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| Product Name | DnaK, NT, aa1-384, ATPase Binding Domain, Recombinant |
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| Description | Purity ≥ 95% as determined by RP-HPLC, anion-exchange FPLC and/or reducing and non-reducing SDS-PAGE Silver Stained gel. 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 |
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| Size | 10ug, 50ug |
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| Concentration | n/a |
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| Applications | n/a |
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| Other Names | n/a |
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| Gene, Accession, CAS # | n/a |
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| Catalog # | D4015-18A |
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| Price | |
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| Order / More Info | DnaK, NT, aa1-384, ATPase Binding Domain, Recombinant from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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