Review



dna sequence coding for the c3 domain of adhesin p1  (GenScript corporation)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
    • 90
      Buy from Supplier

    Structured Review

    GenScript corporation dna sequence coding for the c3 domain of adhesin p1
    Dna Sequence Coding For The C3 Domain Of Adhesin P1, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p1+coding+sequence/pm37864759-47-9-26?v=GenScript+corporation
    Average 90 stars, based on 1 article reviews
    dna sequence coding for the c3 domain of adhesin p1 - by Bioz Stars, 2026-07
    90/100 stars

    Images



    Similar Products

    coding sequences for p1  (ATCC)
    97
    ATCC coding sequences for p1
    Recombinant protein design, construction, and purity validation. ( A ) Schematic diagram of recombinant protein constructs. Mutation sites are indicated by short black lines. ( B – H ) SDS-PAGE, Western blot, and Superdex™ 200 Increase 10/300 GL purification results for recombinant proteins. ( B ) <t>P1</t> (~165 kDa); ( C ) P40/90 complex (~117 kDa); ( D ) CARDS-WT (~69 kDa); ( E ) CARDS-E132A (~69 kDa); ( F ) CARDS-E132Q (~69 kDa); ( G ) CARDS-H36A (~69 kDa); ( H ) CARDS-R10A (~69 kDa). Left lane: protein marker; right lane: purified recombinant protein.
    Coding Sequences For P1, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p1+coding+sequence/pmc13119710-50-1-39?v=ATCC
    Average 97 stars, based on 1 article reviews
    coding sequences for p1 - by Bioz Stars, 2026-07
    97/100 stars
    		  Buy from Supplier
    dna sequence coding for the c3 domain of adhesin p1  (GenScript corporation)
    90
    GenScript corporation dna sequence coding for the c3 domain of adhesin p1
    (a) Annotated 2D 1H,15N TROSY spectrum of <t>Adhesin</t> <t>P1</t> C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.
    Dna Sequence Coding For The C3 Domain Of Adhesin P1, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p1+coding+sequence/pmc10695118-144-9-27?v=GenScript+corporation
    Average 90 stars, based on 1 article reviews
    dna sequence coding for the c3 domain of adhesin p1 - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier
    p1 coding sequences tatg  (ATCC)
    97
    ATCC p1 coding sequences tatg
    (a) Annotated 2D 1H,15N TROSY spectrum of <t>Adhesin</t> <t>P1</t> C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.
    P1 Coding Sequences Tatg, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p1+coding+sequence/deshpande_ria_anand__2023__building_tools_to_improve_the_scope_of_continuous_directed_evolution-509-56-61?v=ATCC
    Average 97 stars, based on 1 article reviews
    p1 coding sequences tatg - by Bioz Stars, 2026-07
    97/100 stars
    		  Buy from Supplier
    pgex-p1 plasmids (additional file 2) carrying the coding sequences for the polypeptides cb1414–472 and cb1414–442  (Millipore)
    90
    Millipore pgex-p1 plasmids (additional file 2) carrying the coding sequences for the polypeptides cb1414–472 and cb1414–442
    (a) Annotated 2D 1H,15N TROSY spectrum of <t>Adhesin</t> <t>P1</t> C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.
    Pgex P1 Plasmids (Additional File 2) Carrying The Coding Sequences For The Polypeptides Cb1414–472 And Cb1414–442, supplied by Millipore, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p1+coding+sequence/pm36109736-238-16-45?v=Millipore
    Average 90 stars, based on 1 article reviews
    pgex-p1 plasmids (additional file 2) carrying the coding sequences for the polypeptides cb1414–472 and cb1414–442 - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier
    p1 coding sequence  (Janssen)
    90
    Janssen p1 coding sequence
    (a) Annotated 2D 1H,15N TROSY spectrum of <t>Adhesin</t> <t>P1</t> C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.
    P1 Coding Sequence, supplied by Janssen, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p1+coding+sequence/pm21451259-146-13-16?v=Janssen
    Average 90 stars, based on 1 article reviews
    p1 coding sequence - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier
    p1 clone containing the coding region of the mouse cp49 gene and 5 -flanking sequence  (Incyte corporation)
    90
    Incyte corporation p1 clone containing the coding region of the mouse cp49 gene and 5 -flanking sequence
    (a) Annotated 2D 1H,15N TROSY spectrum of <t>Adhesin</t> <t>P1</t> C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.
    P1 Clone Containing The Coding Region Of The Mouse Cp49 Gene And 5 Flanking Sequence, supplied by Incyte corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/p1+coding+sequence/pm12506080-57-14-19?v=Incyte+corporation
    Average 90 stars, based on 1 article reviews
    p1 clone containing the coding region of the mouse cp49 gene and 5 -flanking sequence - by Bioz Stars, 2026-07
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    Recombinant protein design, construction, and purity validation. ( A ) Schematic diagram of recombinant protein constructs. Mutation sites are indicated by short black lines. ( B – H ) SDS-PAGE, Western blot, and Superdex™ 200 Increase 10/300 GL purification results for recombinant proteins. ( B ) P1 (~165 kDa); ( C ) P40/90 complex (~117 kDa); ( D ) CARDS-WT (~69 kDa); ( E ) CARDS-E132A (~69 kDa); ( F ) CARDS-E132Q (~69 kDa); ( G ) CARDS-H36A (~69 kDa); ( H ) CARDS-R10A (~69 kDa). Left lane: protein marker; right lane: purified recombinant protein.

    Journal: Vaccines

    Article Title: Three-Component Subunit Vaccine Induces Protective Immunity Against Mycoplasma pneumoniae in Mice

    doi: 10.3390/vaccines14040330

    Figure Lengend Snippet: Recombinant protein design, construction, and purity validation. ( A ) Schematic diagram of recombinant protein constructs. Mutation sites are indicated by short black lines. ( B – H ) SDS-PAGE, Western blot, and Superdex™ 200 Increase 10/300 GL purification results for recombinant proteins. ( B ) P1 (~165 kDa); ( C ) P40/90 complex (~117 kDa); ( D ) CARDS-WT (~69 kDa); ( E ) CARDS-E132A (~69 kDa); ( F ) CARDS-E132Q (~69 kDa); ( G ) CARDS-H36A (~69 kDa); ( H ) CARDS-R10A (~69 kDa). Left lane: protein marker; right lane: purified recombinant protein.

    Article Snippet: The coding sequences for P1 (GenBank I D: X06871 ), P40 (GenBank ID: AF125204 ), P90 (GenBank ID: AF125205 ), and CARDS-WT (GenBank ID: AY189944 ) were retrieved from the NCBI database based on the Mycoplasma pneumoniae standard strain ATCC M129.

    Techniques: Recombinant, Biomarker Discovery, Construct, Mutagenesis, SDS Page, Western Blot, Purification, Marker

    Toxicity screening of CARDS mutants and purity analysis of recombinant proteins. ( A ) Dose–response curves of TNF-α secretion from RAW264.7 cells treated with CARDS-WT and various mutants, used for screening attenuated mutants. ( B – H ) HPLC chromatograms of recombinant proteins on TSKgel G2000SWXL column. Purity values are indicated above the main peaks: ( B ) CARDS-E132A (78.88%), ( C ) CARDS-E132Q (73.47%), ( D ) CARDS-H36A (86.99%), ( E ) CARDS-R10A (82.72%), ( F ) P1 (87.65%), ( G ) P40/90 (96.76%), ( H ) CARDS-WT (91.77%).

    Journal: Vaccines

    Article Title: Three-Component Subunit Vaccine Induces Protective Immunity Against Mycoplasma pneumoniae in Mice

    doi: 10.3390/vaccines14040330

    Figure Lengend Snippet: Toxicity screening of CARDS mutants and purity analysis of recombinant proteins. ( A ) Dose–response curves of TNF-α secretion from RAW264.7 cells treated with CARDS-WT and various mutants, used for screening attenuated mutants. ( B – H ) HPLC chromatograms of recombinant proteins on TSKgel G2000SWXL column. Purity values are indicated above the main peaks: ( B ) CARDS-E132A (78.88%), ( C ) CARDS-E132Q (73.47%), ( D ) CARDS-H36A (86.99%), ( E ) CARDS-R10A (82.72%), ( F ) P1 (87.65%), ( G ) P40/90 (96.76%), ( H ) CARDS-WT (91.77%).

    Article Snippet: The coding sequences for P1 (GenBank I D: X06871 ), P40 (GenBank ID: AF125204 ), P90 (GenBank ID: AF125205 ), and CARDS-WT (GenBank ID: AY189944 ) were retrieved from the NCBI database based on the Mycoplasma pneumoniae standard strain ATCC M129.

    Techniques: Recombinant

    Formulation, immunization schedule, and antigen-specific IgG antibody responses of the three-component M. pneumoniae vaccine. ( A ) Formulation scheme showing the 6 experimental groups, their respective vaccine and adjuvant combinations. ( B ) Immunization schedule showing time points for immunizations (days 0, 14, 28) and serum collection (days 13, 27, 41). ( C – F ) Serum titers (log10) of specific IgG antibodies against P1, P40/90, CARDS-WT, and CARDS-Mut following single antigen immunizations (days 0, 14, 28) and serum collection (days 13, 27, 41). The saline group served as the negative control. ( G – J ) Serum antibody titers (days 41) against P1, P40/90, CARDS-WT, and CARDS-Mut in mice immunized according to the groups shown in ( A ). ( K ) Comparison of antibody titers (days 41) between the MPtriVa-D group (containing CARDS-WT with dual adjuvant) and the MPtriVb-D group (containing CARDS-Mut with dual adjuvant). ( L ) Comparison of antibody titers (days 41) between the MPtriVb-S (single adjuvant) and MPtriVb-D (dual adjuvant) groups. Data are presented as mean ± SD. p > 0.05 (not significant); *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

    Journal: Vaccines

    Article Title: Three-Component Subunit Vaccine Induces Protective Immunity Against Mycoplasma pneumoniae in Mice

    doi: 10.3390/vaccines14040330

    Figure Lengend Snippet: Formulation, immunization schedule, and antigen-specific IgG antibody responses of the three-component M. pneumoniae vaccine. ( A ) Formulation scheme showing the 6 experimental groups, their respective vaccine and adjuvant combinations. ( B ) Immunization schedule showing time points for immunizations (days 0, 14, 28) and serum collection (days 13, 27, 41). ( C – F ) Serum titers (log10) of specific IgG antibodies against P1, P40/90, CARDS-WT, and CARDS-Mut following single antigen immunizations (days 0, 14, 28) and serum collection (days 13, 27, 41). The saline group served as the negative control. ( G – J ) Serum antibody titers (days 41) against P1, P40/90, CARDS-WT, and CARDS-Mut in mice immunized according to the groups shown in ( A ). ( K ) Comparison of antibody titers (days 41) between the MPtriVa-D group (containing CARDS-WT with dual adjuvant) and the MPtriVb-D group (containing CARDS-Mut with dual adjuvant). ( L ) Comparison of antibody titers (days 41) between the MPtriVb-S (single adjuvant) and MPtriVb-D (dual adjuvant) groups. Data are presented as mean ± SD. p > 0.05 (not significant); *, p < 0.05; **, p < 0.01; ***, p < 0.001; ****, p < 0.0001.

    Article Snippet: The coding sequences for P1 (GenBank I D: X06871 ), P40 (GenBank ID: AF125204 ), P90 (GenBank ID: AF125205 ), and CARDS-WT (GenBank ID: AY189944 ) were retrieved from the NCBI database based on the Mycoplasma pneumoniae standard strain ATCC M129.

    Techniques: Formulation, Adjuvant, Saline, Negative Control, Comparison

    (a) Annotated 2D 1H,15N TROSY spectrum of Adhesin P1 C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.

    Journal: Biomolecular NMR assignments

    Article Title: Backbone NMR resonance assignments for the C terminal domain of the Streptococcus mutans adhesin P1

    doi: 10.1007/s12104-023-10158-y

    Figure Lengend Snippet: (a) Annotated 2D 1H,15N TROSY spectrum of Adhesin P1 C3 domain (BMRB 52097) collected in an 800 MHz spectrometer at 25 °C in phosphate buffer pH 6. Resonance assignments are shown with black labels; (b) Alphafold structural model for the new, longer C3 construct with the amino acid residues that are currently assigned shown in blue; (c) C3 domain structure (PDB 3QE5) with the residues assigned using the previous, shorter C3 construct (BMRB 27935) shown in red; (d) comparison of 2D 1H,15N TROSY spectra for the previous, shorter C3 construct (red) and the new, longer construct for the AlphaFold-predicted C3 domain (blue). Disordered, poorly resolved resonances observed for the prior C3 construct are now well resolved for the new C3 construct by addition of the seven C-terminal amino acids.

    Article Snippet: The DNA sequence coding for the C3 domain of adhesin P1 (residues 1328–1490; Uniprot accession number P23504) was synthesized, with codon optimization for E. coli , by Genescript and inserted into pET21a(+) plasmid to yield the pET21a-C3-His 6 plasmid with a C-terminal His tag.

    Techniques: Construct, Comparison