f nucleatum atcc 49256  (ATCC)


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    Name:
    Fusobacterium nucleatum subsp vincentii EM48
    Description:

    Catalog Number:
    49256
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    Structured Review

    ATCC f nucleatum atcc 49256
    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. <t>nucleatum</t> ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    https://www.bioz.com/result/f nucleatum atcc 49256/product/ATCC
    Average 94 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    f nucleatum atcc 49256 - by Bioz Stars, 2020-09
    94/100 stars

    Images

    1) Product Images from "Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria"

    Article Title: Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.187.15.5330-5340.2005

    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    Figure Legend Snippet: Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Techniques Used: Sequencing

    2) Product Images from "Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria"

    Article Title: Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.187.15.5330-5340.2005

    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    Figure Legend Snippet: Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Techniques Used: Sequencing

    3) Product Images from "Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease"

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0111329

    Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).
    Figure Legend Snippet: Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).

    Techniques Used: Mass Spectrometry

    Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.
    Figure Legend Snippet: Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.

    Techniques Used: Molecular Weight

    4) Product Images from "Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease"

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0111329

    Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).
    Figure Legend Snippet: Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).

    Techniques Used: Mass Spectrometry

    Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.
    Figure Legend Snippet: Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.

    Techniques Used: Molecular Weight

    5) Product Images from "Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease"

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0111329

    Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).
    Figure Legend Snippet: Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).

    Techniques Used: Mass Spectrometry

    Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.
    Figure Legend Snippet: Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.

    Techniques Used: Molecular Weight

    6) Product Images from "Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria"

    Article Title: Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.187.15.5330-5340.2005

    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    Figure Legend Snippet: Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Techniques Used: Sequencing

    7) Product Images from "Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria"

    Article Title: Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.187.15.5330-5340.2005

    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    Figure Legend Snippet: Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Techniques Used: Sequencing

    Related Articles

    Sequencing:

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease
    Article Snippet: .. However, while the peptide sequences generated from the 99 kDa proteolytic protein extracted from F. nucleatum ATCC 25586 corresponded to the entire FN1426 protein sequence , those generated from the 55 kDa proteolytic band of F. nucleatum ATCC 49256 matched only the N-terminal domain of FNV0835 ( ) suggesting that the 55 kDa protease of F. nucleatum ATCC 49256 also originated from a larger precursor. .. The 62 kDa protease of the non-sequenced strain FDC 364 was found to be most homologous to the N-terminal domain of FN1426 of F. nucleatum ATCC 25586 (data not shown).

    Isolation:

    Article Title: Abnormal Pregnancy Outcomes in Mice Using an Induced Periodontitis Model and the Haematogenous Migration of Fusobacterium nucleatum Sub-Species to the Murine Placenta
    Article Snippet: .. F . nucleatum type strains Subspecies, nucleatum (ATCC 25586 isolated from a cervico-facial lesion), vincentii (ATCC 49256 isolated from human periodontal pocket), polymorphum (ATCC 10953 isolated from human inflamed gingiva) and fusiforme (ATCC 11326 isolated from sinusitis in upper jaw) were purchased from the ATCC (Cryosite, NSW, Australia) and were maintained on anaerobic blood agar (Oxoid, Vic. ..

    Generated:

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease
    Article Snippet: .. However, while the peptide sequences generated from the 99 kDa proteolytic protein extracted from F. nucleatum ATCC 25586 corresponded to the entire FN1426 protein sequence , those generated from the 55 kDa proteolytic band of F. nucleatum ATCC 49256 matched only the N-terminal domain of FNV0835 ( ) suggesting that the 55 kDa protease of F. nucleatum ATCC 49256 also originated from a larger precursor. .. The 62 kDa protease of the non-sequenced strain FDC 364 was found to be most homologous to the N-terminal domain of FN1426 of F. nucleatum ATCC 25586 (data not shown).

    Purification:

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease
    Article Snippet: .. Tryptic peptides of both the 55 kDa and 101 kDa serine endopeptidases partially purified from F. nucleatum ATCC 49256 were found to match those of the putative 108 kDa serine protease designated FNV0835 (GI:34763535). .. However, while the peptide sequences generated from the 99 kDa proteolytic protein extracted from F. nucleatum ATCC 25586 corresponded to the entire FN1426 protein sequence , those generated from the 55 kDa proteolytic band of F. nucleatum ATCC 49256 matched only the N-terminal domain of FNV0835 ( ) suggesting that the 55 kDa protease of F. nucleatum ATCC 49256 also originated from a larger precursor.

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    ATCC f nucleatum atcc 49256
    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. <t>nucleatum</t> ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are
    F Nucleatum Atcc 49256, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/f nucleatum atcc 49256/product/ATCC
    Average 94 stars, based on 6 article reviews
    Price from $9.99 to $1999.99
    f nucleatum atcc 49256 - by Bioz Stars, 2020-09
    94/100 stars
      Buy from Supplier

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    Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Journal: Journal of Bacteriology

    Article Title: Identification and Characterization of a Novel Adhesin Unique to Oral Fusobacteria

    doi: 10.1128/JB.187.15.5330-5340.2005

    Figure Lengend Snippet: Amino acid sequence alignment of FadA and its paralogues. Highlighted in gray are the identical residues shared among FadA proteins. The sequences of two FadA paralogues, FN1529 from F. nucleatum ATCC 25586 and FNV2159 from F. nucleatum ATCC 49256, are

    Article Snippet: The accession numbers for the FadA sequences from other fusobacterial strains and species are as follows: for F. nucleatum ATCC 10953 , for F. nucleatum ATCC 23726 , for F. nucleatum ATCC 25586 , for F. nucleatum ATCC 49256 , for F. nucleatum ATCC 51190 , for F. nucleatum DUMC1356 , for F. nucleatum DUMC2079 , for F. nucleatum DUMC2929 , for F. nucleatum DUMC3156 , for F. nucleatum DUMC3349 , for F. nucleatum PK1594 , for F. periodonticum ATCC 33693 , and for F. simiae ATCC 33568 .

    Techniques: Sequencing

    Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).

    Journal: PLoS ONE

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease

    doi: 10.1371/journal.pone.0111329

    Figure Lengend Snippet: Identification of the fusobacterial serine protease. Amino acid sequences of the putative serine protease open reading frames FN1426 (Fsp25586) (A), and FNV0835 (Fsp49256) (B). Red highlight indicates sequences identified by mass spectrometry of the 99 kDa serine protease of F. nucleatum ATCC 25586 (A), and of the 55 kDa serine protease of F. nucleatum ATCC 49256 (B).

    Article Snippet: However, while the peptide sequences generated from the 99 kDa proteolytic protein extracted from F. nucleatum ATCC 25586 corresponded to the entire FN1426 protein sequence , those generated from the 55 kDa proteolytic band of F. nucleatum ATCC 49256 matched only the N-terminal domain of FNV0835 ( ) suggesting that the 55 kDa protease of F. nucleatum ATCC 49256 also originated from a larger precursor.

    Techniques: Mass Spectrometry

    Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.

    Journal: PLoS ONE

    Article Title: Identification and Characterization of Fusolisin, the Fusobacterium nucleatum Autotransporter Serine Protease

    doi: 10.1371/journal.pone.0111329

    Figure Lengend Snippet: Protease profiles of F. nucleatum growth medium supernatants on fibrinogen containing zymograms. M, Molecular weight markers. A, F. nucleatum ATCC 49256. B, F. nucleatum FDC 364. C, F. nucleatum ATCC 10953. D, F. nucleatum ATCC 25586. E, F. nucleatum ATCC 23726. F, F. nucleatum 12230. Arrows indicate proteolytic bands. Presented data are of representative zymograms.

    Article Snippet: However, while the peptide sequences generated from the 99 kDa proteolytic protein extracted from F. nucleatum ATCC 25586 corresponded to the entire FN1426 protein sequence , those generated from the 55 kDa proteolytic band of F. nucleatum ATCC 49256 matched only the N-terminal domain of FNV0835 ( ) suggesting that the 55 kDa protease of F. nucleatum ATCC 49256 also originated from a larger precursor.

    Techniques: Molecular Weight