dnaK / Hsp70 (1-384) Escherichia coli Protein

Specifications

Product Data
Species	Escherichia coli
Expression Host	E. coli
Expression cDNA Clone or AA Sequence	Protein Sequence (showhide) MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVT NPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVL KKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG LDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYL VEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKE PRKDVNPDEA VAIGAAVQGG VLTG
Predicted MW	41.6 kDa
Concentration	lot specific
Purity	>95% by SDS-PAGE
Buffer	Presentation State: Purified State: Liquid purified protein Buffer System: 25 mM Tris-HCl, pH 7.5, 100 mM NaCl, 5 mM DTT, 10% Glycerol
Preparation	Liquid purified protein
Protein Description	DnaK (amino acids 1-384) is N-terminal ATPase domain and ATP bound to the ATPase domain induces a conformational change in the substrate binding domain (residues 385-638). The protein coding region of the ATPase domain of DNAK (amino acids 1-384) was amplified by PCR and cloned into an E. coli expression vector. The ATPase domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques.
Storage	Store (in aliquots) at -20°C. Avoid repeated freezing and thawing.
Stability	Shelf life: one year from despatch.
Reference Data
Summary	DnaK, originally identified for its DNA replication by bacteriophage λ 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.

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