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anti-histone+h3


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  • Balance between distinct HP1 family proteins controls heterochromatin assembly in fission yeast. 18809570

    Heterochromatin protein 1 (HP1) is a conserved chromosomal protein with important roles in chromatin packaging and gene silencing. In fission yeast, two HP1 family proteins, Swi6 and Chp2, are involved in transcriptional silencing at heterochromatic regions, but how they function and whether they act cooperatively or differentially in heterochromatin assembly remain elusive. Here, we show that both Swi6 and Chp2 are required for the assembly of fully repressive heterochromatin, in which they play distinct, nonoverlapping roles. Swi6 is expressed abundantly and plays a dose-dependent role in forming a repressive structure through its self-association property. In contrast, Chp2, expressed at a lower level, does not show a simple dose-dependent repressive activity. However, it contributes to the recruitment of chromatin-modulating factors Clr3 and Epe1 and possesses a novel ability to bind the chromatin-enriched nuclear subfraction that is closely linked with its silencing function. Finally, we demonstrate that a proper balance between Swi6 and Chp2 is critical for heterochromatin assembly. Our findings provide novel insight into the distinct and cooperative functions of multiple HP1 family proteins in the formation of higher-order chromatin structure.
    Tipo de documento:
    Referencia
    Referencia del producto:
    07-353
    Nombre del producto:
    Anti-acetyl-Histone H3 (Lys14) Antibody

  • Notch- and transducin-like enhancer of split (TLE)-dependent histone deacetylation explain interleukin 12 (IL-12) p70 inhibition by zymosan. 21402701

    The fungal analog zymosan induces IL-23 and low amounts of IL-12 p70. This study addresses the molecular mechanisms underlying this cytokine pattern in human monocyte-derived dendritic cells. The transcriptional regulation of il23a, one of the chains of IL-23, depended on the activation of c-Rel and histone H3 phosphorylation, as judged from the association of c-Rel with the il23a promoter and the correlation between IL-23 production and Ser-10-histone H3 phosphorylation. Consistent with its reduced ability to produce IL-12 p70, zymosan induced a transient occupancy of the il12a promoter by c-Rel, blocked the production of IL-12 p70 and the transcription of il12a induced by other stimuli, and triggered the expression and nuclear translocation of the transcriptional repressors of the Notch family hairy and enhancer of split (Hes)-1, Hes5, hairy/enhancer-of-split related with YRPW motif protein (Hey)-1, and transducin-like enhancer of split (TLE). Zymosan also induced the interaction of Hes1 and TLE with histone H3 phosphorylated on Ser-10 and deacetylated on Lys-14. Inhibition of class III histone deacetylases increased the production of IL-12 p70 and partially blunted the inhibitory effect of zymosan on the production of IL-12 p70 elicited by LPS and IFN-γ. These results indicate that the selective induction of IL-23 by β-glucans is explained by the activation of c-Rel associated with Ser-10-histone H3 phosphorylation in the il23a promoter mediated by mitogen- and stress-activated kinase and/or protein kinase A and inhibition of il12a transcription by a mechanism involving activation of several corepressors with the ability to bind TLE and to promote histone deacetylation.
    Tipo de documento:
    Referencia
    Referencia del producto:
    Múltiplo
    Nombre del producto:
    Múltiplo

  • Glycosylation and sialylation of macrophage-derived human apolipoprotein E analyzed by SDS-PAGE and mass spectrometry: evidence for a novel site of glycosylation on Ser29 ... 20511397

    Apolipoprotein E (apoE) is a 34-kDa glycoprotein secreted from various cells including hepatocytes and macrophages and plays an important role in remnant lipoprotein clearance, immune responses, Alzheimer disease, and atherosclerosis. Cellular apoE and plasma apoE exist as multiple glycosylated and sialylated glycoforms with plasma apoE being less glycosylated/sialylated than cell-derived apoE. Some of the glycan structures on plasma apoE are characterized; however, the more complicated structures on plasma and cellular/secreted apoE remain unidentified. We investigated glycosylation and sialylation of cellular and secreted apoE from primary human macrophages by one- and two-dimensional gel electrophoresis and mass spectrometry. Our results identify eight different glycoforms with (HexNAc)(2)-Hex(2)-(NeuAc)(2) being the most complex glycan detected on Thr(194) in both cellular and secreted apoE. Four additional glycans were identified on apoE(283-299), and using beta-elimination/alkylation by methylamine in vitro, we identified Ser(290) as a novel site of glycan attachment. Comparison of plasma and cellular/secreted apoE from the same donor confirmed that cell-derived apoE is more extensively sialylated than plasma apoE. Given the importance of the C terminus of apoE in regulating apoE solubility, stability, and lipid binding, these results may have important implications for our understanding of apoE biochemistry.
    Tipo de documento:
    Referencia
    Referencia del producto:
    05-499
    Nombre del producto:
    Anti-Histone H3 Antibody, clone 6.6.2

  • Regulation of chemokine gene expression by hypoxia via cooperative activation of NF-kappaB and histone deacetylase. 19446037

    Hypoxia is a microenvironmental factor frequently associated with tumors and inflammation. This study addresses the question of how hypoxia modulates the basal and IL-1 beta-induced production of cytokines and aims to identify the underlying mechanism of hypoxic transcriptional repression. We found that despite the similarities of the promoter structures of IL-8 and MCP-1, these chemokines were differently regulated by hypoxia (an increase in IL-8, but a decrease in MCP-1 mRNA and protein expression). Such differences were not observed in a reporter gene assay, in which both of the promoters were activated by hypoxia. The difference in the response to hypoxia between MCP-1 expression and the promoter assay was not due to mRNA instability. Using proteosome inhibitor MG132 and I kappaB overexpression we demonstrated that an NF-kappaB-dependent mechanism was involved in both the activation of IL-8 and the repression of MCP-1 mRNA expression in response to hypoxia. The histone deacetylase inhibitor Trihostatin A abolished the inhibitory actions of hypoxia on IL-1 beta-induced MCP-1 gene expression. Furthermore, hypoxia induced histone deacetylase activity in the nuclear extracts. Although stimulation with IL-1 beta and/or hypoxia increased the acetylation of histones H3 and H4 in the presence of Trihostatin A, histone acetylation remained unchanged when the cells were treated without histone deacetylase inhibitor. Collectively, our findings suggest that transiently transfected promoters are not subject to the same NF-kappaB regulatory mechanisms as their chromatinized counterparts. NF-kappaB, activated by hypoxia, can act as a transcriptional repressor via a mechanism that involves deacetylation of histones.
    Tipo de documento:
    Referencia
    Referencia del producto:
    07-108
    Nombre del producto:
    Anti-Histone H4 Antibody

  • Anti-Histone H3, CT, pan -2828613

    Tipo de documento:
    Certificado de análisis
    Número de lote:
    2828613
    Referencia del producto:
    07-690
    Nombre del producto:
    Anti-Histone H3 Antibody, CT, pan

  • Anti-Histone H3.1/H3.2 -2673173

    Tipo de documento:
    Certificado de análisis
    Número de lote:
    2673173
    Referencia del producto:
    ABE154
    Nombre del producto:
    Anti-Histone H3.1/H3.2 Antibody