推荐产品
产品名称
鬼笔环肽 来源于鬼笔鹅膏, ≥90%
生物来源
Amanita phalloides
质量水平
方案
≥90%
表单
powder
SMILES字符串
CC(O)C1NC(=O)C(C)NC(=O)C(CC(C)(O)CO)NC(=O)C2Cc3c(SCC(NC1=O)C(=O)N4CC(O)CC4C(=O)NC(C)C(=O)N2)[nH]c5ccccc35
InChI
1S/C35H48N8O11S/c1-15-27(47)38-22-10-20-19-7-5-6-8-21(19)41-33(20)55-13-24(34(53)43-12-18(46)9-25(43)31(51)37-15)40-32(52)26(17(3)45)42-28(48)16(2)36-30(50)23(39-29(22)49)11-35(4,54)14-44/h5-8,15-18,22-26,41,44-46,54H,9-14H2,1-4H3,(H,36,50)(H,37,51)(H,38,47)(H,39,49)(H,40,52)(H,42,48)
InChI key
KPKZJLCSROULON-UHFFFAOYSA-N
正在寻找类似产品? 访问 产品对比指南
一般描述
鬼笔环肽是由死亡之帽鬼笔鹅膏产生的鬼笔毒素。它是一种可与肌动蛋白相互作用的环状肽,最早是在鬼笔环肽中毒的大鼠中发现的。它是一种七肽,本质上是环状的,在6位色氨酸和3位半胱氨酸之间具有交联键。鬼笔环肽中氨基酸7(γ-δ-二羟基亮氨酸)的侧链可被修饰,通过该修饰可以产生荧光标记的鬼笔环肽化合物。
应用
鬼笔环肽已用于:
- 作为 PEM 缓冲液和二甲基亚砜 (DMSO) 的补充剂。
- 作为药物。
- 在免疫组织化学中用于 F-肌动蛋白的染色。
生化/生理作用
结合聚合F肌动蛋白的毒素,从而稳定肌动蛋白并干扰富含肌动蛋白的结构的功能。
鬼笔环肽与聚合肌动蛋白相互作用,而不与寡聚或单体形式相互作用。这种相互作用产生高度稳定的肌动蛋白丝,能抵抗解聚和分解。在大鼠中,这种毒素可导致肝出血死亡,细胞显示出异常的肌动蛋白聚集。对荧光标记的鬼笔环肽化合物进行衍生化后,鬼笔环肽对肌动蛋白的亲和力并未显著改变改变。这些化合物可用于研究真核细胞内肌动蛋白的结构和组织。
警示用语:
Danger
危险分类
Acute Tox. 2 Oral
储存分类代码
6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
高风险级别生物产品--毒素类产品
Acta biomaterialia, 9(3), 5511-5520 (2012-11-08)
Corneal stem cell niches are located within the limbus of the eye and are believed to play an important role in corneal regeneration. These niches are often lost in corneal disease or trauma. Our work explores the design of artificial
Correlative light and electron microscopy of the cytoskeleton of cultured cells.
Methods in Enzymology, 298, 570-592 (1998)
Proceedings of the National Academy of Sciences of the United States of America, 109(26), 10364-10369 (2012-06-13)
Actin filaments play a fundamental role in cell mechanics: assembled into networks by a large number of partners, they ensure cell integrity, deformability, and migration. Here we focus on the mechanics of the dense branched network found at the leading
Biomaterials, 269, 120356-120356 (2020-11-16)
Epicardial placement of mesenchymal stromal cells (MSCs) is a promising strategy for cardiac repair post-myocardial infarction, but requires the design of biomaterials to maximise the retention of donor cells on the heart surface and control their phenotype. To this end
The EMBO journal, 32(13), 1886-1902 (2013-06-04)
Nuclei of Xenopus laevis oocytes grow 100 000-fold larger in volume than a typical somatic nucleus and require an unusual intranuclear F-actin scaffold for mechanical stability. We now developed a method for mapping F-actin interactomes and identified a comprehensive set of
我们的科学家团队拥有各种研究领域经验,包括生命科学、材料科学、化学合成、色谱、分析及许多其他领域.
联系技术服务部门