重组E. coli Disulfide-bond isomerase蛋白(ab51284)
Key features and details
- Expression system: Escherichia coli
- Purity: > 95% SDS-PAGE
- Suitable for: SDS-PAGE
描述
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产品名称
重组E. coli Disulfide-bond isomerase蛋白
参阅全部 Disulfide-bond isomerase 蛋白酶 -
纯度
> 95 % SDS-PAGE.
This protein was purified using conventional chromatography techniques. -
表达系统
Escherichia coli -
蛋白长度
Protein fragment -
无动物成分
No -
性质
Recombinant -
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种属
Escherichia coli -
序列
DDAAIQQTLA KMGIKSSDIQ PAPVAGMKTV LTNSGVLYIT DDGKHIIQGP MYDVSGTAPV NVTNKMLLKQ LNALEKEMIV YKAPQEKHVI TVFTDITCGY CHKLHEQMAD YNALGITVRY LAFPRQGLDS DAEKEMKAIW CAKDKNKAFD DVMAGKSVAP ASCDVDIADH YVLGVQLGVS GTPAVVLSNG TLVPGYQPPK EMKEFLDEHQ KMTSGK -
氨基酸
21 to 236
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描述
重组E. coli Disulfide-bond isomerase蛋白
技术指标
Our Abpromise guarantee covers the use of ab51284 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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应用
SDS-PAGE
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形式
Liquid -
Concentration information loading...
制备和贮存
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稳定性和存储
Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
pH: 7.50
Constituents: 0.242% Tris, 0.0584% EDTA
常规信息
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别名
- ECK2888
- JW2861
- Protein disulfide isomerase II
see all -
相关性
Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. Disulphide bond isomerase (DsbC), a member of the thioredoxin superfamily, acts as a disulfide isomerase and converts aberrant disulfide bonds to correct ones. It also acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by a yet uncharacterized protein. -
细胞定位
Periplasm
图片
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SDS-PAGE - Recombinant E. coli Disulfide-bond isomerase protein (ab51284)ab51284 run on a 15% SDS-PAGE gel with molecular weight markers.
实验方案
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
数据表及文件
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Datasheet download
文献 (0)
ab51284 尚未被引用在任何文献中。
