EasySep™小鼠TIL（CD45）正选试剂盒
产品号 #73012_C
蛋白质运输抑制剂；抑制含sec7的鸟嘌呤交换因子（GEF）
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总览
Brefeldin A 是一种由多种真菌（包括 Eupenicillium brefeldianum）产生的内酯类抗生素（Klausner 等人）。它通过间接抑制ADP -核糖基化因子（ARF）可逆地干扰高尔基体和内质网介导的蛋白质运输和分泌；（Klausner等；Helms & Rothman；Robinson等；Morinaga等；Moss & Vaughan；Nebenführ 等；Ktistakis等)。Brefeldin A在ARF-GDP- sec7界面与含sec7的鸟嘌呤交换因子（GEF）结合，阻止释放GDP和激活ARF所需的构象变化（Mossessova等人）。
细胞系发育
·在小鼠胚胎干细胞中，增强成簇规律间隔短回文重复序列（CRISPR介导的同源定向修复（HDR） （Yu等人）。
癌症研究
·诱导人类白血病（HL60, K562）和结肠癌（HT-29）细胞系的细胞凋亡（Shao等人）。
·可降低 Colo 205 结直肠癌干细胞系的存活率，诱导其凋亡并抑制其克隆生成活力（Tseng 等人）。
细胞类型
癌细胞及细胞系，多能干细胞
种属
人，小鼠，非人灵长类，其他物种，大鼠
应用
抗生素
研究领域
癌症，细胞系制备，干细胞生物学
CAS 编号
20350-15-6
化学式
C₁₆H₂₄O₄
纯度
≥98%
靶点
GEF
产品说明书及文档
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相关材料与文献
技术资料 (2)
文献 (11)
Activation of toxin ADP-ribosyltransferases by eukaryotic ADP-ribosylation factors.
Molecular and cellular biochemistry 1999 MAR
Abstract
ADP-ribosylation factors (ARFs) are members of a multigene family of 20-kDa guanine nucleotide-binding proteins that are regulatory components in several pathways of intracellular vesicular trafficking. The relatively small (approximately 180-amino acids) ARF proteins interact with a variety of molecules (in addition to GTP/GDP,of course). Cholera toxin was the first to be recognized,hence the name. Later it was shown that ARF also activates phospholipase D. Different parts of the molecule are responsible for activation of the two enzymes. In vesicular trafficking,ARF must interact with coatomer to recruit it to a membrane and thereby initiate vesicle budding. ARF function requires that it alternate between GTP- and GDP-bound forms,which involves interaction with regulatory proteins. Inactivation of ARF-GTP depends on a GTPase-activating protein or GAP. A guanine nucleotide-exchange protein or GEP accelerates release of bound GDP from inactive ARF-GDP to permit GTP binding. Inhibition of GEP by brefeldin A (BFA) blocks ARF activation and thereby vesicular transport. In cells,it causes apparent disintegration of Golgi structure. Both BFA-sensitive and insensitive GEPs are known. Sequences of peptides from a BFA-sensitive GEP purified in our laboratory revealed the presence of a Sec7 domain,a sequence of approximately 200 amino acids that resembles a region in the yeast Sec7 gene product,which is involved in Golgi vesicular transport. Other proteins of unknown function also contain Sec7 domains,among them a lymphocyte protein called cytohesin-1. To determine whether it had GEP activity,recombinant cytohesin-1 was synthesized in E. coli. It preferentially activated class I ARFs 1 and 3 and was not inhibited by BFA but failed to activate ARF5 (class II). There are now five Sec7 domain proteins known to have GEP activity toward class I ARFs. It remains to be determined whether there are other Sec7 domain proteins that are GEPs for ARFs 4,5,or 6.
Brefeldin A inhibited activity of the sec7 domain of p200, a mammalian guanine nucleotide-exchange protein for ADP-ribosylation factors.
The Journal of biological chemistry 1999
Abstract
A brefeldin A (BFA)-inhibited guanine nucleotide-exchange protein (GEP) for ADP-ribosylation factors (ARF) was purified earlier from bovine brain cytosol. Cloning and expression of the cDNA confirmed that the recombinant protein (p200) is a BFA-sensitive ARF GEP. p200 contains a domain that is 50% identical in amino acid sequence to a region in yeast Sec7,termed the Sec7 domain. Sec7 domains have been identified also in other proteins with ARF GEP activity,some of which are not inhibited by BFA. To identify structural elements that influence GEP activity and its BFA sensitivity,several truncated mutants of p200 were made. Deletion of sequence C-terminal to the Sec7 domain did not affect GEP activity. A protein lacking 594 amino acids at the N terminus,as well as sequence following the Sec7 domain,also had high activity. The mutant lacking 630 N-terminal amino acids was,however,only 1% as active,as was the Sec7 domain itself (mutant lacking 697 N-terminal residues). It appears that the Sec7 domain of p200 contains the catalytic site but additional sequence (perhaps especially that between positions 595 and 630) modifies activity dramatically. Myristoylated recombinant ARFs were better than non-myristoylated as substrates; ARFs 1 and 3 were better than ARF5,and no activity was detected with ARF6. Physical interaction of the Sec7 domain with an ARF1 mutant was demonstrated,but it was much weaker than that of the cytohesin-1 Sec7 domain with the same ARF protein. Effects of BFA on p200 and all mutants with high activity were similar with approximately 50% inhibition at textless/=50 microM. The inactive BFA analogue B36 did not inhibit the Sec7 domain or p200. Thus,the Sec7 domain of p200,like that of Sec7 itself (Sata,M.,Donaldson,J. G.,Moss,J.,and Vaughan,M. (1998) Proc. Natl. Acad. Sci. U. S. A. 95,4204-4208),plays a role in BFA inhibition as well as in GEP activity,although the latter is markedly modified by other structural elements.
Brefeldin A: deciphering an enigmatic inhibitor of secretion.
Plant physiology 2002
Abstract
更多信息
| 物种 | 人, 其它物种, 大鼠, 小鼠, 非人灵长类 |
|---|---|
| Cas Number | 20350-15-6 |
| Chemical Formula | C₁₆H₂₄O₄ |
| 纯度 | ≥ 98% |
| Target | GEF |
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