Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HSP-010

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.
DnaK (amino acids1-384) 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 purified to apparent homogeneity by using conventional column chromatography techniques.
Recombinant Dnak Substrate Binding Domain produced in E.Coli is a single,non-glycosylated polypeptide chain conjtaining 384 amino acids and having a molecular mass of 48.1 kDa.

Physical Appearance:

Sterile filtered clorless solution.

Formulation:

The protein (1mg/ml) contains 25mM Tris-HCl, pH7.5, 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.

Sequence:

MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVTNPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVLKKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIIN EPTAAALAYGLDKGTGNRTI AVYDLGGGTF DISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYLVEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKV TRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKEPRKDVNPDEA VAIGAAVQGG VLTG.

Usage:

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

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