank the random peptide coding sequence was used to amplify a 50-bp fragment. Data analysis to classify peptides that were specific to Pmdx-infected, -vaccinated and NT1-diseased individuals was carried out by comparing the profiles of peptides (mimotopes) from diseased to those from non-diseased ( Peptide profile analysis ). On average, MVA generated 1.8 million peptide sequences with unique structure (divergence) totaling 2.8 million peptide sequences in abundance (total abundance; number of reads) per sample. Altogether, a peptide data set with > 16 million sequences (Totpep) with unique structure was generated. B. Analysis of peptides revealed highly divergent patterns (immunoprofiles) across study cohorts. The fraction of top 2500 peptides with unique structure and highest values of abundance - reflecting the peaking immune reactivity of each sample - was analyzed for variance. Top2500 peptide dataset contained altogether 160,000 sequences out of which 121,142 were unique. Pie charts display the sequence distribution of unique peptides across all samples analyzed. The left pie ( blue ) displays the proportion of shared vs. unique peptides: ~86% were unique to one individual whereas ~14% of the peptide sequences were shared between samples, out of these ~8.5% were common to 2 samples, 5% to 3–10 samples and 0.5% were detected in > 10 samples. The right pie ( red ) displays the distribution of shared 16,844 peptide sequences out of which ~60.7% were common to 2 samples, 35.7% to 3–10 samples and 3.6% were seen in > 10 samples. The four pie charts (below) exemplify the peptide profile structures in different clinical cohorts. The size of each pie piece is proportional to the number of unique peptides common to one or more samples of a clinical cohort. Blue - represents unique peptides, red - the most shared. C. Individual variation in peptide divergence is characteristic to all immunoprofiles. Top 2500 peptides were analyzed to assess the range of individual peptide variation across study cohorts. Blue dots mark peptide divergence in a single sample. As indicated, between one to two thousand peptides were individual-specific, whilst the most common peptides (shared by > 10 individuals) ranged in divergence from tens to 350 across samples. Range of unique peptide variations was similar across all study samples. D. Heat map image of a random fragment of MVA profile encompassing 400 peptides across study samples. Peptide profiles were individual-specific with a highly varying abundance. Each column represents the peptide profile of a single individual, and each line represents a peptide with a unique primary structure. Abundance is presented as counts in logarithmic scale ( in log ); black colour depicts peptides captured at higher abundance, and white those at lower abundance. Shown are peptide profiles that were common to 3–10 individuals. Abbreviations: Abundance – peptide frequency; Divergence – all unique peptides; HC - healthy control; H1N1-HC – H1N1 infected; Pdmx-HC - Pandemrix-vaccinated; NT1 - narcolepsy type 1 (including 10 Pandemrix-induced NT1 samples).
    Figure Legend Snippet: Humoral immune response studied using the mimotope-variation analysis (MVA) method. A. Schematic drawing of the workflow in MVA. MVA is a high-throughput random peptide phage display analysis. A random peptide display library (PhD12) was used which contained 10^9 different 12-mer peptide sequences introduced to the N-terminus of the phage major coat protein pIII (NEB). For MVA, sample-specific IgG proteins (antibodies, Human IgG fraction ) present in human sera of interest are allowed to interact with the phage-displayed peptides and the IgG-phage complexes were captured to protein G magnetic beads, while the unbound phages were washed away ( Peptide library display ). Captured phages were lysed and DNA amplified with primer sequences containing a tag with a unique barcode sequence and the final amplicons were pooled for NGS analysis ( HTS sequencing ). The primer set homologous to the M13KE vector sequences that flank the random peptide coding sequence was used to amplify a 50-bp fragment. Data analysis to classify peptides that were specific to Pmdx-infected, -vaccinated and NT1-diseased individuals was carried out by comparing the profiles of peptides (mimotopes) from diseased to those from non-diseased ( Peptide profile analysis ). On average, MVA generated 1.8 million peptide sequences with unique structure (divergence) totaling 2.8 million peptide sequences in abundance (total abundance; number of reads) per sample. Altogether, a peptide data set with > 16 million sequences (Totpep) with unique structure was generated. B. Analysis of peptides revealed highly divergent patterns (immunoprofiles) across study cohorts. The fraction of top 2500 peptides with unique structure and highest values of abundance - reflecting the peaking immune reactivity of each sample - was analyzed for variance. Top2500 peptide dataset contained altogether 160,000 sequences out of which 121,142 were unique. Pie charts display the sequence distribution of unique peptides across all samples analyzed. The left pie ( blue ) displays the proportion of shared vs. unique peptides: ~86% were unique to one individual whereas ~14% of the peptide sequences were shared between samples, out of these ~8.5% were common to 2 samples, 5% to 3–10 samples and 0.5% were detected in > 10 samples. The right pie ( red ) displays the distribution of shared 16,844 peptide sequences out of which ~60.7% were common to 2 samples, 35.7% to 3–10 samples and 3.6% were seen in > 10 samples. The four pie charts (below) exemplify the peptide profile structures in different clinical cohorts. The size of each pie piece is proportional to the number of unique peptides common to one or more samples of a clinical cohort. Blue - represents unique peptides, red - the most shared. C. Individual variation in peptide divergence is characteristic to all immunoprofiles. Top 2500 peptides were analyzed to assess the range of individual peptide variation across study cohorts. Blue dots mark peptide divergence in a single sample. As indicated, between one to two thousand peptides were individual-specific, whilst the most common peptides (shared by > 10 individuals) ranged in divergence from tens to 350 across samples. Range of unique peptide variations was similar across all study samples. D. Heat map image of a random fragment of MVA profile encompassing 400 peptides across study samples. Peptide profiles were individual-specific with a highly varying abundance. Each column represents the peptide profile of a single individual, and each line represents a peptide with a unique primary structure. Abundance is presented as counts in logarithmic scale ( in log ); black colour depicts peptides captured at higher abundance, and white those at lower abundance. Shown are peptide profiles that were common to 3–10 individuals. Abbreviations: Abundance – peptide frequency; Divergence – all unique peptides; HC - healthy control; H1N1-HC – H1N1 infected; Pdmx-HC - Pandemrix-vaccinated; NT1 - narcolepsy type 1 (including 10 Pandemrix-induced NT1 samples).

    Techniques Used: High Throughput Screening Assay, Magnetic Beads, Amplification, Sequencing, Next-Generation Sequencing, Plasmid Preparation, Infection, Generated

    5) Product Images from "Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization"

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-02891-x

    Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.
    Figure Legend Snippet: Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Clone Assay, Blocking Assay

    6) Product Images from "Prostaglandin D2 Receptor DP1 Antibodies Predict Vaccine-induced and Spontaneous Narcolepsy Type 1: Large-scale Study of Antibody Profiling"

    Article Title: Prostaglandin D2 Receptor DP1 Antibodies Predict Vaccine-induced and Spontaneous Narcolepsy Type 1: Large-scale Study of Antibody Profiling

    Journal: EBioMedicine

    doi: 10.1016/j.ebiom.2018.01.043

    Humoral immune response studied using the mimotope-variation analysis (MVA) method. A. Schematic drawing of the workflow in MVA. MVA is a high-throughput random peptide phage display analysis. A random peptide display library (PhD12) was used which contained 10^9 different 12-mer peptide sequences introduced to the N-terminus of the phage major coat protein pIII (NEB). For MVA, sample-specific IgG proteins (antibodies, Human IgG fraction ) present in human sera of interest are allowed to interact with the phage-displayed peptides and the IgG-phage complexes were captured to protein G magnetic beads, while the unbound phages were washed away ( Peptide library display ). Captured phages were lysed and DNA amplified with primer sequences containing a tag with a unique barcode sequence and the final amplicons were pooled for NGS analysis ( HTS sequencing ). The primer set homologous to the M13KE vector sequences that flank the random peptide coding sequence was used to amplify a 50-bp fragment. Data analysis to classify peptides that were specific to Pmdx-infected, -vaccinated and NT1-diseased individuals was carried out by comparing the profiles of peptides (mimotopes) from diseased to those from non-diseased ( Peptide profile analysis ). On average, MVA generated 1.8 million peptide sequences with unique structure (divergence) totaling 2.8 million peptide sequences in abundance (total abundance; number of reads) per sample. Altogether, a peptide data set with > 16 million sequences (Totpep) with unique structure was generated. B. Analysis of peptides revealed highly divergent patterns (immunoprofiles) across study cohorts. The fraction of top 2500 peptides with unique structure and highest values of abundance - reflecting the peaking immune reactivity of each sample - was analyzed for variance. Top2500 peptide dataset contained altogether 160,000 sequences out of which 121,142 were unique. Pie charts display the sequence distribution of unique peptides across all samples analyzed. The left pie ( blue ) displays the proportion of shared vs. unique peptides: ~86% were unique to one individual whereas ~14% of the peptide sequences were shared between samples, out of these ~8.5% were common to 2 samples, 5% to 3–10 samples and 0.5% were detected in > 10 samples. The right pie ( red ) displays the distribution of shared 16,844 peptide sequences out of which ~60.7% were common to 2 samples, 35.7% to 3–10 samples and 3.6% were seen in > 10 samples. The four pie charts (below) exemplify the peptide profile structures in different clinical cohorts. The size of each pie piece is proportional to the number of unique peptides common to one or more samples of a clinical cohort. Blue - represents unique peptides, red - the most shared. C. Individual variation in peptide divergence is characteristic to all immunoprofiles. Top 2500 peptides were analyzed to assess the range of individual peptide variation across study cohorts. Blue dots mark peptide divergence in a single sample. As indicated, between one to two thousand peptides were individual-specific, whilst the most common peptides (shared by > 10 individuals) ranged in divergence from tens to 350 across samples. Range of unique peptide variations was similar across all study samples. D. Heat map image of a random fragment of MVA profile encompassing 400 peptides across study samples. Peptide profiles were individual-specific with a highly varying abundance. Each column represents the peptide profile of a single individual, and each line represents a peptide with a unique primary structure. Abundance is presented as counts in logarithmic scale ( in log ); black colour depicts peptides captured at higher abundance, and white those at lower abundance. Shown are peptide profiles that were common to 3–10 individuals. Abbreviations: Abundance – peptide frequency; Divergence – all unique peptides; HC - healthy control; H1N1-HC – H1N1 infected; Pdmx-HC - Pandemrix-vaccinated; NT1 - narcolepsy type 1 (including 10 Pandemrix-induced NT1 samples).
    Figure Legend Snippet: Humoral immune response studied using the mimotope-variation analysis (MVA) method. A. Schematic drawing of the workflow in MVA. MVA is a high-throughput random peptide phage display analysis. A random peptide display library (PhD12) was used which contained 10^9 different 12-mer peptide sequences introduced to the N-terminus of the phage major coat protein pIII (NEB). For MVA, sample-specific IgG proteins (antibodies, Human IgG fraction ) present in human sera of interest are allowed to interact with the phage-displayed peptides and the IgG-phage complexes were captured to protein G magnetic beads, while the unbound phages were washed away ( Peptide library display ). Captured phages were lysed and DNA amplified with primer sequences containing a tag with a unique barcode sequence and the final amplicons were pooled for NGS analysis ( HTS sequencing ). The primer set homologous to the M13KE vector sequences that flank the random peptide coding sequence was used to amplify a 50-bp fragment. Data analysis to classify peptides that were specific to Pmdx-infected, -vaccinated and NT1-diseased individuals was carried out by comparing the profiles of peptides (mimotopes) from diseased to those from non-diseased ( Peptide profile analysis ). On average, MVA generated 1.8 million peptide sequences with unique structure (divergence) totaling 2.8 million peptide sequences in abundance (total abundance; number of reads) per sample. Altogether, a peptide data set with > 16 million sequences (Totpep) with unique structure was generated. B. Analysis of peptides revealed highly divergent patterns (immunoprofiles) across study cohorts. The fraction of top 2500 peptides with unique structure and highest values of abundance - reflecting the peaking immune reactivity of each sample - was analyzed for variance. Top2500 peptide dataset contained altogether 160,000 sequences out of which 121,142 were unique. Pie charts display the sequence distribution of unique peptides across all samples analyzed. The left pie ( blue ) displays the proportion of shared vs. unique peptides: ~86% were unique to one individual whereas ~14% of the peptide sequences were shared between samples, out of these ~8.5% were common to 2 samples, 5% to 3–10 samples and 0.5% were detected in > 10 samples. The right pie ( red ) displays the distribution of shared 16,844 peptide sequences out of which ~60.7% were common to 2 samples, 35.7% to 3–10 samples and 3.6% were seen in > 10 samples. The four pie charts (below) exemplify the peptide profile structures in different clinical cohorts. The size of each pie piece is proportional to the number of unique peptides common to one or more samples of a clinical cohort. Blue - represents unique peptides, red - the most shared. C. Individual variation in peptide divergence is characteristic to all immunoprofiles. Top 2500 peptides were analyzed to assess the range of individual peptide variation across study cohorts. Blue dots mark peptide divergence in a single sample. As indicated, between one to two thousand peptides were individual-specific, whilst the most common peptides (shared by > 10 individuals) ranged in divergence from tens to 350 across samples. Range of unique peptide variations was similar across all study samples. D. Heat map image of a random fragment of MVA profile encompassing 400 peptides across study samples. Peptide profiles were individual-specific with a highly varying abundance. Each column represents the peptide profile of a single individual, and each line represents a peptide with a unique primary structure. Abundance is presented as counts in logarithmic scale ( in log ); black colour depicts peptides captured at higher abundance, and white those at lower abundance. Shown are peptide profiles that were common to 3–10 individuals. Abbreviations: Abundance – peptide frequency; Divergence – all unique peptides; HC - healthy control; H1N1-HC – H1N1 infected; Pdmx-HC - Pandemrix-vaccinated; NT1 - narcolepsy type 1 (including 10 Pandemrix-induced NT1 samples).

    Techniques Used: High Throughput Screening Assay, Magnetic Beads, Amplification, Sequencing, Next-Generation Sequencing, Plasmid Preparation, Infection, Generated

    7) Product Images from "Membrane Protein Complex ExbB4-ExbD1-TonB1 from Escherichia coli Demonstrates Conformational Plasticity"

    Article Title: Membrane Protein Complex ExbB4-ExbD1-TonB1 from Escherichia coli Demonstrates Conformational Plasticity

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.00069-15

    (A and B) Alignment of ExbD 43–141 and TonB 33–239 affinity-selected Ph.D.-C7C and Ph.D.-12 peptides to the ExbD sequence. (A) The top 10 scoring ExbD 43–141 affinity-selected peptides aligned to residues 46 to 73 of the periplasmic domain of ExbD. See also Table S1 in the supplemental material for peptide match scores and window sizes. (B) The top nine scoring TonB 33–239 affinity-selected peptides aligned to residues 46 to 62 of the periplasmic domain of ExbD. See also Table S2 in the supplemental material for peptide match scores and window sizes. (C and D) Alignment of ExbD 43–141 affinity-selected Ph.D.-C7C and Ph.D.-12 peptides to TonB sequence. (C) The top six scoring peptides aligned to residues 38 to 55 of the periplasmic domain of TonB. (D) The top nine scoring peptides aligned to residues 125 to 144 of the central region of periplasmic TonB. See also Table S3 in the supplemental material for peptide match scores and window sizes. Only top-scoring peptides are shown for clarity; see the corresponding tables in the supplemental material for all peptides.
    Figure Legend Snippet: (A and B) Alignment of ExbD 43–141 and TonB 33–239 affinity-selected Ph.D.-C7C and Ph.D.-12 peptides to the ExbD sequence. (A) The top 10 scoring ExbD 43–141 affinity-selected peptides aligned to residues 46 to 73 of the periplasmic domain of ExbD. See also Table S1 in the supplemental material for peptide match scores and window sizes. (B) The top nine scoring TonB 33–239 affinity-selected peptides aligned to residues 46 to 62 of the periplasmic domain of ExbD. See also Table S2 in the supplemental material for peptide match scores and window sizes. (C and D) Alignment of ExbD 43–141 affinity-selected Ph.D.-C7C and Ph.D.-12 peptides to TonB sequence. (C) The top six scoring peptides aligned to residues 38 to 55 of the periplasmic domain of TonB. (D) The top nine scoring peptides aligned to residues 125 to 144 of the central region of periplasmic TonB. See also Table S3 in the supplemental material for peptide match scores and window sizes. Only top-scoring peptides are shown for clarity; see the corresponding tables in the supplemental material for all peptides.

    Techniques Used: Sequencing

    8) Product Images from "Identification of a peptide for folate receptor alpha by phage display and its tumor targeting activity in ovary cancer xenograft"

    Article Title: Identification of a peptide for folate receptor alpha by phage display and its tumor targeting activity in ovary cancer xenograft

    Journal: Scientific Reports

    doi: 10.1038/s41598-018-26683-z

    Screening and identification of FRα binding peptides. A Ph.D.-12 phage library was used to screen FRα binding phages with four rounds of biopanning. ( A ) The enrichment of FRα binding phages were evaluated by phage recovery yields of each round selection. ( B ) Polyclonal phage ELISA using elutes after each round selection. ( C ) 94 phage clones were randomLy picked from the third round selection, and their binding affinities for FRα were analyzed individually by phage ELISA.
    Figure Legend Snippet: Screening and identification of FRα binding peptides. A Ph.D.-12 phage library was used to screen FRα binding phages with four rounds of biopanning. ( A ) The enrichment of FRα binding phages were evaluated by phage recovery yields of each round selection. ( B ) Polyclonal phage ELISA using elutes after each round selection. ( C ) 94 phage clones were randomLy picked from the third round selection, and their binding affinities for FRα were analyzed individually by phage ELISA.

    Techniques Used: Binding Assay, Selection, Enzyme-linked Immunosorbent Assay, Clone Assay

    9) Product Images from "Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization"

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-02891-x

    Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.
    Figure Legend Snippet: Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Clone Assay, Blocking Assay

    10) Product Images from "Screening and selection of peptides specific for esophageal cancer cells from a phage display peptide library"

    Article Title: Screening and selection of peptides specific for esophageal cancer cells from a phage display peptide library

    Journal: Journal of Cardiothoracic Surgery

    doi: 10.1186/1749-8090-9-76

    Enrichment of phage achieved with each round of selection from a Ph. D.-12TM phage display peptide library using Eca109 cells. (A-C) Dilution of phage at 1:100 were plated for rounds 1 and 2, then a dilution of 1:1000 was plated for round 3.
    Figure Legend Snippet: Enrichment of phage achieved with each round of selection from a Ph. D.-12TM phage display peptide library using Eca109 cells. (A-C) Dilution of phage at 1:100 were plated for rounds 1 and 2, then a dilution of 1:1000 was plated for round 3.

    Techniques Used: Selection

    11) Product Images from "Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization"

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-02891-x

    Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.
    Figure Legend Snippet: Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Clone Assay, Blocking Assay

    12) Product Images from "Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization"

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization

    Journal: Scientific Reports

    doi: 10.1038/s41598-017-02891-x

    Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.
    Figure Legend Snippet: Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Clone Assay, Blocking Assay

    13) Product Images from "Generation of a novel therapeutic peptide that depletes MDSC in tumor-bearing mice"

    Article Title: Generation of a novel therapeutic peptide that depletes MDSC in tumor-bearing mice

    Journal: Nature medicine

    doi: 10.1038/nm.3560

    Identification and characterization of MDSC-binding peptides ( a ) Identification of Gr-1 + CD11b + MDSC in spleens of C57BL/6 mice ( n = 5) challenged subcutaneously with EL4 mouse lymphoma cells for 3 weeks. Double positive cells contain 2 distinct populations including Gr-1 high CD11b + granulocytic (P7) and Gr-1 int CD11b + monocytic (P10) MDSC subsets. ( b–c ) Biopanning with Ph.D.-12 peptide phage display library on Gr-1 and CD11b labeled splenocytes showed enriched phage eluted from sorted MDSC subsets. Biopanning enrichment was expressed in either “Number of plaques / 10 6 cells” or phage “Output / Input ratio” (× 10 –8 ). ( d ) Binding of synthetic FITC-conjugated G3 and H6 peptides on Gr-1 + CD11b + gated MDSC from EL4-bearing C57BL/6 mice ( n = 4), compared with Gr-1 − CD11b − gated non-MDSC splenocytes. A non-specific peptide (irrel peptide) was used as a negative control to exclude non-specific binding. The data are representative of 3 identical experiments.
    Figure Legend Snippet: Identification and characterization of MDSC-binding peptides ( a ) Identification of Gr-1 + CD11b + MDSC in spleens of C57BL/6 mice ( n = 5) challenged subcutaneously with EL4 mouse lymphoma cells for 3 weeks. Double positive cells contain 2 distinct populations including Gr-1 high CD11b + granulocytic (P7) and Gr-1 int CD11b + monocytic (P10) MDSC subsets. ( b–c ) Biopanning with Ph.D.-12 peptide phage display library on Gr-1 and CD11b labeled splenocytes showed enriched phage eluted from sorted MDSC subsets. Biopanning enrichment was expressed in either “Number of plaques / 10 6 cells” or phage “Output / Input ratio” (× 10 –8 ). ( d ) Binding of synthetic FITC-conjugated G3 and H6 peptides on Gr-1 + CD11b + gated MDSC from EL4-bearing C57BL/6 mice ( n = 4), compared with Gr-1 − CD11b − gated non-MDSC splenocytes. A non-specific peptide (irrel peptide) was used as a negative control to exclude non-specific binding. The data are representative of 3 identical experiments.

    Techniques Used: Binding Assay, Mouse Assay, Labeling, Negative Control

    14) Product Images from "Peptidic inhibitors of insulin-degrading enzyme with potential for dermatological applications discovered via phage display"

    Article Title: Peptidic inhibitors of insulin-degrading enzyme with potential for dermatological applications discovered via phage display

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0193101

    Peptides derived by phage display. A , Peptide sequences deduced from DNA sequencing of 20 clones from the Ph.D.™-C7C library. B , Consensus sequence derived from analysis of all data. C , Parent peptides selected for synthesis and testing. C , D , Peptide sequences deduced from DNA sequencing of 39 clones from the Ph.D.™-12 library, conducted as two independent runs ( D and E ). Note that Seq-12A-07 did not yield a decipherable sequence. F , Parent peptides selected for subsequent synthesis and testing based on prevalence.
    Figure Legend Snippet: Peptides derived by phage display. A , Peptide sequences deduced from DNA sequencing of 20 clones from the Ph.D.™-C7C library. B , Consensus sequence derived from analysis of all data. C , Parent peptides selected for synthesis and testing. C , D , Peptide sequences deduced from DNA sequencing of 39 clones from the Ph.D.™-12 library, conducted as two independent runs ( D and E ). Note that Seq-12A-07 did not yield a decipherable sequence. F , Parent peptides selected for subsequent synthesis and testing based on prevalence.

    Techniques Used: Derivative Assay, DNA Sequencing, Clone Assay, Sequencing

    Related Articles

    Incubation:

    Article Title: Identification of a peptide for folate receptor alpha by phage display and its tumor targeting activity in ovary cancer xenograft
    Article Snippet: .. After washing 3 times with TBS containing 0.05% (v/v) Tween 20 (TBST), 100 μL Ph.D.-12 peptide library aliquot (New England Biolabs, Inc., USA) containing 1011 phages was added to each well and the plate was incubated for 1 hour at 37 °C. ..

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization
    Article Snippet: .. 1010 pfu of PB-TUP, Ph.D.-12 peptide library, M13KE, and D12 clone were added to the microtiter plates and incubated overnight at 4 °C. .. Next day, the plates were washed 3 times with TBST and 3 times with TBS and the relative number of bound phage was determined by phage ELISA.

    Amplification:

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization
    Article Snippet: .. 106 PB-TUP, Ph.D.-12 peptide library, M13KE, and D12 clone were added separately into the logarithmic growth phase culture for infection and amplification. .. Concentration dependent binding to polystyrene Different concentrations of PB-TUP, Ph.D.-12 library, M13KE, and D12 clone were individually added into the blocked microtiter wells.

    Infection:

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization
    Article Snippet: .. 106 PB-TUP, Ph.D.-12 peptide library, M13KE, and D12 clone were added separately into the logarithmic growth phase culture for infection and amplification. .. Concentration dependent binding to polystyrene Different concentrations of PB-TUP, Ph.D.-12 library, M13KE, and D12 clone were individually added into the blocked microtiter wells.

    Selection:

    Article Title: Targeting of Embryonic Stem Cells by Peptide-Conjugated Quantum Dots
    Article Snippet: .. Phage peptide library selection The Ph.D-12 peptide phage display library was obtained from New England Biolabs (Beijing, China). ..

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    New England Biolabs ph d 12 peptide library
    Polystyrene binding of PB-TUP, <t>Ph.D.-12</t> peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.
    Ph D 12 Peptide Library, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.

    Journal: Scientific Reports

    Article Title: Discovery of a polystyrene binding peptide isolated from phage display library and its application in peptide immobilization

    doi: 10.1038/s41598-017-02891-x

    Figure Lengend Snippet: Polystyrene binding of PB-TUP, Ph.D.-12 peptide library, M13KE, and a non-relevant phage clone (D12) determined by ELISA. Four phage clones were added to the microtiter plates and the wells were treated with six different blocking buffers (first line) and six different washing buffers (second line), separately. ELISA values were used to evaluate the binding ability of these four phage clones to polystyrene. NFM had the best blocking effect. PBST and TBST were more effective washing buffers than the others. PB-TUP phage clone always had much higher absorbance comparing with the other phage clones. The experiments were performed in triplicates and repeated twice.

    Article Snippet: 1010 pfu of PB-TUP, Ph.D.-12 peptide library, M13KE, and D12 clone were added to the microtiter plates and incubated overnight at 4 °C.

    Techniques: Binding Assay, Enzyme-linked Immunosorbent Assay, Clone Assay, Blocking Assay

    Selection of Ph.D-12 phage pools against ES cells. (A) Subtraction efficiency with dES cells and PMEFs. The phage pool underwent three subtractions with dES cells and three subtractions with PMEFs in each round of biopanning. The efficiency is shown as the percentage of recovered phage numbers from subtraction to input phage numbers. (B) Selection efficiency with ES cells. The binding efficiency of phage pool is shown as the percentage of eluted phage numbers to input phage numbers in each round of biopanning. (C) Alignment of peptide sequences displayed by monoclonal M13 phages selected binding to ES cells. Identical sequences are shown in color. (D) Affinity and specificity of purified candidate M13 phages binding to indicated cell types using ELISA. The peptides displayed by selected phages are APWHLSSQYSRT, GYPHPWTLWHLN, LDVRPWYVTPLP, TPLINMNALTVT, and WAPEKDYMQLMK. The first three amino acid letters of these sequences are used to stand for the corresponding phages. Results are presented as absorption value (mean ± standard derivation) in ELISA assay. Each experiment was repeated three times independently. **: p

    Journal: PLoS ONE

    Article Title: Targeting of Embryonic Stem Cells by Peptide-Conjugated Quantum Dots

    doi: 10.1371/journal.pone.0012075

    Figure Lengend Snippet: Selection of Ph.D-12 phage pools against ES cells. (A) Subtraction efficiency with dES cells and PMEFs. The phage pool underwent three subtractions with dES cells and three subtractions with PMEFs in each round of biopanning. The efficiency is shown as the percentage of recovered phage numbers from subtraction to input phage numbers. (B) Selection efficiency with ES cells. The binding efficiency of phage pool is shown as the percentage of eluted phage numbers to input phage numbers in each round of biopanning. (C) Alignment of peptide sequences displayed by monoclonal M13 phages selected binding to ES cells. Identical sequences are shown in color. (D) Affinity and specificity of purified candidate M13 phages binding to indicated cell types using ELISA. The peptides displayed by selected phages are APWHLSSQYSRT, GYPHPWTLWHLN, LDVRPWYVTPLP, TPLINMNALTVT, and WAPEKDYMQLMK. The first three amino acid letters of these sequences are used to stand for the corresponding phages. Results are presented as absorption value (mean ± standard derivation) in ELISA assay. Each experiment was repeated three times independently. **: p

    Article Snippet: Phage peptide library selection The Ph.D-12 peptide phage display library was obtained from New England Biolabs (Beijing, China).

    Techniques: Selection, Binding Assay, Purification, Enzyme-linked Immunosorbent Assay

    Screening of HCC-specific peptides from 12-mer peptide libraries. (A) Output assay for each plaque selection round. The output ratio was calculated as output number/input number. (B) Binding assay of positive clones to the hepatoma cell lines (SMMC-7721

    Journal:

    Article Title: Targeting of Hepatoma Cell and Suppression of Tumor Growth by a Novel 12mer Peptide Fused to Superantigen TSST-1

    doi: 10.2119/2006-00011.Jiang

    Figure Lengend Snippet: Screening of HCC-specific peptides from 12-mer peptide libraries. (A) Output assay for each plaque selection round. The output ratio was calculated as output number/input number. (B) Binding assay of positive clones to the hepatoma cell lines (SMMC-7721

    Article Snippet: The 12-mer phage-displayed library was purchased from New England BioLabs (Beverly, MA, USA).

    Techniques: Selection, Binding Assay, Clone Assay

    Humoral immune response studied using the mimotope-variation analysis (MVA) method. A. Schematic drawing of the workflow in MVA. MVA is a high-throughput random peptide phage display analysis. A random peptide display library (PhD12) was used which contained 10^9 different 12-mer peptide sequences introduced to the N-terminus of the phage major coat protein pIII (NEB). For MVA, sample-specific IgG proteins (antibodies, Human IgG fraction ) present in human sera of interest are allowed to interact with the phage-displayed peptides and the IgG-phage complexes were captured to protein G magnetic beads, while the unbound phages were washed away ( Peptide library display ). Captured phages were lysed and DNA amplified with primer sequences containing a tag with a unique barcode sequence and the final amplicons were pooled for NGS analysis ( HTS sequencing ). The primer set homologous to the M13KE vector sequences that flank the random peptide coding sequence was used to amplify a 50-bp fragment. Data analysis to classify peptides that were specific to Pmdx-infected, -vaccinated and NT1-diseased individuals was carried out by comparing the profiles of peptides (mimotopes) from diseased to those from non-diseased ( Peptide profile analysis ). On average, MVA generated 1.8 million peptide sequences with unique structure (divergence) totaling 2.8 million peptide sequences in abundance (total abundance; number of reads) per sample. Altogether, a peptide data set with > 16 million sequences (Totpep) with unique structure was generated. B. Analysis of peptides revealed highly divergent patterns (immunoprofiles) across study cohorts. The fraction of top 2500 peptides with unique structure and highest values of abundance - reflecting the peaking immune reactivity of each sample - was analyzed for variance. Top2500 peptide dataset contained altogether 160,000 sequences out of which 121,142 were unique. Pie charts display the sequence distribution of unique peptides across all samples analyzed. The left pie ( blue ) displays the proportion of shared vs. unique peptides: ~86% were unique to one individual whereas ~14% of the peptide sequences were shared between samples, out of these ~8.5% were common to 2 samples, 5% to 3–10 samples and 0.5% were detected in > 10 samples. The right pie ( red ) displays the distribution of shared 16,844 peptide sequences out of which ~60.7% were common to 2 samples, 35.7% to 3–10 samples and 3.6% were seen in > 10 samples. The four pie charts (below) exemplify the peptide profile structures in different clinical cohorts. The size of each pie piece is proportional to the number of unique peptides common to one or more samples of a clinical cohort. Blue - represents unique peptides, red - the most shared. C. Individual variation in peptide divergence is characteristic to all immunoprofiles. Top 2500 peptides were analyzed to assess the range of individual peptide variation across study cohorts. Blue dots mark peptide divergence in a single sample. As indicated, between one to two thousand peptides were individual-specific, whilst the most common peptides (shared by > 10 individuals) ranged in divergence from tens to 350 across samples. Range of unique peptide variations was similar across all study samples. D. Heat map image of a random fragment of MVA profile encompassing 400 peptides across study samples. Peptide profiles were individual-specific with a highly varying abundance. Each column represents the peptide profile of a single individual, and each line represents a peptide with a unique primary structure. Abundance is presented as counts in logarithmic scale ( in log ); black colour depicts peptides captured at higher abundance, and white those at lower abundance. Shown are peptide profiles that were common to 3–10 individuals. Abbreviations: Abundance – peptide frequency; Divergence – all unique peptides; HC - healthy control; H1N1-HC – H1N1 infected; Pdmx-HC - Pandemrix-vaccinated; NT1 - narcolepsy type 1 (including 10 Pandemrix-induced NT1 samples).

    Journal: EBioMedicine

    Article Title: Prostaglandin D2 Receptor DP1 Antibodies Predict Vaccine-induced and Spontaneous Narcolepsy Type 1: Large-scale Study of Antibody Profiling

    doi: 10.1016/j.ebiom.2018.01.043

    Figure Lengend Snippet: Humoral immune response studied using the mimotope-variation analysis (MVA) method. A. Schematic drawing of the workflow in MVA. MVA is a high-throughput random peptide phage display analysis. A random peptide display library (PhD12) was used which contained 10^9 different 12-mer peptide sequences introduced to the N-terminus of the phage major coat protein pIII (NEB). For MVA, sample-specific IgG proteins (antibodies, Human IgG fraction ) present in human sera of interest are allowed to interact with the phage-displayed peptides and the IgG-phage complexes were captured to protein G magnetic beads, while the unbound phages were washed away ( Peptide library display ). Captured phages were lysed and DNA amplified with primer sequences containing a tag with a unique barcode sequence and the final amplicons were pooled for NGS analysis ( HTS sequencing ). The primer set homologous to the M13KE vector sequences that flank the random peptide coding sequence was used to amplify a 50-bp fragment. Data analysis to classify peptides that were specific to Pmdx-infected, -vaccinated and NT1-diseased individuals was carried out by comparing the profiles of peptides (mimotopes) from diseased to those from non-diseased ( Peptide profile analysis ). On average, MVA generated 1.8 million peptide sequences with unique structure (divergence) totaling 2.8 million peptide sequences in abundance (total abundance; number of reads) per sample. Altogether, a peptide data set with > 16 million sequences (Totpep) with unique structure was generated. B. Analysis of peptides revealed highly divergent patterns (immunoprofiles) across study cohorts. The fraction of top 2500 peptides with unique structure and highest values of abundance - reflecting the peaking immune reactivity of each sample - was analyzed for variance. Top2500 peptide dataset contained altogether 160,000 sequences out of which 121,142 were unique. Pie charts display the sequence distribution of unique peptides across all samples analyzed. The left pie ( blue ) displays the proportion of shared vs. unique peptides: ~86% were unique to one individual whereas ~14% of the peptide sequences were shared between samples, out of these ~8.5% were common to 2 samples, 5% to 3–10 samples and 0.5% were detected in > 10 samples. The right pie ( red ) displays the distribution of shared 16,844 peptide sequences out of which ~60.7% were common to 2 samples, 35.7% to 3–10 samples and 3.6% were seen in > 10 samples. The four pie charts (below) exemplify the peptide profile structures in different clinical cohorts. The size of each pie piece is proportional to the number of unique peptides common to one or more samples of a clinical cohort. Blue - represents unique peptides, red - the most shared. C. Individual variation in peptide divergence is characteristic to all immunoprofiles. Top 2500 peptides were analyzed to assess the range of individual peptide variation across study cohorts. Blue dots mark peptide divergence in a single sample. As indicated, between one to two thousand peptides were individual-specific, whilst the most common peptides (shared by > 10 individuals) ranged in divergence from tens to 350 across samples. Range of unique peptide variations was similar across all study samples. D. Heat map image of a random fragment of MVA profile encompassing 400 peptides across study samples. Peptide profiles were individual-specific with a highly varying abundance. Each column represents the peptide profile of a single individual, and each line represents a peptide with a unique primary structure. Abundance is presented as counts in logarithmic scale ( in log ); black colour depicts peptides captured at higher abundance, and white those at lower abundance. Shown are peptide profiles that were common to 3–10 individuals. Abbreviations: Abundance – peptide frequency; Divergence – all unique peptides; HC - healthy control; H1N1-HC – H1N1 infected; Pdmx-HC - Pandemrix-vaccinated; NT1 - narcolepsy type 1 (including 10 Pandemrix-induced NT1 samples).

    Article Snippet: In brief, a random 12-mer peptide phage library (Ph.D.-12, NEB, UK) was used according to the manufacturer's protocol.

    Techniques: High Throughput Screening Assay, Magnetic Beads, Amplification, Sequencing, Next-Generation Sequencing, Plasmid Preparation, Infection, Generated