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  • 92
    Biosynth Carbosynth xenopus hdac1
    Inhibition of <t>HDAC1/2</t> counteracts transcription suppression and increases DNA accessibility. A , pActin was incubated in NPE supplemented with 100 μM of the indicated HDAC inhibitor. RNA was isolated and quantified after 120 min (n = 3). B , pActin and pActin ΔTATA were incubated in NPE supplemented with 10 ng/μl α-amanitin and/or 100 μM Romidepsin, as indicated. RNA was isolated and quantified after 120 min (n = 2). C , pActin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). D , pActin was incubated in NPE for 90 min. Reactions were then supplemented with either buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). E , about 30 ng/μl pActin was incubated in NPE supplemented with buffer or Romidepsin for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ) (n = 2). G , sperm chromatin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area from ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. NPE, nucleoplasmic extract.
    Xenopus Hdac1, supplied by Biosynth Carbosynth, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/xenopus hdac1/product/Biosynth Carbosynth
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    xenopus hdac1 - by Bioz Stars, 2024-06
    92/100 stars
      Buy from Supplier

    90
    ProSci Incorporated nalp2 antibody
    Inhibition of <t>HDAC1/2</t> counteracts transcription suppression and increases DNA accessibility. A , pActin was incubated in NPE supplemented with 100 μM of the indicated HDAC inhibitor. RNA was isolated and quantified after 120 min (n = 3). B , pActin and pActin ΔTATA were incubated in NPE supplemented with 10 ng/μl α-amanitin and/or 100 μM Romidepsin, as indicated. RNA was isolated and quantified after 120 min (n = 2). C , pActin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). D , pActin was incubated in NPE for 90 min. Reactions were then supplemented with either buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). E , about 30 ng/μl pActin was incubated in NPE supplemented with buffer or Romidepsin for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ) (n = 2). G , sperm chromatin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area from ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. NPE, nucleoplasmic extract.
    Nalp2 Antibody, supplied by ProSci Incorporated, 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/result/nalp2 antibody/product/ProSci Incorporated
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    nalp2 antibody - by Bioz Stars, 2024-06
    90/100 stars
      Buy from Supplier

    96
    Cell Signaling Technology Inc rabbit anti igf1r β polyclonal
    Inhibition of <t>HDAC1/2</t> counteracts transcription suppression and increases DNA accessibility. A , pActin was incubated in NPE supplemented with 100 μM of the indicated HDAC inhibitor. RNA was isolated and quantified after 120 min (n = 3). B , pActin and pActin ΔTATA were incubated in NPE supplemented with 10 ng/μl α-amanitin and/or 100 μM Romidepsin, as indicated. RNA was isolated and quantified after 120 min (n = 2). C , pActin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). D , pActin was incubated in NPE for 90 min. Reactions were then supplemented with either buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). E , about 30 ng/μl pActin was incubated in NPE supplemented with buffer or Romidepsin for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ) (n = 2). G , sperm chromatin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area from ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. NPE, nucleoplasmic extract.
    Rabbit Anti Igf1r β Polyclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti igf1r β polyclonal/product/Cell Signaling Technology Inc
    Average 96 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti igf1r β polyclonal - by Bioz Stars, 2024-06
    96/100 stars
      Buy from Supplier

    86
    DSMZ methanocorpusculum
    Inhibition of <t>HDAC1/2</t> counteracts transcription suppression and increases DNA accessibility. A , pActin was incubated in NPE supplemented with 100 μM of the indicated HDAC inhibitor. RNA was isolated and quantified after 120 min (n = 3). B , pActin and pActin ΔTATA were incubated in NPE supplemented with 10 ng/μl α-amanitin and/or 100 μM Romidepsin, as indicated. RNA was isolated and quantified after 120 min (n = 2). C , pActin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). D , pActin was incubated in NPE for 90 min. Reactions were then supplemented with either buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). E , about 30 ng/μl pActin was incubated in NPE supplemented with buffer or Romidepsin for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ) (n = 2). G , sperm chromatin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area from ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. NPE, nucleoplasmic extract.
    Methanocorpusculum, supplied by DSMZ, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/methanocorpusculum/product/DSMZ
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    methanocorpusculum - by Bioz Stars, 2024-06
    86/100 stars
      Buy from Supplier

    86
    Cell Signaling Technology Inc ○ ○ ○ ○ 3027
    Inhibition of <t>HDAC1/2</t> counteracts transcription suppression and increases DNA accessibility. A , pActin was incubated in NPE supplemented with 100 μM of the indicated HDAC inhibitor. RNA was isolated and quantified after 120 min (n = 3). B , pActin and pActin ΔTATA were incubated in NPE supplemented with 10 ng/μl α-amanitin and/or 100 μM Romidepsin, as indicated. RNA was isolated and quantified after 120 min (n = 2). C , pActin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). D , pActin was incubated in NPE for 90 min. Reactions were then supplemented with either buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). E , about 30 ng/μl pActin was incubated in NPE supplemented with buffer or Romidepsin for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ) (n = 2). G , sperm chromatin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area from ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. NPE, nucleoplasmic extract.
    ○ ○ ○ ○ 3027, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/○ ○ ○ ○ 3027/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    ○ ○ ○ ○ 3027 - by Bioz Stars, 2024-06
    86/100 stars
      Buy from Supplier

    Image Search Results


    Inhibition of HDAC1/2 counteracts transcription suppression and increases DNA accessibility. A , pActin was incubated in NPE supplemented with 100 μM of the indicated HDAC inhibitor. RNA was isolated and quantified after 120 min (n = 3). B , pActin and pActin ΔTATA were incubated in NPE supplemented with 10 ng/μl α-amanitin and/or 100 μM Romidepsin, as indicated. RNA was isolated and quantified after 120 min (n = 2). C , pActin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). D , pActin was incubated in NPE for 90 min. Reactions were then supplemented with either buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). E , about 30 ng/μl pActin was incubated in NPE supplemented with buffer or Romidepsin for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ) (n = 2). G , sperm chromatin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area from ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. NPE, nucleoplasmic extract.

    Journal: The Journal of Biological Chemistry

    Article Title: Transcription suppression is mediated by the HDAC1–Sin3 complex in Xenopus nucleoplasmic extract

    doi: 10.1016/j.jbc.2022.102578

    Figure Lengend Snippet: Inhibition of HDAC1/2 counteracts transcription suppression and increases DNA accessibility. A , pActin was incubated in NPE supplemented with 100 μM of the indicated HDAC inhibitor. RNA was isolated and quantified after 120 min (n = 3). B , pActin and pActin ΔTATA were incubated in NPE supplemented with 10 ng/μl α-amanitin and/or 100 μM Romidepsin, as indicated. RNA was isolated and quantified after 120 min (n = 2). C , pActin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). D , pActin was incubated in NPE for 90 min. Reactions were then supplemented with either buffer or 100 μM Romidepsin. RNA was isolated and quantified at the indicated time points (n = 2). E , about 30 ng/μl pActin was incubated in NPE supplemented with buffer or Romidepsin for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ) (n = 2). G , sperm chromatin was incubated in NPE supplemented with buffer or 100 μM Romidepsin. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area from ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. NPE, nucleoplasmic extract.

    Article Snippet: Antibodies for Xenopus HDAC1, HDAC2, and BRD4 were produced by New England Peptide (NEP) using the following antigen sequences: HDAC1, KTDSKRVKEETKS; HDAC2, MDTKGVKSEQPINP; and BRD4, NFQSELMEIFEQNLFS.

    Techniques: Inhibition, Incubation, Isolation, Cleavage Assay, Plasmid Preparation, Light Microscopy

    HDAC1 drives transcription suppression. A , schematic representation of HDAC1 and HDAC2. Unique amino acid sequences used to generate peptide antigens are shown at the C terminus for each protein. B , pActin was incubated in NPE supplemented with buffer or Romidepsin. Samples were withdrawn at the indicated time points and binding of HDAC1 and HDAC2 to the actb promoter region was analyzed by ChIP (n = 3). Significance shown for comparison between +Buffer and +Romidepsin reactions. C , NPE was immunodepleted using preimmune (ΔMock), HDAC1 (ΔHDAC1), HDAC2 (ΔHDAC2), or a combination HDAC1 and 2 (ΔHDAC1&2) antibodies. Depleted extracts were analyzed by Western blot with the indicated antibodies. D , pActin was incubated in depleted extracts from ( C ). RNA was isolated and quantified after 120 min (n = 3). E , pActin was incubated in mock-, HDAC1-, or HDAC2-depleted extract for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ). G , sperm chromatin was incubated in mock-, HDAC1-, or HDAC2-depleted extracts. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area in ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. ChIP, chromatin immunoprecipitation; NPE, nucleoplasmic extract.

    Journal: The Journal of Biological Chemistry

    Article Title: Transcription suppression is mediated by the HDAC1–Sin3 complex in Xenopus nucleoplasmic extract

    doi: 10.1016/j.jbc.2022.102578

    Figure Lengend Snippet: HDAC1 drives transcription suppression. A , schematic representation of HDAC1 and HDAC2. Unique amino acid sequences used to generate peptide antigens are shown at the C terminus for each protein. B , pActin was incubated in NPE supplemented with buffer or Romidepsin. Samples were withdrawn at the indicated time points and binding of HDAC1 and HDAC2 to the actb promoter region was analyzed by ChIP (n = 3). Significance shown for comparison between +Buffer and +Romidepsin reactions. C , NPE was immunodepleted using preimmune (ΔMock), HDAC1 (ΔHDAC1), HDAC2 (ΔHDAC2), or a combination HDAC1 and 2 (ΔHDAC1&2) antibodies. Depleted extracts were analyzed by Western blot with the indicated antibodies. D , pActin was incubated in depleted extracts from ( C ). RNA was isolated and quantified after 120 min (n = 3). E , pActin was incubated in mock-, HDAC1-, or HDAC2-depleted extract for 120 min. Samples were then analyzed by the MNase cleavage assay (n = 2). Supercoiled (SC). F , quantification of SC plasmid intensity in ( E ). G , sperm chromatin was incubated in mock-, HDAC1-, or HDAC2-depleted extracts. At the indicated time points, samples were withdrawn and visualized by phase contrast light microscopy (n = 2). H , quantification of two-dimensional chromatin area in ( G ). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. ChIP, chromatin immunoprecipitation; NPE, nucleoplasmic extract.

    Article Snippet: Antibodies for Xenopus HDAC1, HDAC2, and BRD4 were produced by New England Peptide (NEP) using the following antigen sequences: HDAC1, KTDSKRVKEETKS; HDAC2, MDTKGVKSEQPINP; and BRD4, NFQSELMEIFEQNLFS.

    Techniques: Incubation, Binding Assay, Western Blot, Isolation, Cleavage Assay, Plasmid Preparation, Light Microscopy, Chromatin Immunoprecipitation

    The Sin3 deacetylase complex promotes transcription suppression. A , sequential IP schematic. B , mock, HDAC1, or HDAC2 IPs were performed in NPE. The supernatants from HDAC1 or HDAC2 IPs were then used for a second round of IPs using the converse antibody. Isolated proteins were then analyzed by Western blot with the indicated antibodies (n = 3). 10% of total reaction sample (IN), supernatant (S), pellet (P). C , NPE was immunodepleted using preimmune (ΔMock) or MTA2 (ΔMTA2) antibodies. Depleted extracts were analyzed by Western blot using the indicated antibodies. D , pActin was incubated in mock- or MTA2-depleted extract. RNA was isolated and quantified after 120 min (n = 2). E , NPE was immunodepleted using preimmune (ΔMock) or Sin3a (ΔSin3a) antibodies. Depleted extracts were analyzed by Western blot using the indicated antibodies. F , pActin was incubated in mock- or Sin3a-depleted extract. RNA was isolated and quantified after 120 min (n = 2). G , NPE was immunodepleted using preimmune (ΔMock) or HDAC1 (ΔHDAC1) antibodies. HDAC1-depleted extract was then supplemented with immunoprecipitated proteins recovered by preimmune (+Mock IP) or Sin3a (+Sin3a IP) IP. pActin was incubated in each extract and RNA was isolated and quantified after 120 min (n = 2). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. IP, immunoprecipitation; NPE, nucleoplasmic extract.

    Journal: The Journal of Biological Chemistry

    Article Title: Transcription suppression is mediated by the HDAC1–Sin3 complex in Xenopus nucleoplasmic extract

    doi: 10.1016/j.jbc.2022.102578

    Figure Lengend Snippet: The Sin3 deacetylase complex promotes transcription suppression. A , sequential IP schematic. B , mock, HDAC1, or HDAC2 IPs were performed in NPE. The supernatants from HDAC1 or HDAC2 IPs were then used for a second round of IPs using the converse antibody. Isolated proteins were then analyzed by Western blot with the indicated antibodies (n = 3). 10% of total reaction sample (IN), supernatant (S), pellet (P). C , NPE was immunodepleted using preimmune (ΔMock) or MTA2 (ΔMTA2) antibodies. Depleted extracts were analyzed by Western blot using the indicated antibodies. D , pActin was incubated in mock- or MTA2-depleted extract. RNA was isolated and quantified after 120 min (n = 2). E , NPE was immunodepleted using preimmune (ΔMock) or Sin3a (ΔSin3a) antibodies. Depleted extracts were analyzed by Western blot using the indicated antibodies. F , pActin was incubated in mock- or Sin3a-depleted extract. RNA was isolated and quantified after 120 min (n = 2). G , NPE was immunodepleted using preimmune (ΔMock) or HDAC1 (ΔHDAC1) antibodies. HDAC1-depleted extract was then supplemented with immunoprecipitated proteins recovered by preimmune (+Mock IP) or Sin3a (+Sin3a IP) IP. pActin was incubated in each extract and RNA was isolated and quantified after 120 min (n = 2). Student t test: p -value < 0.05 (∗), p -value < 0.01 (∗∗), p -value < 0.001 (∗∗∗), not significant (n.s.). Error bars represent ±1 SD. IP, immunoprecipitation; NPE, nucleoplasmic extract.

    Article Snippet: Antibodies for Xenopus HDAC1, HDAC2, and BRD4 were produced by New England Peptide (NEP) using the following antigen sequences: HDAC1, KTDSKRVKEETKS; HDAC2, MDTKGVKSEQPINP; and BRD4, NFQSELMEIFEQNLFS.

    Techniques: Histone Deacetylase Assay, Isolation, Western Blot, Incubation, Immunoprecipitation