| Product Name | Dnak (C-term;385-638), 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. The protein coding region of the substrate binding domain of DNAK (amino acids 385-638) 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 |
| Synonyms | Dnak (C-term, 385-638), Substrate binding domain, Heat shock protein 70, Heat shock 70 kDa protein, HSP70, Chaperone protein dnaK, Chaperone Hsp 70, Co chaperone with DnaJ, dnaK, Heat shock 70 kDa protein, |
| Host | E. coli |
| Molecular Weight | 92.1kDa (850aa), confirmed by MALDI-TOF. |
| Amino Acid Sequence | MDVKDVLLLD VTPLSLGIET MGGVMTTLIA KNTTIPTKHS QVFSTAEDNQ SAVTIHVLQG ERKRAADNKS LGQFNLDGIN PAPRGMPQIE VTFDIDADGI LHVSAKDKNS GKEQKITIKA SSGLNEDEIQ KMVRDAEANA EADRKFEELV QTRNQGDHLL HSTRKQVEEA GDKLPADDKT AIESALTALE TALKGEDKAA IEAKMQELAQ VSQKLMEIAQ QQHAQQQTAG ADASANNAKD DDVVDAEFEE VKDKK |
| Tag | His-tag |
| Reactivity | E. coli |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris pH 8.0, 20% glycerol Molecular Weight: 92.1kDa (850 a.a) |
| 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 (1984) Proc. Natl. Acad. Sci. 81, 848-852 Zhu 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. The protein coding region of the substrate binding domain of DNAK (amino acids 385-638) 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 |
| Supplier | ARP |
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