Dnak protein (30R-1020)
Purified recombinant E.coli Dnak protein
Overview
Overview
| Synonyms | grpF protein, seg protein, , Heat shock protein 70 protein, HSP70 protein, dnaK protein, Chaperone Hsp70 protein, groP protein, Chaperone protein dnaK protein, Heat shock 70 kDa protein protein, Co chaperone with DnaJ protein |
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| Species | E.coli |
| Protein Type | Recombinant |
| Applications | SDS-PAGE |
Images
Coomassie Blue stained SDS-PAGE of Dnak protein (30R-1020)
Figure annotation denotes ug of protein loaded and % gel used.
Specifications
| Residues | Full length1-638 amino acids: 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 VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPT KHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMP QIEVTFDIDA DGILHVSAKD KNSGKEQKIT IKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGD HLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLME IAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK |
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| Expression System | E.coli |
| Grade & Purity | > 95% pure |
| Molecular Weight | 69 kDa (638aa) |
| Form & Buffer | Supplied as a liquid in 25mM Tris-HCl, pH 7.5, containing 100 mM NaCl, 5mM DTT, and 10% glycerol. |
| Concentration | 1 mg/ml |
Storage & Safety
| Storage | Store at 4 deg C for short term storage (1/2 weeks). Aliquot and store at -20 deg C or - 70 deg C for long term storage. Avoid repeated freeze/thaw cycles. |
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General Information
| Biological Significance | DNAK, originally identified for its DNA replication by bacteriophage in E. coli is the bacterial hsp70 chaperone. The protein coding region of the substrate binding domain of DNAK (amino acids 385-546) was amplified by PCR and cloned into an E. coli expression vector. The substrate binding domain of DNAK was overexpressed in E. coli and the recombinant protein was purified to apparent homogeneity by using conventional column chromatography techniques. Additional amino acid(Met) is attached at N- terminus. |
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