Kim J and Roeder RG (2011),&
Nucleosomal H2B ubiquitylation with purified fa... -
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XB-ART-44266
Nucleosomal
ubiquitylation with purified factors.
Diverse histone modifications play important roles in transcriptional regulation throughout eukaryotes, and recent studies have implicated histone
ubiquitylation in active transcription. The necessity of at least three enzymes (E1-E3), as well as ongoing transcription events, for efficient
ubiquitylation complicates mechanistic studies of
ubiquitylation relative to other histone modifications. Here we describe experimental protocols for preparation of human
ubiquitylation factors, ubiquitylation substrates and transcription factors, as well as the use of these factors to establish
ubiquitylation mechanisms during transcription. The methods include reliable protein interaction and E3 ubiquitylation assays that can be widely applied to confirm cognate E2-E3 pairs in other protein ubiquitylation systems, optimized in vitro ubiquitylation assays for various histone substrates, and a transcription-coupled
ubiquitylation assay in a highly purified transcription system. These comprehensive analyses have revealed (i) that RAD6 serves as the cognate E2 for the BRE1 complex in human cells, as previously established in yeast, (ii) that RAD6, through direct interaction with the BRE1 complex, ubiquitylates chromatinized
at lysine 120 and (iii) that
complex-mediated transcription is required for efficient
ubiquitylation. This experimental system permits detailed mechanistic analyses of
ubiquitylation during transcription by providing information concerning both precise enzyme functions and physical interactions between the transcription and histone modification machineries.
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,&DK071900
,&R01 CA129325
,&R01 DK071900
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Major funding for Xenbase is provided by the , grant P41 HD064556Pre-mRNA splicing by complementation with purified human U1, U2, U4/U6 and U5 snRNPs.
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1988 Oct 25;16(20):9415-29.Pre-mRNA splicing by complementation with purified human U1, U2, U4/U6 and U5 snRNPs.1.1Cold Spring Harbor Laboratory, NY 11724.AbstractThe four major nucleoplasmic small nuclear ribonucleoprotein particles U1, U2, U4/U6 and U5 can be extensively purified from HeLa cells by immunoaffinity chromatography using a monoclonal anti-trimethylguanosine antibody. The snRNP particles in active splicing extracts are selectively bound to the immunoaffinity matrix, and are then gently eluted by competition with an excess of free nucleoside. Biochemical complementation studies show that the purified snRNPs are active in pre-mRNA splicing, but only in the presence of additional non-snRNP protein factors. All the RNPs that are necessary for splicing can be purified in this manner. The active snRNPs are characterized with respect to their polypeptide composition, and shown to be distinct from several other activities implicated in splicing.PMID: 3141901
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External link. Please review our .In vitro and in vivo studies with purified recombinant human interleukin 5.
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):112-21.In vitro and in vivo studies with purified recombinant human interleukin 5.1, , , , , .1Biochemistry Department, Glaxo Group Research Ltd., Greenford, Middlesex, UK.AbstractThe functional activities of highly purified recombinant human IL 5 (hIL 5) have been characterized on a number of cell types in vitro and in BALB/c mice in vivo. In vitro, hIL 5 could induce the differentiation of eosinophils from precursors in both human and mouse bone marrow with approximately the same efficiency. A mouse IL 5/3-dependent B cell line, LyH7.B13, was found to proliferate in response to hIL 5 but not human interleukin 1 (IL 1), interleukin 2 (IL 2), interleukin 3 (IL 3), interleukin 4 (IL 4), interleukin 6 (IL 6), interferon-gamma (IFN-gamma), or granulocyte macrophage-colony stimulating factor (GM-CSF) and was at least 10-fold more sensitive than BCL1 mouse lymphoma cells. We have successfully used this cell line to demonstrate the production of IL 5 by human T cell clones. In marked contrast to its effects on murine B cell lines, hIL 5 had no demonstrable activity on CD23 expression, anti-mu costimulated proliferation or IgM, IgG, or IgE production by tonsillar B cells and did not influence such responses triggered by IL 4. BALB/c mice injected with hIL 5 for 7 consecutive days were shown to develop an eosinophilia comparable to that induced by infection with the parasite Mesocestoid corti.PMID: 2151763
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External link. Please review our .the study of Eu and Gd interaction with (purified Aldrich) HA._百度知道
the study of Eu and Gd interaction with (purified Aldrich) HA.
括号里是什么意思
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括号里的是
提纯奥尔德利奇
Aldrich 是一种产品，
purified 是净化的
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