||The substrate binding domain of recombinant DNAK was overexpressed in E. coli and purified to apparent homogeneity by using conventional column chromatography techniques (255 aa, 27.7 kDa).
||DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial hsp70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins. The protein coding region of the substrate binding domain of DNAK (amino acids 385-638) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid(Met) is attached at N- terminus.
||Liquid. In 25 mM Tris-HCl buffer (pH 7.5) containing 100 mM NaCl, 5 mM DTT, 10% glycerol.
||> 95% by SDS – PAGE.
||1 mg/ml (determined by Bradford assay).
||MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKT AIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK
||Can be stored at +4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.