Description

  • Product name

    Recombinant Chlamydia Trachomatis HSP70 protein
  • Biological activity

    This protein is immunoreactive with sera of Chlamydia Trachomatis infected individuals.
  • Purity

    > 95 % SDS-PAGE.
    This protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC. It was purified by proprietary chromatographic techniques.
  • Expression system

    Escherichia coli
  • Protein length

    Protein fragment
  • Animal free

    No
  • Nature

    Recombinant
    • Sequence

      PAPRGHPQI EVTFDIDANG ILHVSAKDAA SGREQKIRIE ASS
    • Amino acids

      462 to 503

Specifications

Our Abpromise guarantee covers the use of ab67711 in the following tested applications.

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

  • Applications

    SDS-PAGE

    ELISA

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 8.00
    Constituents: 48% Urea, 0.79% Tris HCl, 0.348% Sodium chloride

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names

    • 75 kDa membrane protein
    • Chaperone protein
    • Dnak
    • Heat shock protein 70
  • Relevance

    HSP70 is the eukaryotic analogue of prokaryotic DnaK. Heat-shock proteins applies to a group of proteins that assist in the assembly, folding, and translocation of other proteins. In addition, they protect the cell against heat injury or other forms of stress. All cells, prokaryotic and eukaryotic, are able to respond to different cellular stresses by synthesizing these proteins. Heat shock proteins are highly conserved, ubiquitously distributed, and involved in important aspects of viral and bacterial infections, autoimmune diseases, and in cancer immunity. Two families of molecular chaperones have been identified. The members of the Hsp70 family (DnaK/DnaJ/GrpE) bind to the growing polypeptide chain and prevent its premature folding. The chaperonin family (GroEL and GroES) assists in correct folding when the complete polypeptide chain is formed and is transported into the cytosol or mitochondria. All the major heat shock proteins help to suppress irreversible unfolding reactions. These protein folding 'assistants' may have important functions in amyloid diseases where incorrectly folded proteins accumulate as folded aggregates.

References

ab67711 has not yet been referenced specifically in any publications.

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