Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • SequenceM-DVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKT AIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK
    • Amino acids385 to 638

Specifications

Our Abpromise guarantee covers the use of ab51119 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

  • Purity> 95 % SDS-PAGE.
    This recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.
  • FormLiquid
  • 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.

    Preservative: None
    Constituents: 10% Glycerol, 5mM DTT, 25mM Tris HCl, 100mM Sodium chloride, pH 7.5

General Info

  • Alternative names
    • Chaperone Hsp70
    • Chaperone protein dnaK
    • Co chaperone with DnaJ
    • dnaK
    • Heat shock 70 kDa protein
    • HSP70
    see all
  • RelevanceDnaK 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 localizationCytoplasm. Cell inner membrane; Peripheral membrane protein.

Recombinant DnaK protein images

  • ab51119 in 14% SDS-PAGE

References for Recombinant DnaK protein (ab51119)

ab51119 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"