Recombinant E. coli GrpE protein (ab168056)

Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Escherichia coli
    • Sequence
      MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQVDPRDEKVANLEAQ LAEAQTRERDGILRVKAEMENLRRRTELDIEKAHKFALEKFINELLPVID SLDRALEVADKANPDMSAMVEGIELTLKSMLDVVRKFGVEVIAETNVPLD PNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA
    • Molecular weight
      22 kDa
    • Amino acids
      1 to 197

Specifications

Our Abpromise guarantee covers the use of ab168056 in the following tested applications.

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

  • Applications

    Western blot

  • Purity
    >= 99 % .

  • Form
    Liquid
  • Additional notes
    For maximum product recovery after thawing, centrifuge the vial before opening the cap.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 7.00
    Constituents: 0.075% Potassium chloride, 0.72% HEPES, 5% Glycerol

General Info

  • Alternative names
    • Heat shock protein B25.3
    • HSP 70 cofactor
    • HSP24
  • Relevance
    GrpE is a so-called co-chaperone because it is known to assist the DnaK (Hsp70) protein to effectively carry out DnaK-dependent chaperone activity (i.e. protein folding, protein transport, disaggregation of heat inactivated proteins, activation of mutant protein). GrpE acts as a nucleotide exchange factor for DnaK, the main Hsp70 protein in bacteria, accelerating ADP/ATP exchange by several orders of magnitude. Unfolded proteins bind initially to dnaJ; upon interaction with the dnaJ-bound protein, dnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from dnaK; ATP binding to dnaK triggers the release of the substrate protein, thus completing the reaction cycle. GrpE may also function as a thermosensor. GrpE is a homodimer, each subunit containing three structural domains: a N-terminal unordered segment, two long coils and a C-terminal globular domain formed by a four-helix bundle, and a beta-subdomain.
  • Cellular localization
    Cytoplasmic

References

ab168056 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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