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| Product Name | DnaK, NT, aa1-384, ATPase Binding Domain, Recombinant, E. coli |
| Description | Purity ≥ 95% by SDS PAGE; Purified by using conventional chromatography techniques. 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 1-384) 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. Molecular Weight: 41.6kD (384 amino acids) Sequence: MGKIIGIDLG/ TTNSCVAIMD/ GTTPRVLENA/ EGDRTTPSII/ AYTQDGETLV/ GQPAKRQAVT/ NPQNTLFAIK/ RLIGRRFQDE/ EVQRDVSIMP/ FKIIAADNGD/ AWVEVKGQKM/ APPQISAEVL/ KKMKKTAEDY/ LGEPVTEAVI/ TVPAYFNDAQ/ RQATKDAGRI/ AGLEVKRIIN/ EPTAAALAYG/ LDKGTGNRTI/ AVYDLGGGTF/ DISIIEIDEV/ DGEKTFEVLA/ TNGDTHL |
| Size | 500ug |
| Concentration | n/a |
| Applications | n/a |
| Other Names | n/a |
| Gene, Accession, CAS # | n/a |
| Catalog # | D4015-18 |
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| Order / More Info | DnaK, NT, aa1-384, ATPase Binding Domain, Recombinant, E. coli from UNITED STATES BIOLOGICAL |
| Product Specific References | n/a |
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