(HSP-70, HSP70, DnaK, Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.)
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. Dnak(residues 508-638) of the substrate binding domain is a-helical and appears to act as a lid covering the substrate binding cleft. DnaK(amino acid 508-638) was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid (Met) is attached at N- terminus.
Recombinant DnaK Substrate Binding domain produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 14.6 kDa.
Purity: Greater than 95.0% as determined by(a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Source: Escherichia Coli.
Physical Appearance: Sterile filtered colorless solution.
Formulation: The protein contains 25mM Tris-HCl, pH7.5, 100mM NaCl, 5mM DTT and 10%Glycerol.
Amino acid sequence:
MNEDEIQKMV RDAEANAEAD RKFEELVQTR NQGDHLLHST RKQVEEAGDK LPADDKTAIESALTALETAL KGEDKAAIEA KMQELAQVSQ KLMEIAQQQH AQQQTAGADASANNAKDDDVVDAEFEEVKDKK.
Storage:
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.
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