Description
Data Sheet
| Description | 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. |
| Expression host | Escherichia Coli. |
| Formulation | The DnaK protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10% Glycerol. |
| Protein Background | 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. |
| Purity | Greater than 95.0% as determined by SDS-PAGE. |
| Reagent Appearance | Sterile filtered colorless solution. |
| Stability | 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. |
| Synonyms | HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013. |
