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  • 93
    Thermo Fisher dna fragment
    Localisation properties of the various tethering constructs HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for <t>CENP‐C</t> after pre‐extraction. Line scan showing the expressed HP1α construct and CENP‐C (i); the expressed HP1α construct only (ii); CENP‐C only (iii). Scale bars, 5 μm. Alignment of the CENP‐B <t>DNA‐binding</t> domain protein sequences from various species. Multiple sequence alignment was performed using Clustal Omega and edited with Aline for display. The following species were used for the alignment: Homo sapiens , Mus musculus , Cricetulus griseus , Rattus norvegicus , Schizosaccharomyces pombe (CENP‐B homolog proteins 1 and 2), Ornithorhynchus anatinus , Bos taurus , Cavia porcellus , Macaca mulatta and Pediculus humanus . Structure of the CENP‐B DNA‐binding domain is shown as a ribbon diagram interacting with DNA (PDB code 1HLV). Mutated residues are shown in stick. HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C. Scale bar, 5 μm. Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs were detected with anti‐GFP antibody and α‐tubulin was used as a loading control.
    Dna Fragment, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Thermo Fisher dna binding domain dbd
    Localisation properties of the various tethering constructs HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for <t>CENP‐C</t> after pre‐extraction. Line scan showing the expressed HP1α construct and CENP‐C (i); the expressed HP1α construct only (ii); CENP‐C only (iii). Scale bars, 5 μm. Alignment of the CENP‐B <t>DNA‐binding</t> domain protein sequences from various species. Multiple sequence alignment was performed using Clustal Omega and edited with Aline for display. The following species were used for the alignment: Homo sapiens , Mus musculus , Cricetulus griseus , Rattus norvegicus , Schizosaccharomyces pombe (CENP‐B homolog proteins 1 and 2), Ornithorhynchus anatinus , Bos taurus , Cavia porcellus , Macaca mulatta and Pediculus humanus . Structure of the CENP‐B DNA‐binding domain is shown as a ribbon diagram interacting with DNA (PDB code 1HLV). Mutated residues are shown in stick. HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C. Scale bar, 5 μm. Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs were detected with anti‐GFP antibody and α‐tubulin was used as a loading control.
    Dna Binding Domain Dbd, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher human cell line expression
    Localisation properties of the various tethering constructs HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for <t>CENP‐C</t> after pre‐extraction. Line scan showing the expressed HP1α construct and CENP‐C (i); the expressed HP1α construct only (ii); CENP‐C only (iii). Scale bars, 5 μm. Alignment of the CENP‐B <t>DNA‐binding</t> domain protein sequences from various species. Multiple sequence alignment was performed using Clustal Omega and edited with Aline for display. The following species were used for the alignment: Homo sapiens , Mus musculus , Cricetulus griseus , Rattus norvegicus , Schizosaccharomyces pombe (CENP‐B homolog proteins 1 and 2), Ornithorhynchus anatinus , Bos taurus , Cavia porcellus , Macaca mulatta and Pediculus humanus . Structure of the CENP‐B DNA‐binding domain is shown as a ribbon diagram interacting with DNA (PDB code 1HLV). Mutated residues are shown in stick. HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C. Scale bar, 5 μm. Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs were detected with anti‐GFP antibody and α‐tubulin was used as a loading control.
    Human Cell Line Expression, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher r125a
    Localisation properties of the various tethering constructs HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for <t>CENP‐C</t> after pre‐extraction. Line scan showing the expressed HP1α construct and CENP‐C (i); the expressed HP1α construct only (ii); CENP‐C only (iii). Scale bars, 5 μm. Alignment of the CENP‐B <t>DNA‐binding</t> domain protein sequences from various species. Multiple sequence alignment was performed using Clustal Omega and edited with Aline for display. The following species were used for the alignment: Homo sapiens , Mus musculus , Cricetulus griseus , Rattus norvegicus , Schizosaccharomyces pombe (CENP‐B homolog proteins 1 and 2), Ornithorhynchus anatinus , Bos taurus , Cavia porcellus , Macaca mulatta and Pediculus humanus . Structure of the CENP‐B DNA‐binding domain is shown as a ribbon diagram interacting with DNA (PDB code 1HLV). Mutated residues are shown in stick. HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C. Scale bar, 5 μm. Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs were detected with anti‐GFP antibody and α‐tubulin was used as a loading control.
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    Standard format Plasmid sent in bacteria as agar stab
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    Image Search Results


    Localisation properties of the various tethering constructs HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C after pre‐extraction. Line scan showing the expressed HP1α construct and CENP‐C (i); the expressed HP1α construct only (ii); CENP‐C only (iii). Scale bars, 5 μm. Alignment of the CENP‐B DNA‐binding domain protein sequences from various species. Multiple sequence alignment was performed using Clustal Omega and edited with Aline for display. The following species were used for the alignment: Homo sapiens , Mus musculus , Cricetulus griseus , Rattus norvegicus , Schizosaccharomyces pombe (CENP‐B homolog proteins 1 and 2), Ornithorhynchus anatinus , Bos taurus , Cavia porcellus , Macaca mulatta and Pediculus humanus . Structure of the CENP‐B DNA‐binding domain is shown as a ribbon diagram interacting with DNA (PDB code 1HLV). Mutated residues are shown in stick. HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C. Scale bar, 5 μm. Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs were detected with anti‐GFP antibody and α‐tubulin was used as a loading control.

    Journal: The EMBO Journal

    Article Title: HP1α targets the chromosomal passenger complex for activation at heterochromatin before mitotic entry

    doi: 10.15252/embj.201797677

    Figure Lengend Snippet: Localisation properties of the various tethering constructs HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C after pre‐extraction. Line scan showing the expressed HP1α construct and CENP‐C (i); the expressed HP1α construct only (ii); CENP‐C only (iii). Scale bars, 5 μm. Alignment of the CENP‐B DNA‐binding domain protein sequences from various species. Multiple sequence alignment was performed using Clustal Omega and edited with Aline for display. The following species were used for the alignment: Homo sapiens , Mus musculus , Cricetulus griseus , Rattus norvegicus , Schizosaccharomyces pombe (CENP‐B homolog proteins 1 and 2), Ornithorhynchus anatinus , Bos taurus , Cavia porcellus , Macaca mulatta and Pediculus humanus . Structure of the CENP‐B DNA‐binding domain is shown as a ribbon diagram interacting with DNA (PDB code 1HLV). Mutated residues are shown in stick. HeLa cells expressing the indicated HP1α fusion constructs, stained with Hoechst 33342 and immunostained for CENP‐C. Scale bar, 5 μm. Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs were detected with anti‐GFP antibody and α‐tubulin was used as a loading control.

    Article Snippet: To generate CENP‐BDBD‐mut ‐EYFP‐HP1α, the DNA fragment corresponding to the DBD of human CENP‐B (1–159aa), but coding for the substitutions S40A, N120A, R125A, was synthesised by Geneart and cloned into the NheI and AgeI restriction sites of the pYIP CENP‐BDBD ‐EYFP‐HP1α plasmid, replacing the wild‐type CENP‐BDBD .

    Techniques: Construct, Expressing, Staining, Binding Assay, Sequencing, Transfection

    Tethering HP 1α to centromeres via fusion to a CENP ‐B DNA ‐binding domain causes a mitotic delay Schematic representation of the various HP1α constructs. Frequency of mitotic HeLa cells 24 h after transfection with the indicated constructs (transfection efficiency ˜70%, judged by fluorescence microscopy). Graphs represent the mean, and error bars represent the standard deviation (SD) of three independent experiments ( n = 500 cells per experiment). Frequency of mitotic phases in HeLa cells 24 h after transfection. Graphs show mean and SD of three independent experiments ( n = 60 mitotic cells per experiment). Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs and endogenous HP1α were identified using an anti‐HP1α antibody, and GAPDH was used as a loading control. Quantitative FRAP analysis of the indicated HP1α fusion constructs in interphase HeLa cells. Error bars show SD. Diagram of the tethered HP1α mutants and their perturbed functions. Frequency of mitotic phases in HeLa cells 24 h after transfection. Graphs show mean and SD of three independent experiments ( n = 60 mitotic cells per experiment). Data information: (B, C, G) Statistical significance was determined by Fisher's exact test followed by the Benjamini–Hochberg multiple comparison test. * P

    Journal: The EMBO Journal

    Article Title: HP1α targets the chromosomal passenger complex for activation at heterochromatin before mitotic entry

    doi: 10.15252/embj.201797677

    Figure Lengend Snippet: Tethering HP 1α to centromeres via fusion to a CENP ‐B DNA ‐binding domain causes a mitotic delay Schematic representation of the various HP1α constructs. Frequency of mitotic HeLa cells 24 h after transfection with the indicated constructs (transfection efficiency ˜70%, judged by fluorescence microscopy). Graphs represent the mean, and error bars represent the standard deviation (SD) of three independent experiments ( n = 500 cells per experiment). Frequency of mitotic phases in HeLa cells 24 h after transfection. Graphs show mean and SD of three independent experiments ( n = 60 mitotic cells per experiment). Immunoblot of HeLa cell lysates transfected with the indicated HP1α fusion constructs. HP1α fusion constructs and endogenous HP1α were identified using an anti‐HP1α antibody, and GAPDH was used as a loading control. Quantitative FRAP analysis of the indicated HP1α fusion constructs in interphase HeLa cells. Error bars show SD. Diagram of the tethered HP1α mutants and their perturbed functions. Frequency of mitotic phases in HeLa cells 24 h after transfection. Graphs show mean and SD of three independent experiments ( n = 60 mitotic cells per experiment). Data information: (B, C, G) Statistical significance was determined by Fisher's exact test followed by the Benjamini–Hochberg multiple comparison test. * P

    Article Snippet: To generate CENP‐BDBD‐mut ‐EYFP‐HP1α, the DNA fragment corresponding to the DBD of human CENP‐B (1–159aa), but coding for the substitutions S40A, N120A, R125A, was synthesised by Geneart and cloned into the NheI and AgeI restriction sites of the pYIP CENP‐BDBD ‐EYFP‐HP1α plasmid, replacing the wild‐type CENP‐BDBD .

    Techniques: Binding Assay, Construct, Transfection, Fluorescence, Microscopy, Standard Deviation