{"product_id":"recombinant-e-coli-dnak-atpase-binding-domain-bhp11003439","title":"Recombinant E.Coli Dnak ATPase Binding Domain","description":"\u003cp\u003e\u003cstrong\u003eRecombinant E.Coli Dnak ATPase Binding Domain\u003c\/strong\u003e is supplied as a recombinant protein for in vitro research use.\u003c\/p\u003e\n\u003ch3\u003eBackground\u003c\/h3\u003e\n\u003cp\u003eDnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP-70 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.\u003c\/p\u003e\n\u003ch3\u003eProduct format\u003c\/h3\u003e\n\u003cp\u003eProvided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.\u003c\/p\u003e","brand":"ProSpec-Tany TechnoGene Ltd","offers":[{"title":"10 ug","offer_id":53038112571757,"sku":"hsp-010-10UG","price":60.0,"currency_code":"USD","in_stock":true},{"title":"50 ug","offer_id":53038406959469,"sku":"hsp-010-50UG","price":145.0,"currency_code":"USD","in_stock":true},{"title":"1 mg","offer_id":53038406992237,"sku":"hsp-010-1MG","price":1800.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0949\/7424\/7277\/files\/Prospecbio-dnak-atpase-bd-HSP-010.png?v=1782158262","url":"https:\/\/www.ebiohippo.com\/products\/recombinant-e-coli-dnak-atpase-binding-domain-bhp11003439","provider":"BioHippo","version":"1.0","type":"link"}