Dnak protein (30R-1019)
Purified recombinant E.coli Dnak protein
|Synonyms||Heat shock protein 70 protein, Chaperone Hsp70 protein, dnaK protein, seg protein, grpF protein, Heat shock 70 kDa protein protein, , Chaperone protein dnaK protein, Co chaperone with DnaJ protein, groP protein, HSP70 protein|
Coomassie Blue stained SDS-PAGE of Dnak protein (30R-1019)
Figure annotation denotes ug of protein loaded and % gel used.
|Residues||Substrate binding domain 385-546 amino acids: MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HST|
|Purity||> 95% pure|
|Molecular Weight||17.7 kDa (163aa)|
|Form & Buffer||Supplied as a liquid in 25mM Tris-HCl, pH7.5, containing 2 mM beta-mercaptoethanol, and 1 mM EDTA.|
Storage & Safety
|Storage||Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles.|
|Biological Significance||DNAK, originally identified for its DNA replication by bacteriophage in E. coli is the bacterial hsp70 chaperone. The protein coding region of the substrate binding domain of DNAK (amino acids 385-546) 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.|
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