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 (aa1-384) 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 (aa1-384) 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.
Source:Recombinant protein corresponding to a single, non-glycosylated polypeptide chain containing 384aa from DnaK Substrate Binding Domain, expressed in E. coli.
Storage and Stability:May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
仕様
Size:20ug
Source Antigen:Recombinant, E. coli
Grade:Highly Purified
Purity:~95% (RP-HPLC, SDS-PAGE)
Form:Supplied as a liquid in 25mM Tris-HCl, pH 7.5, 100mM sodium chloride, 5mM DTT, 10% glycerol.