Description

  • Product name

    Recombinant DnaK protein
    See all DnaK proteins and peptides
  • Purity

    > 85 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Sequence

      MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK
    • Amino acids

      1 to 638

Specifications

Our Abpromise guarantee covers the use of ab51121 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

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C. Avoid freeze / thaw cycle.

    pH: 7.50
    Constituents: 0.077% DTT, 0.395% Tris HCl, 10% Glycerol, 0.58% Sodium chloride

General Info

  • Alternative names

    • Chaperone Hsp70
    • Chaperone protein dnaK
    • Co chaperone with DnaJ
    • dnaK
    • Heat shock 70 kDa protein
    • HSP70
    see all
  • Relevance

    DnaK is the prokaryotic analogue of eukaryotic Hsp70. 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.
  • Cellular localization

    Cytoplasm. Cell inner membrane; Peripheral membrane protein.

Images

  • 15% SDS-PAGE

References

ab51121 has not yet been referenced specifically in any publications.

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There are currently no Customer reviews or Questions for ab51121.
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