Purity: > 95% by SDS - PAGE Format: Liquid. 25 mM Tris-HCl, pH7.5, 100 mM NaCl, 5mM DTT,10%Glycerol . DnaK, originally identified for its DNA replication by bacteriophage lambda 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. DnaK (amino acids 1-638) was amplified by PCR and cloned into an E. coli expression vector. DnaK 1-638 was overexpressed in E. coli and was purified to apparent homogeneity by using conventional column chromatography techniques.
Size
0.5mg, 100ug, 20ug
Concentration
n/a
Applications
SDS-PAGE
Other Names
Chaperone protein dnaK, HSP70, groP, grpF, seg, Heat shock protein 70, Chaperone Hsp70, Co chaperone with DnaJ, dnaK, Heat shock 70 kDa protein,