| Product Name | Dnak (full length; 1-638), Recombinant |
|---|---|
| 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 acids 1-638) was amplified by PCR and cloned into an E. coli expression vector. DnaK 1-638 was overexpressed in E. coli and was purified to apparent homogeneity by using conventional column chromatography techniques. |
| Synonyms | Chaperone protein dnaK, HSP70, groP, grpF, seg, Heat shock protein 70, Chaperone Hsp70, Co chaperone with DnaJ, dnaK, Heat shock 70 kDa protein, |
| Host | E. coli |
| Molecular Weight | 42.9kDa (390aa), confirmed by MALDI-TOF. |
| Amino Acid Sequence | 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 |
| Tag | His-tag |
| Reactivity | E. coli |
| Applications | SDS-PAGE |
| Form | Liquid, in Phosphate buffered saline (pH7.4) , 10% glycerol |
| Concentration | 1 mg/ml (determined by Bradford assay) |
| Purity | > 95% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Bardwell & Craig., et al (1984) Proc. Natl. Acad. Sci. 81, 848-852. Zhu et al.,et al (1996) Science 272, 1606-1614. Naoki tanaka., et al (2002) PNAS 26(99)15398-15403 |
| Background | 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 acids 1-638) was amplified by PCR and cloned into an E. coli expression vector. DnaK 1-638 was overexpressed in E. coli and was purified to apparent homogeneity by using conventional column chromatography techniques. |
| Supplier | ARP |
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