Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H||IF, WB, Mplex, ICC||Rb||Affinity Purified||Polyclonal Antibody|
|Description||Anti-dimethyl-Histone H4 (Lys20) Antibody|
|Presentation||0.2M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide, 5mg/ml BSA before the addition of glycerol to 30%|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||1 year at -20°C|
|Material Size||100 µL|
|Anti-dimethyl-Histone H4 (Lys20) - 20299||20299|
|Anti-dimethyl-Histone H4 (Lys20) - 24799||24799|
|Reference overview||Application||Pub Med ID|
|A cellular study of teosinte Zea mays subsp. parviglumis (Poaceae) caryopsis development showing several processes conserved in maize.|
Marina Dermastia,Ales Kladnik,Jasna Dolenc Koce,Prem S Chourey
American journal of botany 96 2009
The evolutionary history of maize (Zea mays subsp. mays) is of general interest because of its economic and scientific importance. Here we show that many cellular traits described previously in developing caryopses of maize are also seen in its wild progenitor teosinte (Zea mays subsp. parviglumis). These features, each with a possible role in development, include (1) an early programmed cell death in the maternal placento-chalazal (P-C) layer that may lead to increased hydrolytic conductance to the developing seed; (2) accumulation of phenolics and flavonoids in the P-C layer that may be related to antimicrobial activity; (3) formation of wall ingrowths in the basal endosperm transfer layer (BETL); (4) localization of cell wall invertase in the BETL, which is attributed to the increased transport capacity of photosynthates to the sink; and (5) endoreduplication in endosperm nuclei suggested to contribute to increased gene expression and greater sink capacity of the developing seed. In maize caryopsis, these cellular traits have been previously attributed to domestication and selection for larger seed size and vigor. Given the conservation of the entire cellular program in developing teosinte caryopses described here, we suggest that these traits evolved independently of domestication and predate human selection pressure.
|An in vitro investigation of herbs traditionally used for kidney and urinary system disorders: potential therapeutic and toxic effects.|
Ken Wojcikowski,Hans Wohlmuth,David W Johnson,Margaret Rolfe,Glenda Gobe
Nephrology (Carlton, Vic.) 14 2009
Renal fibrosis is central to progression of most chronic renal pathologies. Antioxidants that protect the tubular epithelium and anti-fibrotics that induce apoptosis of pro-fibrotic myofibroblasts without adversely affecting tubular epithelium may slow progression of renal fibrosis, while toxic substances may exacerbate renal scarring. We investigated 47 herbs for their in vitro toxic or antioxidant effects on normal renal mammalian fibroblasts (NRK49F) and tubular epithelial cells (NRK52E) to determine their potential value as therapeutic agents in renal fibrosis involving oxidative stress.
|The fission yeast Jmj2 reverses histone H3 Lysine 4 trimethylation.|
Huarte, M; Lan, F; Kim, T; Vaughn, MW; Zaratiegui, M; Martienssen, RA; Buratowski, S; Shi, Y
The Journal of biological chemistry 282 21662-70 2007
Histone methylation regulates transcription, chromatin structure, and the epigenetic state of the cell. Recent studies identified the JmjC domain as a catalytic module for histone demethylation. Schizosaccharomyces pombe contains seven JmjC proteins, but it was unclear whether any of them functioned as histone demethylases. In this report, we show that the JmjC protein Jmj2, which is evolutionarily conserved from yeast to human, reversed trimethylated H3-Lys-4 to di- and mono-but not unmethylated products. Overexpression of Jmj2 but not a catalytically inactive mutant reduced H3-Lys-4 trimethylation levels in vivo and suppressed the toxicity caused by overexpression of the H3-Lys-4-me3-binding protein Yng1 in budding yeast. Genome-wide analysis showed that the loss of jmj2 was associated with an increase in the H3-Lys-4-me3 signal, which was enriched near the transcriptional start sites and the coding regions. At the mating-type locus, the loss of jmj2 or substitution of jmj2 with a catalytically inactive form is correlated with increased reporter gene transcription and H3-Lys-4-me3/2 levels, suggesting that Jmj2 and its demethylase activity may play a role in heterochromatin biology. Our findings identified a novel S. pombe histone demethylase with specificity toward di- and trimethylated histone H3-Lys-4 and a possible role in heterochromatin regulation.
|Profile of histone lysine methylation across transcribed mammalian chromatin.|
Vakoc, CR; Sachdeva, MM; Wang, H; Blobel, GA
Molecular and cellular biology 26 9185-95 2006
Complex patterns of histone lysine methylation encode distinct functions within chromatin. We previously reported that trimethylation of lysine 9 of histone H3 (H3K9) occurs at both silent heterochromatin and at the transcribed regions of active mammalian genes, suggesting that the extent of histone lysine methylation involved in mammalian gene activation is not completely defined. To identify additional sites of histone methylation that respond to mammalian gene activity, we describe here a comparative assessment of all six known positions of histone lysine methylation and relate them to gene transcription. Using several model loci, we observed high trimethylation of H3K4, H3K9, H3K36, and H3K79 in the transcribed region, consistent with previous findings. We identify H4K20 monomethylation, a modification previously linked with repression, as a mark of transcription elongation in mammalian cells. In contrast, H3K27 monomethylation, a modification enriched at pericentromeric heterochromatin, was observed broadly distributed throughout all euchromatic sites analyzed, with selective depletion in the vicinity of the transcription start sites at active genes. Together, these results underscore that similar to other described methyl-lysine modifications, H4K20 and H3K27 monomethylation are versatile and dynamic with respect to gene activity, suggesting the existence of novel site-specific methyltransferases and demethylases coupled to the transcription cycle.
|Granulocyte heterochromatin: defining the epigenome.|
Olins, DE; Olins, AL
BMC cell biology 6 39 2005
Mammalian blood neutrophilic granulocytes are terminally differentiated cells, possessing extensive heterochromatin and lobulated (or ring-shaped) nuclei. Despite the extensive amount of heterochromatin, neutrophils are capable of increased gene expression, when activated by bacterial infection. Understanding the mechanisms of transcriptional repression and activation in neutrophils requires detailing the chromatin epigenetic markers, which are virtually undescribed in this cell type. Much is known about the heterochromatin epigenetic markers in other cell-types, permitting a basis for comparison with those of mature normal neutrophilic granulocytes.Immunostaining and immunoblotting procedures were employed to study the presence of repressive histone modifications and HP1 proteins in normal human and mouse blood neutrophils, and in vitro differentiated granulocytes of the mouse promyelocytic (MPRO) system. A variety of repressive histone methylation markers were detectable in these granulocytes (di- and trimethylated H3K9; mono-, di- and trimethyl H3K27; di- and trimethyl H4K20). However, a paucity of HP1 proteins was noted. These granulocytes revealed negligible amounts of HP1 alpha and beta, but exhibited detectable levels of HP1 gamma. Of particular interest, mouse blood and MPRO undifferentiated cells and granulocytes revealed clear co-localization of trimethylated H3K9, trimethylated H4K20 and HP1 gamma with pericentric heterochromatin.Mature blood neutrophils possess some epigenetic heterochromatin features that resemble those of well-studied cells, such as lymphocytes. However, the apparent paucity of HP1 proteins in neutrophils suggests that heterochromatin organization and binding to the nuclear envelope may differ in this cell-type. Future investigations should follow changes in epigenetic markers and levels of HP1 proteins during granulopoiesis and bacterial activation of neutrophils.Full Text Article
|What is the concentration of this antibody?||The presence of BSA in this antibody limits our ability to perform a Bradford Concentration assay.|