Recombinant E. coli Disulphide oxidoreductase protein (ab73431)

概述

描述

  • 性质Recombinant
  • 来源Escherichia coli
  • 氨基酸序列
    • 种属Escherichia coli
    • 序列The sequence of the first five N-terminal amino acids was determined and was found to be Met-Lys-Lys-Ala-Trp.
    • 分子量23 kDa
    • 额外的序列信息Disulfide Oxidoreductase produced in E.Coli is a periplasmic protein isolated from E. coli, containing 208 amino acids having a molecular mass of 23,149 Dalton.

技术指标

Our Abpromise guarantee covers the use of ab73431 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • 应用

    Western blot

  • 纯度> 95 % SDS-PAGE.
    Purity is greater than 95.0% as determined by RP-HPLC and SDS-PAGE and was purified by proprietary chromatographic techniques.
  • 形式Lyophilised
  • 补充说明For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
  • Concentration information loading...

制备和贮存

  • 稳定性和存储

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 50mM Sodium phosphate, 100mM Sodium chloride

  • 复溶Reconstitute in sterile 18MOhm/cm H2O to not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.dsbA

常规信息

  • 别名
    • dsbA
    • periplasmic protein disulfide isomerase I
    • Thiol disulfide interchange protein dsbA
  • 相关性Disulphide oxidoreductase (DsbA) is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. It is a member of the thioredoxin superfamily. DsbA introduces disulfide bonds directly into substrate proteins by donating the disulfide bond in its active site Cys30-Pro31-His32-Cys33 to a pair of cysteines in substrate proteins. DsbA is reoxidized by dsbB. It is required for pilus biogenesis.
  • 细胞定位Periplasm

Recombinant E. coli Disulphide oxidoreductase protein (ab73431)参考文献

ab73431 has not yet been referenced specifically in any publications.

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