mcherry cenexin s796a plasmids  (New England Biolabs)


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    Structured Review

    New England Biolabs mcherry cenexin s796a plasmids
    Cenexin phosphorylation at its conserved C-terminal PLK1 binding site is required for maintenance of PCM in vivo . (A) Schematic representation of human hODF2 and cenexin (Cnxn, ODF2 isoform 9). The blue and magenta boxes highlight the N- and C-terminal extensions unique to cenexin. (B) Phylogenetic tree of the evolution of cenexin and its N-terminus and C-terminus in relation to Cep192 and centrin across different animal phyla. Cyan and orange boxes indicate whether cenexin and centrosome components (Cep192 and centrin) are detected or not detected within representative species of each phylum. Dark blue boxes highlight two species (humans and zebrafish). (C) Amino acid alignment between human and zebrafish cenexin C-terminal PLK1 binding motif. The serine highlighted in magenta represents the known human cenexin-PLK1 site (S796) and potential zebrafish biding site (S829). Letters in the middle between two sequences represent identical amino acids, and the + sign represent an amino acid of functional identity. Representative confocal maximum projection of cenexin from expanded (ExM) human cells and from a zebrafish embryo cell shown. Scale bar 0.05 μm. (D-F) Representative cells from 512-cell zebrafish embryos under cenexin depletion conditions (Cenexin MO, D), or rescue conditions (cenexin MO plus mCh-cenexin or <t>mCh-cenexin-S796A,</t> magenta in E-F) fixed and immunostained for γ-tubulin (inverted grey, D-E) or pST (inverted grey, F). Insets (D’, E’, E”, F’, and F”) at 5x magnification, corresponding areas outlined (μm 2 ). Scale bar, 5μm. (G) Scatter plot depicting γ-tubulin area (μm 2 ) at mitotic centrosomes under control, cenexin MO, and rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A). Mean (magenta) with 95% confidence intervals shown. One-way ANOVA with multiple comparisons to control cells, n.s. not significant, **p
    Mcherry Cenexin S796a Plasmids, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mcherry cenexin s796a plasmids/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mcherry cenexin s796a plasmids - by Bioz Stars, 2022-08
    99/100 stars

    Images

    1) Product Images from "Pericentriolar matrix integrity relies on cenexin and Polo-Like Kinase (PLK)1"

    Article Title: Pericentriolar matrix integrity relies on cenexin and Polo-Like Kinase (PLK)1

    Journal: bioRxiv

    doi: 10.1101/2022.01.09.475500

    Cenexin phosphorylation at its conserved C-terminal PLK1 binding site is required for maintenance of PCM in vivo . (A) Schematic representation of human hODF2 and cenexin (Cnxn, ODF2 isoform 9). The blue and magenta boxes highlight the N- and C-terminal extensions unique to cenexin. (B) Phylogenetic tree of the evolution of cenexin and its N-terminus and C-terminus in relation to Cep192 and centrin across different animal phyla. Cyan and orange boxes indicate whether cenexin and centrosome components (Cep192 and centrin) are detected or not detected within representative species of each phylum. Dark blue boxes highlight two species (humans and zebrafish). (C) Amino acid alignment between human and zebrafish cenexin C-terminal PLK1 binding motif. The serine highlighted in magenta represents the known human cenexin-PLK1 site (S796) and potential zebrafish biding site (S829). Letters in the middle between two sequences represent identical amino acids, and the + sign represent an amino acid of functional identity. Representative confocal maximum projection of cenexin from expanded (ExM) human cells and from a zebrafish embryo cell shown. Scale bar 0.05 μm. (D-F) Representative cells from 512-cell zebrafish embryos under cenexin depletion conditions (Cenexin MO, D), or rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A, magenta in E-F) fixed and immunostained for γ-tubulin (inverted grey, D-E) or pST (inverted grey, F). Insets (D’, E’, E”, F’, and F”) at 5x magnification, corresponding areas outlined (μm 2 ). Scale bar, 5μm. (G) Scatter plot depicting γ-tubulin area (μm 2 ) at mitotic centrosomes under control, cenexin MO, and rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A). Mean (magenta) with 95% confidence intervals shown. One-way ANOVA with multiple comparisons to control cells, n.s. not significant, **p
    Figure Legend Snippet: Cenexin phosphorylation at its conserved C-terminal PLK1 binding site is required for maintenance of PCM in vivo . (A) Schematic representation of human hODF2 and cenexin (Cnxn, ODF2 isoform 9). The blue and magenta boxes highlight the N- and C-terminal extensions unique to cenexin. (B) Phylogenetic tree of the evolution of cenexin and its N-terminus and C-terminus in relation to Cep192 and centrin across different animal phyla. Cyan and orange boxes indicate whether cenexin and centrosome components (Cep192 and centrin) are detected or not detected within representative species of each phylum. Dark blue boxes highlight two species (humans and zebrafish). (C) Amino acid alignment between human and zebrafish cenexin C-terminal PLK1 binding motif. The serine highlighted in magenta represents the known human cenexin-PLK1 site (S796) and potential zebrafish biding site (S829). Letters in the middle between two sequences represent identical amino acids, and the + sign represent an amino acid of functional identity. Representative confocal maximum projection of cenexin from expanded (ExM) human cells and from a zebrafish embryo cell shown. Scale bar 0.05 μm. (D-F) Representative cells from 512-cell zebrafish embryos under cenexin depletion conditions (Cenexin MO, D), or rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A, magenta in E-F) fixed and immunostained for γ-tubulin (inverted grey, D-E) or pST (inverted grey, F). Insets (D’, E’, E”, F’, and F”) at 5x magnification, corresponding areas outlined (μm 2 ). Scale bar, 5μm. (G) Scatter plot depicting γ-tubulin area (μm 2 ) at mitotic centrosomes under control, cenexin MO, and rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A). Mean (magenta) with 95% confidence intervals shown. One-way ANOVA with multiple comparisons to control cells, n.s. not significant, **p

    Techniques Used: Binding Assay, In Vivo, Functional Assay

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    New England Biolabs mcherry cenexin s796a plasmids
    Cenexin phosphorylation at its conserved C-terminal PLK1 binding site is required for maintenance of PCM in vivo . (A) Schematic representation of human hODF2 and cenexin (Cnxn, ODF2 isoform 9). The blue and magenta boxes highlight the N- and C-terminal extensions unique to cenexin. (B) Phylogenetic tree of the evolution of cenexin and its N-terminus and C-terminus in relation to Cep192 and centrin across different animal phyla. Cyan and orange boxes indicate whether cenexin and centrosome components (Cep192 and centrin) are detected or not detected within representative species of each phylum. Dark blue boxes highlight two species (humans and zebrafish). (C) Amino acid alignment between human and zebrafish cenexin C-terminal PLK1 binding motif. The serine highlighted in magenta represents the known human cenexin-PLK1 site (S796) and potential zebrafish biding site (S829). Letters in the middle between two sequences represent identical amino acids, and the + sign represent an amino acid of functional identity. Representative confocal maximum projection of cenexin from expanded (ExM) human cells and from a zebrafish embryo cell shown. Scale bar 0.05 μm. (D-F) Representative cells from 512-cell zebrafish embryos under cenexin depletion conditions (Cenexin MO, D), or rescue conditions (cenexin MO plus mCh-cenexin or <t>mCh-cenexin-S796A,</t> magenta in E-F) fixed and immunostained for γ-tubulin (inverted grey, D-E) or pST (inverted grey, F). Insets (D’, E’, E”, F’, and F”) at 5x magnification, corresponding areas outlined (μm 2 ). Scale bar, 5μm. (G) Scatter plot depicting γ-tubulin area (μm 2 ) at mitotic centrosomes under control, cenexin MO, and rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A). Mean (magenta) with 95% confidence intervals shown. One-way ANOVA with multiple comparisons to control cells, n.s. not significant, **p
    Mcherry Cenexin S796a Plasmids, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mcherry cenexin s796a plasmids/product/New England Biolabs
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    mcherry cenexin s796a plasmids - by Bioz Stars, 2022-08
    99/100 stars
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    Cenexin phosphorylation at its conserved C-terminal PLK1 binding site is required for maintenance of PCM in vivo . (A) Schematic representation of human hODF2 and cenexin (Cnxn, ODF2 isoform 9). The blue and magenta boxes highlight the N- and C-terminal extensions unique to cenexin. (B) Phylogenetic tree of the evolution of cenexin and its N-terminus and C-terminus in relation to Cep192 and centrin across different animal phyla. Cyan and orange boxes indicate whether cenexin and centrosome components (Cep192 and centrin) are detected or not detected within representative species of each phylum. Dark blue boxes highlight two species (humans and zebrafish). (C) Amino acid alignment between human and zebrafish cenexin C-terminal PLK1 binding motif. The serine highlighted in magenta represents the known human cenexin-PLK1 site (S796) and potential zebrafish biding site (S829). Letters in the middle between two sequences represent identical amino acids, and the + sign represent an amino acid of functional identity. Representative confocal maximum projection of cenexin from expanded (ExM) human cells and from a zebrafish embryo cell shown. Scale bar 0.05 μm. (D-F) Representative cells from 512-cell zebrafish embryos under cenexin depletion conditions (Cenexin MO, D), or rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A, magenta in E-F) fixed and immunostained for γ-tubulin (inverted grey, D-E) or pST (inverted grey, F). Insets (D’, E’, E”, F’, and F”) at 5x magnification, corresponding areas outlined (μm 2 ). Scale bar, 5μm. (G) Scatter plot depicting γ-tubulin area (μm 2 ) at mitotic centrosomes under control, cenexin MO, and rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A). Mean (magenta) with 95% confidence intervals shown. One-way ANOVA with multiple comparisons to control cells, n.s. not significant, **p

    Journal: bioRxiv

    Article Title: Pericentriolar matrix integrity relies on cenexin and Polo-Like Kinase (PLK)1

    doi: 10.1101/2022.01.09.475500

    Figure Lengend Snippet: Cenexin phosphorylation at its conserved C-terminal PLK1 binding site is required for maintenance of PCM in vivo . (A) Schematic representation of human hODF2 and cenexin (Cnxn, ODF2 isoform 9). The blue and magenta boxes highlight the N- and C-terminal extensions unique to cenexin. (B) Phylogenetic tree of the evolution of cenexin and its N-terminus and C-terminus in relation to Cep192 and centrin across different animal phyla. Cyan and orange boxes indicate whether cenexin and centrosome components (Cep192 and centrin) are detected or not detected within representative species of each phylum. Dark blue boxes highlight two species (humans and zebrafish). (C) Amino acid alignment between human and zebrafish cenexin C-terminal PLK1 binding motif. The serine highlighted in magenta represents the known human cenexin-PLK1 site (S796) and potential zebrafish biding site (S829). Letters in the middle between two sequences represent identical amino acids, and the + sign represent an amino acid of functional identity. Representative confocal maximum projection of cenexin from expanded (ExM) human cells and from a zebrafish embryo cell shown. Scale bar 0.05 μm. (D-F) Representative cells from 512-cell zebrafish embryos under cenexin depletion conditions (Cenexin MO, D), or rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A, magenta in E-F) fixed and immunostained for γ-tubulin (inverted grey, D-E) or pST (inverted grey, F). Insets (D’, E’, E”, F’, and F”) at 5x magnification, corresponding areas outlined (μm 2 ). Scale bar, 5μm. (G) Scatter plot depicting γ-tubulin area (μm 2 ) at mitotic centrosomes under control, cenexin MO, and rescue conditions (cenexin MO plus mCh-cenexin or mCh-cenexin-S796A). Mean (magenta) with 95% confidence intervals shown. One-way ANOVA with multiple comparisons to control cells, n.s. not significant, **p

    Article Snippet: Plasmid Constructs and mRNA Gibson cloning methods were used to generate mCherry-cenexin-WT and mCherry-cenexin-S796A plasmids (NEBuilder HiFi DNA assembly kit), then purified using DNA maxi-prep kit (Bio Basic; 9K-006-0023). mRNA was generated from plasmids using mMESSAGE mMACHINE™SP6 transcription kit (Thermo Fisher Scientific; AM1340).

    Techniques: Binding Assay, In Vivo, Functional Assay