pet-21d cloning vector (Millipore)
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Millipore
pet-21d cloning vector
Pet 21d Cloning Vector, supplied by Millipore, 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/product/pet-21d+cloning+vector/pet28a/pm39191340-45-29-32
Average 90 stars, based on 1 article reviews
Pet 21d Cloning Vector, supplied by Millipore, 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/product/pet-21d+cloning+vector/pet28a/pm39191340-45-29-32
Average 90 stars, based on 1 article reviews
pet-21d cloning vector - by Bioz Stars,
2026-10
90/100 stars
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Ligation:Article Title: Molecular mechanism of thiocyanate dehydrogenase at atomic resolution. Article Snippet: Some sulfur-oxidizing bacteria playing an important role in global geochemical cycles utilize thiocyanate as the sole source of energy and nitrogen.. In these bacteria the process of thiocyanate into cyanate conversion is mediated by thiocyanate dehydrogenases – a recently discovered family of copper-containing enzymes with the three-copper active site unique among the other copper proteins.. To get a deeper insight into the structure and molecular mechanism of action of thiocyanate dehydrogenases we isolated, purified, and comprehensively characterized an enzyme from the bacterium Pelomicrobium methylotrophicum. Article Title: Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3 Article Snippet: The Article Title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein fromSpiroplasma melliferumKC3 Article Snippet: Following NdeI and EcoRI digestion, the PCR # 2015 International Union of Crystallography All rights reserved product was ligated in frame with the oligonucleotide duplex encoding the N-terminal tag sequence (Table 1) into the pET-21d cloning vector (5443 bp; Novagen, Darmstadt, Germany) digested with the NdeI and EcoRI restriction enzymes. Polymerase Chain Reaction:Article Title: Molecular mechanism of thiocyanate dehydrogenase at atomic resolution. Article Snippet: Some sulfur-oxidizing bacteria playing an important role in global geochemical cycles utilize thiocyanate as the sole source of energy and nitrogen.. In these bacteria the process of thiocyanate into cyanate conversion is mediated by thiocyanate dehydrogenases – a recently discovered family of copper-containing enzymes with the three-copper active site unique among the other copper proteins.. To get a deeper insight into the structure and molecular mechanism of action of thiocyanate dehydrogenases we isolated, purified, and comprehensively characterized an enzyme from the bacterium Pelomicrobium methylotrophicum. Article Title: Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3 Article Snippet: The Article Title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein fromSpiroplasma melliferumKC3 Article Snippet: Following NdeI and EcoRI digestion, the PCR # 2015 International Union of Crystallography All rights reserved product was ligated in frame with the oligonucleotide duplex encoding the N-terminal tag sequence (Table 1) into the pET-21d cloning vector (5443 bp; Novagen, Darmstadt, Germany) digested with the NdeI and EcoRI restriction enzymes. Modification:Article Title: Molecular mechanism of thiocyanate dehydrogenase at atomic resolution. Article Snippet: Some sulfur-oxidizing bacteria playing an important role in global geochemical cycles utilize thiocyanate as the sole source of energy and nitrogen.. In these bacteria the process of thiocyanate into cyanate conversion is mediated by thiocyanate dehydrogenases – a recently discovered family of copper-containing enzymes with the three-copper active site unique among the other copper proteins.. To get a deeper insight into the structure and molecular mechanism of action of thiocyanate dehydrogenases we isolated, purified, and comprehensively characterized an enzyme from the bacterium Pelomicrobium methylotrophicum. Article Title: Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3 Article Snippet: The Article Title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein fromSpiroplasma melliferumKC3 Article Snippet: Following NdeI and EcoRI digestion, the PCR # 2015 International Union of Crystallography All rights reserved product was ligated in frame with the oligonucleotide duplex encoding the N-terminal tag sequence (Table 1) into the pET-21d cloning vector (5443 bp; Novagen, Darmstadt, Germany) digested with the NdeI and EcoRI restriction enzymes. Clone Assay:Article Title: Molecular mechanism of thiocyanate dehydrogenase at atomic resolution. Article Snippet: Some sulfur-oxidizing bacteria playing an important role in global geochemical cycles utilize thiocyanate as the sole source of energy and nitrogen.. In these bacteria the process of thiocyanate into cyanate conversion is mediated by thiocyanate dehydrogenases – a recently discovered family of copper-containing enzymes with the three-copper active site unique among the other copper proteins.. To get a deeper insight into the structure and molecular mechanism of action of thiocyanate dehydrogenases we isolated, purified, and comprehensively characterized an enzyme from the bacterium Pelomicrobium methylotrophicum. Article Title: Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3 Article Snippet: The Article Title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein fromSpiroplasma melliferumKC3 Article Snippet: Following NdeI and EcoRI digestion, the PCR # 2015 International Union of Crystallography All rights reserved product was ligated in frame with the oligonucleotide duplex encoding the N-terminal tag sequence (Table 1) into the pET-21d cloning vector (5443 bp; Novagen, Darmstadt, Germany) digested with the NdeI and EcoRI restriction enzymes. Plasmid Preparation:Article Title: Molecular mechanism of thiocyanate dehydrogenase at atomic resolution. Article Snippet: Some sulfur-oxidizing bacteria playing an important role in global geochemical cycles utilize thiocyanate as the sole source of energy and nitrogen.. In these bacteria the process of thiocyanate into cyanate conversion is mediated by thiocyanate dehydrogenases – a recently discovered family of copper-containing enzymes with the three-copper active site unique among the other copper proteins.. To get a deeper insight into the structure and molecular mechanism of action of thiocyanate dehydrogenases we isolated, purified, and comprehensively characterized an enzyme from the bacterium Pelomicrobium methylotrophicum. Article Title: Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3 Article Snippet: The Article Title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein fromSpiroplasma melliferumKC3 Article Snippet: Following NdeI and EcoRI digestion, the PCR # 2015 International Union of Crystallography All rights reserved product was ligated in frame with the oligonucleotide duplex encoding the N-terminal tag sequence (Table 1) into the pET-21d cloning vector (5443 bp; Novagen, Darmstadt, Germany) digested with the NdeI and EcoRI restriction enzymes. Sequencing:Article Title: Molecular mechanism of thiocyanate dehydrogenase at atomic resolution. Article Snippet: Some sulfur-oxidizing bacteria playing an important role in global geochemical cycles utilize thiocyanate as the sole source of energy and nitrogen.. In these bacteria the process of thiocyanate into cyanate conversion is mediated by thiocyanate dehydrogenases – a recently discovered family of copper-containing enzymes with the three-copper active site unique among the other copper proteins.. To get a deeper insight into the structure and molecular mechanism of action of thiocyanate dehydrogenases we isolated, purified, and comprehensively characterized an enzyme from the bacterium Pelomicrobium methylotrophicum. Article Title: Structural basis of the high thermal stability of the histone-like HU protein from the mollicute Spiroplasma melliferum KC3 Article Snippet: The Article Title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the histone-like HU protein fromSpiroplasma melliferumKC3 Article Snippet: Following NdeI and EcoRI digestion, the PCR # 2015 International Union of Crystallography All rights reserved product was ligated in frame with the oligonucleotide duplex encoding the N-terminal tag sequence (Table 1) into the pET-21d cloning vector (5443 bp; Novagen, Darmstadt, Germany) digested with the NdeI and EcoRI restriction enzymes. |