Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HSP-006

Description :

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.
Recombinant Dnak produced in E.Coli is a single,non-glycosylated polypeptide chain conjtaining 638 amino acids and having a molecular mass of 69 kDa.

Physical Appearance:

Sterile filtered clorless solution.

Formulation:

The protein (1mg/ml) contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.

Stability:

Store at 4蚓 if entire vial will be used within 2-4 weeks. Store, frozen at -20蚓 for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by reducing and non-reducing SDS-PAGE Coomassie.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.

Latest Publications:

1. The DnaK chaperone machinery converts the native FlhDC hetero-tetramer into a functional transcriptional regulator of flagellar regulon expression in Salmonella.
Mol Microbiol 2006 Feb;59(4):1327-40
2. Ionic contacts at DnaK substrate binding domain involved in allosteric regulation of lid dynamics.
J Biol Chem 2006 Jan 16;
3. Modulation of costimulatory molecules CD80/CD86 on B cells and macrophages by stress proteins GroEL, GroES and DnaK.
Int J Immunopathol Pharmacol 2005 Oct-Dec;18(4):637-44
4. The allosteric transition in DnaK probed by infrared difference spectroscopy. Concerted ATP-induced rearrangement of the substrate binding domain.
Protein Sci 2006 Feb;15(2):223-33
5. Organization of heat shock dnaK and groE operons of the nosocomial pathogen Enterococcus faecium.
Res Microbiol 2005 Aug 8;
6. Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli.
Arch Biochem Biophys 2005 Dec 1;444(1):61-5