E6763
Erabutoxin A from Laticauda semifasciata (Sea Snake)
lyophilized powder
别名:
Snake toxin from Laticauda semifasciata (Sea Snake)
表单
lyophilized powder
组成
Protein, ~80% Lowry
储存温度
2-8°C
生化/生理作用
Postsynaptic neurotoxin.
包装
Package size based on protein content
外形
含磷酸钾缓冲盐的冻干粉
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
S Zinn-Justin et al.
Protein engineering, 7(7), 917-923 (1994-07-01)
Structural features associated with the ability of a monoclonal antibody (mAb) to discriminate between protein variants are identified and engineered. The variants are the curaremimetic toxin alpha from Naja nigricollis and erabutoxin a or b from Laticauda semifasciata, which differ
S Sato et al.
The Biochemical journal, 122(4), 453-461 (1971-05-01)
1. Erabutoxin b was reduced, S-carboxymethylated and hydrolysed with trypsin. Seven tryptic fragments were isolated by column chromatography and paper electrophoresis. Some of the fragments were further hydrolysed with alpha-chymotrypsin, pepsin, Nagarse, Proctase A or Proctase B. The amino acid
D Gillet et al.
Protein engineering, 5(3), 273-278 (1992-04-01)
We have inserted a disulfide-containing snake neurotoxin into the N-terminal end of Escherichia coli alkaline phosphatase, between residues +6 and +7 of the mature enzyme. For this purpose, we have designed a cloning and expression vector which allows insertion of
A Spura et al.
The Journal of biological chemistry, 275(29), 22452-22460 (2000-05-03)
Although previous results indicate that alpha-subunit residues Trp(187), Val(188), Phe(189), Tyr(190), and Pro(194) of the mouse nicotinic acetylcholine receptor are solvent-accessible and are in a position to contribute to the alpha-bungarotoxin (alpha-Bgtx) binding site (Spura, A., Russin, T. S., Freedman
C Fromen-Romano et al.
Protein engineering, 10(10), 1213-1220 (1998-03-06)
Curaremimetic toxins are typical non-enzymatic toxins that bind to their target [the nicotinic acetylcholine receptor (AChR)] through multiple residues. Nevertheless, we show that the concomitant substitutions of only three of the ten functionally important residues of such a toxin sufficed
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