Recombinant E.Coli Dnak ATPase Binding Domain
Source : Escherichia Coli. 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.
Product Specifications
Product Name Alternative
HSP-70||HSP70||DnaK||Chaperone protein dnaK||Heat shock protein 70||Heat shock 70 kDa protein||groP||grpF||seg||b0014||JW0013.
Purification
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Components
The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10%Glycerol.
Storage Conditions
Amino Acids
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