Name: Recombinant E.Coli Dnak ATPase Binding Domain
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- Overview
  - Recombinant DnaK Substrate Binding Domain produced in E. Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids and having a molecular mass of 48.1 kDa. DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP-70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. DnaK(amino acids1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was purified to apparent homogeneity by using conventional column chromatography techniques.
    
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- Properties
  - Protein Name
    
    HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.
    
    Source
    
    E. coli
    
    Type
    
    Recombinant Proteins
    
    Purification
    
    Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
    
    Formulation
    
    The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10% Glycerol.
    
    Storage
    
    Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
    
    * For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Recombinant E.Coli Dnak ATPase Binding Domain

Recombinant E.Coli Dnak ATPase Binding Domain

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