Product nameRecombinant DnaK protein
See all DnaK proteins and peptides
Protein lengthProtein fragment
Amino Acid Sequence
SequenceMDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA ADRKFEELV QTRNQGDHLL HST
Amino acids385 to 546
Our Abpromise guarantee covers the use of ab51115 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Purity> 95 % SDS-PAGE.
This recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.
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.
Constituents: 0.0156% Beta mercaptoethanol, 0.395% Tris HCl, 0.0292% EDTA
- Chaperone Hsp70
- Chaperone protein dnaK
- Co chaperone with DnaJ
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.
ab51115 has not yet been referenced specifically in any publications.