ph d c7c phage display peptide library kit  (New England Biolabs)


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    Name:
    Ph D C7C Phage Display Peptide Library Kit
    Description:
    Ph D C7C Phage Display Peptide Library Kit 10 panning exps
    Catalog Number:
    e8120s
    Price:
    666
    Size:
    10 exps
    Category:
    Phage Display Systems
    Buy from Supplier


    Structured Review

    New England Biolabs ph d c7c phage display peptide library kit
    Ph D C7C Phage Display Peptide Library Kit
    Ph D C7C Phage Display Peptide Library Kit 10 panning exps
    https://www.bioz.com/result/ph d c7c phage display peptide library kit/product/New England Biolabs
    Average 95 stars, based on 58 article reviews
    Price from $9.99 to $1999.99
    ph d c7c phage display peptide library kit - by Bioz Stars, 2020-09
    95/100 stars

    Images

    1) Product Images from "Generation and characterization of cross neutralizing human monoclonal antibody against 4 serotypes of dengue virus without enhancing activity"

    Article Title: Generation and characterization of cross neutralizing human monoclonal antibody against 4 serotypes of dengue virus without enhancing activity

    Journal: PeerJ

    doi: 10.7717/peerj.4021

    Epitope mapping by phage display of random peptide libraries. (A) Affinity selection of phage-display. Ph.D.-12 and Ph.D.-C7C Phage Display Peptide Libraries were used in biopanning step. The constant units of phage (5 × 10 10 PFU) was used for three rounds of biopanning. Increasing percent yields of output phages represents the specific enrichment. (B) Alignment of phage-displayed peptide sequences selected by HuMAbs. Phage clones were shown to display a consensus sequences LXXXG (show in the box). (C) Comparison of the amino acid sequences of E proteins DENV1–4. In the box, DENV1–4 shared the same amino acids at positions 107 (L), 108 (F), 109 (G), 110 (K), and 111 (G). (D) Phage inhibition ELISA of eight phage clones which matched to the motif of 107LXXXG111. Phage lysate of selected clones bound with HuMAb in solution phase and the free phage clones were detected by ELISA. The absorbance values were measured at 450 nm using an ELISA reader (TECAN). Absorbance values of each concentration (A) were divided by absorbance values of no antibody (control) (A0), resulting in normalized values (A/A0). Anti-influenza antibody was used as negative control.
    Figure Legend Snippet: Epitope mapping by phage display of random peptide libraries. (A) Affinity selection of phage-display. Ph.D.-12 and Ph.D.-C7C Phage Display Peptide Libraries were used in biopanning step. The constant units of phage (5 × 10 10 PFU) was used for three rounds of biopanning. Increasing percent yields of output phages represents the specific enrichment. (B) Alignment of phage-displayed peptide sequences selected by HuMAbs. Phage clones were shown to display a consensus sequences LXXXG (show in the box). (C) Comparison of the amino acid sequences of E proteins DENV1–4. In the box, DENV1–4 shared the same amino acids at positions 107 (L), 108 (F), 109 (G), 110 (K), and 111 (G). (D) Phage inhibition ELISA of eight phage clones which matched to the motif of 107LXXXG111. Phage lysate of selected clones bound with HuMAb in solution phase and the free phage clones were detected by ELISA. The absorbance values were measured at 450 nm using an ELISA reader (TECAN). Absorbance values of each concentration (A) were divided by absorbance values of no antibody (control) (A0), resulting in normalized values (A/A0). Anti-influenza antibody was used as negative control.

    Techniques Used: Selection, Clone Assay, Inhibition, Enzyme-linked Immunosorbent Assay, Concentration Assay, Negative Control

    2) Product Images from "Identification of Novel Short BaTiO3-Binding/Nucleating Peptides for Phage-Templated in Situ Synthesis of BaTiO3 Polycrystalline Nanowires at Room Temperature"

    Article Title: Identification of Novel Short BaTiO3-Binding/Nucleating Peptides for Phage-Templated in Situ Synthesis of BaTiO3 Polycrystalline Nanowires at Room Temperature

    Journal: ACS applied materials & interfaces

    doi: 10.1021/acsami.6b09708

    Schematic of affinity-selection of BaTiO 3 -binding peptides utilizing the Ph.D.-C7C phage library. (a) BaTiO 3 nanocrystals are dispersed in the buffer. (b) The phage library is allowed to incubate with the BaTiO 3 nanocrystals. (c) BaTiO 3 -bound phages precipitate
    Figure Legend Snippet: Schematic of affinity-selection of BaTiO 3 -binding peptides utilizing the Ph.D.-C7C phage library. (a) BaTiO 3 nanocrystals are dispersed in the buffer. (b) The phage library is allowed to incubate with the BaTiO 3 nanocrystals. (c) BaTiO 3 -bound phages precipitate

    Techniques Used: Selection, Binding Assay

    3) 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

    4) Product Images from "Phage display of dynamic covalent binding motifs enables facile development of targeted antibiotics"

    Article Title: Phage display of dynamic covalent binding motifs enables facile development of targeted antibiotics

    Journal: Journal of the American Chemical Society

    doi: 10.1021/jacs.8b02461

    Modification of Ph.D.-C7C library with APBA warheads. (a) Illustration of a modified phage binding to bacterial cells via iminoboronate formation. (b) Illustration of the cysteine labeling strategy to display 2-APBA on phage. (c) Structure of the chemical modifiers of the C7C phage library. (d) Confirmation of APBA labeling of phage via fluorescent gel imaging after conjugation with Scz-FITC.
    Figure Legend Snippet: Modification of Ph.D.-C7C library with APBA warheads. (a) Illustration of a modified phage binding to bacterial cells via iminoboronate formation. (b) Illustration of the cysteine labeling strategy to display 2-APBA on phage. (c) Structure of the chemical modifiers of the C7C phage library. (d) Confirmation of APBA labeling of phage via fluorescent gel imaging after conjugation with Scz-FITC.

    Techniques Used: Modification, Binding Assay, Labeling, Imaging, Conjugation Assay

    Related Articles

    Clone Assay:

    Article Title: A specific affinity cyclic peptide enhances the adhesion, expansion and proliferation of rat bone mesenchymal stem cells on β-tricalcium phosphate scaffolds
    Article Snippet: .. The eluted phage clones that had bound to the BMSCs were then amplified in Escherichia coli ER2738 (provided in the Ph.D.™-C7C kit; cat. no. E8120S; New England BioLabs, Inc.). .. Subsequently, titration and purification of the bound phage clones were performed according to the manufacturer's protocol.

    Purification:

    Article Title: A systems medicine approach reveals disordered immune system and lipid metabolism in multiple sclerosis patients
    Article Snippet: .. According to the manufacturer's instruction, the Ph.D.TM ‐C7C phage display peptide library kit (New England Biolabs, Beverly, MA, USA) was used to perform three successive cycles of biopanning on purified IgG of the NDP and RP groups . .. Polyclonal phage ELISA was performed on the input and output phages of biopanning cycles in the NDP and RP groups.

    Amplification:

    Article Title: A specific affinity cyclic peptide enhances the adhesion, expansion and proliferation of rat bone mesenchymal stem cells on β-tricalcium phosphate scaffolds
    Article Snippet: .. The eluted phage clones that had bound to the BMSCs were then amplified in Escherichia coli ER2738 (provided in the Ph.D.™-C7C kit; cat. no. E8120S; New England BioLabs, Inc.). .. Subsequently, titration and purification of the bound phage clones were performed according to the manufacturer's protocol.

    Selection:

    Article Title: Identification of Novel Short BaTiO3-Binding/Nucleating Peptides for Phage-Templated in Situ Synthesis of BaTiO3 Polycrystalline Nanowires at Room Temperature
    Article Snippet: .. A Ph.D.-C7C phage display peptide library from New England Biolabs, Inc., was used for the phage display selection against BT crystals. ..

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  • 95
    New England Biolabs ph d c7c phage display peptide library kit
    Epitope mapping by phage display of random peptide libraries. (A) Affinity selection of phage-display. <t>Ph.D.-12</t> and <t>Ph.D.-C7C</t> Phage Display Peptide Libraries were used in biopanning step. The constant units of phage (5 × 10 10 PFU) was used for three rounds of biopanning. Increasing percent yields of output phages represents the specific enrichment. (B) Alignment of phage-displayed peptide sequences selected by HuMAbs. Phage clones were shown to display a consensus sequences LXXXG (show in the box). (C) Comparison of the amino acid sequences of E proteins DENV1–4. In the box, DENV1–4 shared the same amino acids at positions 107 (L), 108 (F), 109 (G), 110 (K), and 111 (G). (D) Phage inhibition ELISA of eight phage clones which matched to the motif of 107LXXXG111. Phage lysate of selected clones bound with HuMAb in solution phase and the free phage clones were detected by ELISA. The absorbance values were measured at 450 nm using an ELISA reader (TECAN). Absorbance values of each concentration (A) were divided by absorbance values of no antibody (control) (A0), resulting in normalized values (A/A0). Anti-influenza antibody was used as negative control.
    Ph D C7c Phage Display Peptide Library Kit, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ph d c7c phage display peptide library kit/product/New England Biolabs
    Average 95 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    ph d c7c phage display peptide library kit - by Bioz Stars, 2020-09
    95/100 stars
      Buy from Supplier

    Image Search Results


    Epitope mapping by phage display of random peptide libraries. (A) Affinity selection of phage-display. Ph.D.-12 and Ph.D.-C7C Phage Display Peptide Libraries were used in biopanning step. The constant units of phage (5 × 10 10 PFU) was used for three rounds of biopanning. Increasing percent yields of output phages represents the specific enrichment. (B) Alignment of phage-displayed peptide sequences selected by HuMAbs. Phage clones were shown to display a consensus sequences LXXXG (show in the box). (C) Comparison of the amino acid sequences of E proteins DENV1–4. In the box, DENV1–4 shared the same amino acids at positions 107 (L), 108 (F), 109 (G), 110 (K), and 111 (G). (D) Phage inhibition ELISA of eight phage clones which matched to the motif of 107LXXXG111. Phage lysate of selected clones bound with HuMAb in solution phase and the free phage clones were detected by ELISA. The absorbance values were measured at 450 nm using an ELISA reader (TECAN). Absorbance values of each concentration (A) were divided by absorbance values of no antibody (control) (A0), resulting in normalized values (A/A0). Anti-influenza antibody was used as negative control.

    Journal: PeerJ

    Article Title: Generation and characterization of cross neutralizing human monoclonal antibody against 4 serotypes of dengue virus without enhancing activity

    doi: 10.7717/peerj.4021

    Figure Lengend Snippet: Epitope mapping by phage display of random peptide libraries. (A) Affinity selection of phage-display. Ph.D.-12 and Ph.D.-C7C Phage Display Peptide Libraries were used in biopanning step. The constant units of phage (5 × 10 10 PFU) was used for three rounds of biopanning. Increasing percent yields of output phages represents the specific enrichment. (B) Alignment of phage-displayed peptide sequences selected by HuMAbs. Phage clones were shown to display a consensus sequences LXXXG (show in the box). (C) Comparison of the amino acid sequences of E proteins DENV1–4. In the box, DENV1–4 shared the same amino acids at positions 107 (L), 108 (F), 109 (G), 110 (K), and 111 (G). (D) Phage inhibition ELISA of eight phage clones which matched to the motif of 107LXXXG111. Phage lysate of selected clones bound with HuMAb in solution phase and the free phage clones were detected by ELISA. The absorbance values were measured at 450 nm using an ELISA reader (TECAN). Absorbance values of each concentration (A) were divided by absorbance values of no antibody (control) (A0), resulting in normalized values (A/A0). Anti-influenza antibody was used as negative control.

    Article Snippet: Panning was performed by using Ph.D.-12 and Ph.D.-C7C Phage Display Peptide Library Kit (New England Biolabs Inc., Hitchin, UK) according to the manufacturer’s instructions.

    Techniques: Selection, Clone Assay, Inhibition, Enzyme-linked Immunosorbent Assay, Concentration Assay, Negative Control

    Schematic of affinity-selection of BaTiO 3 -binding peptides utilizing the Ph.D.-C7C phage library. (a) BaTiO 3 nanocrystals are dispersed in the buffer. (b) The phage library is allowed to incubate with the BaTiO 3 nanocrystals. (c) BaTiO 3 -bound phages precipitate

    Journal: ACS applied materials & interfaces

    Article Title: Identification of Novel Short BaTiO3-Binding/Nucleating Peptides for Phage-Templated in Situ Synthesis of BaTiO3 Polycrystalline Nanowires at Room Temperature

    doi: 10.1021/acsami.6b09708

    Figure Lengend Snippet: Schematic of affinity-selection of BaTiO 3 -binding peptides utilizing the Ph.D.-C7C phage library. (a) BaTiO 3 nanocrystals are dispersed in the buffer. (b) The phage library is allowed to incubate with the BaTiO 3 nanocrystals. (c) BaTiO 3 -bound phages precipitate

    Article Snippet: A Ph.D.-C7C phage display peptide library from New England Biolabs, Inc., was used for the phage display selection against BT crystals.

    Techniques: Selection, Binding Assay

    (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.

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00069-15

    Figure Lengend 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.

    Article Snippet: A Ph.D.-12 phage library or Ph.D.-C7C phage library (1.5 × 1011 PFU each; New England BioLabs) was then added.

    Techniques: Sequencing

    Modification of Ph.D.-C7C library with APBA warheads. (a) Illustration of a modified phage binding to bacterial cells via iminoboronate formation. (b) Illustration of the cysteine labeling strategy to display 2-APBA on phage. (c) Structure of the chemical modifiers of the C7C phage library. (d) Confirmation of APBA labeling of phage via fluorescent gel imaging after conjugation with Scz-FITC.

    Journal: Journal of the American Chemical Society

    Article Title: Phage display of dynamic covalent binding motifs enables facile development of targeted antibiotics

    doi: 10.1021/jacs.8b02461

    Figure Lengend Snippet: Modification of Ph.D.-C7C library with APBA warheads. (a) Illustration of a modified phage binding to bacterial cells via iminoboronate formation. (b) Illustration of the cysteine labeling strategy to display 2-APBA on phage. (c) Structure of the chemical modifiers of the C7C phage library. (d) Confirmation of APBA labeling of phage via fluorescent gel imaging after conjugation with Scz-FITC.

    Article Snippet: The Ph.D.™-C7C Phage Display Peptide Library Kit and the E. coli K12 ER2738 strain were purchased from New England Biolabs.

    Techniques: Modification, Binding Assay, Labeling, Imaging, Conjugation Assay