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5μg/10μg/20μg/50μg
| 规格： | 5μg | 产品价格： | ￥307.0 |
|---|---|---|---|
| 规格： | 10μg | 产品价格： | ￥498.0 |
| 规格： | 20μg | 产品价格： | ￥811.0 |
| 规格： | 50μg | 产品价格： | ￥1626.0 |
Product Introduction
Bioactivity
| 名称 | Shiga toxin II subunit B Protein, E. coli, Recombinant (His) |
| 描述 | E. Coli STX2B is a subunit of Stx2. Stx2, together with Stx1, formed a family of related toxins which are known as shiga toxins. Shiga toxins are mainly produced by the bacteria S. dysenteriae and the Shigatoxigenic group of Escherichia coli, which includes serotypes O157:H7, O104:H4, and other enterohemorrhagic E. coli (EHEC). A total of 3222 outbreak cases (including 39 deaths) have been reported in northern Germany in May through June 2011. The outbreak strain was typed as an enteroaggregative Shiga-toxin–producing E. coli O104:H4, producing extended-spectrum beta-lactamase. The toxin has two subunits—A and B. E. Coli STX2B is the B subunit. It is a pentamer that binds to specific glycolipids on the host cell, specifically globotriaosylceramide. Following this, the A subunit is internalised and cleaved into two parts. Stx2 has been found to be approximately 400 times more toxic (as quantified by LD50 in mice) than Stx-1. The Stx1 and Stx2 B subunits form a pentameric structure that binds to globotriaosylceramide receptors on eukaryotic cells and promotes endocytosis. |
| 存储条件 | Store at low temperature Store at -80°C |
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文献和实验Shiga Toxin B-Subunit as a Tool to Study Retrograde Transport
Shiga toxin, produced by Shigella dysenteriae and Shiga toxin-producing Escherichia coli , is a bacterial protein toxin composed of two subunits, A and B (1 ). The A-subunit is the actual toxin whose ribosomal RNA N -glycosidase activity
Protocols to Study Effects of Shiga Toxin on Mononuclear Leukocytes
Endothelial cells are regarded as the main targets of the Shiga toxins (Stxs) during infections caused by Stx-producing Escherichia coli (STEC). However, several investigations also confirmed an effect of these toxins on immune cell functions
Strategies to Optimize Protein Expression in E. coli
on its in vivo activity. J. Biol. Chem. 260:3539‐3541. Brown, B.L., Hadley, M., and Page, R. 2008. Heterologous high‐level E. coli expression, purification and biophysical
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