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Merck KGaA nco i/ xho i sites of pet32b(+) plasmid
Nco I/ Xho I Sites Of Pet32b(+) Plasmid, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/nco i/ xho i sites of pet32b(+) plasmid/product/Merck KGaA
Average 90 stars, based on 1 article reviews
nco i/ xho i sites of pet32b(+) plasmid - by Bioz Stars, 2026-02
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Scheme of the recombinant proteins as produced upon cloning in pET32b (Trx-TB10.4, Trx-Ag85B and Trx- full ) or pColdI (His- full 1 and His- full 2) vectors. Trx: thioredoxin (116 amino acids, aa). The arrow indicates the EK cleavage site. The entire amino acid sequences are reported in the Additional file : Figure S2.

Journal: Microbial Cell Factories

Article Title: Optimizing Escherichia coli as a protein expression platform to produce Mycobacterium tuberculosis immunogenic proteins

doi: 10.1186/1475-2859-12-115

Figure Lengend Snippet: Scheme of the recombinant proteins as produced upon cloning in pET32b (Trx-TB10.4, Trx-Ag85B and Trx- full ) or pColdI (His- full 1 and His- full 2) vectors. Trx: thioredoxin (116 amino acids, aa). The arrow indicates the EK cleavage site. The entire amino acid sequences are reported in the Additional file : Figure S2.

Article Snippet: To prepare His- full 1 form, the full cDNA was extracted from pET32b plasmid using Kpn I and Eco RI restriction sites and cloned into pColdI plasmid (TaKaRa Bio Inc., Otsu, Japan).

Techniques: Recombinant, Produced, Clone Assay

Time course of pH (○, solid line), dO 2 (♦, solid line) and OD 600nm (●, dashed line) in 3 L batch cultivation trials of recombinant E. coli BL21(DE3) cells producing M. tuberculosis immunogenic proteins. A) E. coli BL21(DE3) cells containing pET32b-Trx-TB10.4 plasmid and grown in LB medium. B) E. coli BL21(DE3) cells containing pET32b-Trx-Ag85B plasmid and grown in SB medium. C) E. coli BL21(DE3) cells containing pColdI-His- full 2 and growing in SB/NaCl medium. Temperature (■, dashed line) was kept constant at 37°C before IPTG addition and then reduced to 18°C for Trx-TB10.4 and Trx-Ag85B production, and at 15°C for His- full 2 production, until harvest. The induction of protein expression was done at OD 600nm = 0.8 with 0.1 mM IPTG for Trx-TB10.4, at OD 600nm = 2 with 0.1 mM IPTG for Trx-Ag85B, and at OD 600nm = 2 with 0.1 mM IPTG for His- full 2. Biomass (wet weight) collected at the harvest time was 8.5 g/L for Trx-TB10.4, 19.5 g/L for Trx-Ag85B and 6.5 g/L for His- full 2.

Journal: Microbial Cell Factories

Article Title: Optimizing Escherichia coli as a protein expression platform to produce Mycobacterium tuberculosis immunogenic proteins

doi: 10.1186/1475-2859-12-115

Figure Lengend Snippet: Time course of pH (○, solid line), dO 2 (♦, solid line) and OD 600nm (●, dashed line) in 3 L batch cultivation trials of recombinant E. coli BL21(DE3) cells producing M. tuberculosis immunogenic proteins. A) E. coli BL21(DE3) cells containing pET32b-Trx-TB10.4 plasmid and grown in LB medium. B) E. coli BL21(DE3) cells containing pET32b-Trx-Ag85B plasmid and grown in SB medium. C) E. coli BL21(DE3) cells containing pColdI-His- full 2 and growing in SB/NaCl medium. Temperature (■, dashed line) was kept constant at 37°C before IPTG addition and then reduced to 18°C for Trx-TB10.4 and Trx-Ag85B production, and at 15°C for His- full 2 production, until harvest. The induction of protein expression was done at OD 600nm = 0.8 with 0.1 mM IPTG for Trx-TB10.4, at OD 600nm = 2 with 0.1 mM IPTG for Trx-Ag85B, and at OD 600nm = 2 with 0.1 mM IPTG for His- full 2. Biomass (wet weight) collected at the harvest time was 8.5 g/L for Trx-TB10.4, 19.5 g/L for Trx-Ag85B and 6.5 g/L for His- full 2.

Article Snippet: To prepare His- full 1 form, the full cDNA was extracted from pET32b plasmid using Kpn I and Eco RI restriction sites and cloned into pColdI plasmid (TaKaRa Bio Inc., Otsu, Japan).

Techniques: Recombinant, Plasmid Preparation, Expressing

Chemico-physical parameters of the recombinant proteins as produced upon cloning in  pET32b  or pColdI

Journal: Microbial Cell Factories

Article Title: Optimizing Escherichia coli as a protein expression platform to produce Mycobacterium tuberculosis immunogenic proteins

doi: 10.1186/1475-2859-12-115

Figure Lengend Snippet: Chemico-physical parameters of the recombinant proteins as produced upon cloning in pET32b or pColdI

Article Snippet: To prepare His- full 1 form, the full cDNA was extracted from pET32b plasmid using Kpn I and Eco RI restriction sites and cloned into pColdI plasmid (TaKaRa Bio Inc., Otsu, Japan).

Techniques: Recombinant, Produced, Clone Assay