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p1 clone containing the coding region of the mouse cp49 gene and 5 -flanking sequence  (Incyte corporation)

 
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    Incyte corporation p1 clone containing the coding region of the mouse cp49 gene and 5 -flanking sequence
    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/p1+clone+containing+the+coding+region+of+the+mouse+cp49+gene+and+5++flanking+sequence/pm12506080-57-14-19
    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, 2026-10
    90/100 stars

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    Related Articles

    other:

    Article Title: Aspergillus flavus expressed sequence tags for identification of genes with putative roles in aflatoxin contamination of crops.
    Article Snippet: Aflatoxins, produced primarily by Aspergillus flavus and A. parasiticus, are among the most toxic and carcinogenic naturally occurring compounds.. In an attempt to identify genes potentially involved in aflatoxin contamination of crops, and to better understand the biology of A. flavus, a large scale sequencing of A. flavus expressed sequence tags (EST) was conducted.. The 5 0 ends of 26,110 cDNA clones from a normalized cDNA expression library were sequenced.

    Sequencing:

    Article Title: Isolation and characterization of the human CP49 gene promoter.
    Article Snippet: METHODS.. The DNA sequence upstream of the human CP49 coding region was subcloned as a set of 5 and 3 deletion series.. The constructs were transfected into lens (N/N1003A) and nonlens (NIH3T3) cell lines and chicken primary lens cultures, to test for promoter activity and specificity.



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    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