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Ni nta chromatography resin

Manufactured by Qiagen
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Sourced in Germany, United States

Ni-NTA chromatography resin is a nickel-nitrilotriacetic acid-based solid support used for the purification of proteins with a histidine-tag. The resin binds to the histidine-tagged proteins, allowing their separation from other components in the sample.

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Lab products found in correlation

Phusion dna polymerase, by Thermo Fisher Scientific (1 mentions) Restriction enzyme, by New England Biolabs (1 mentions) Pfu dna polymerase, by Thermo Fisher Scientific (1 mentions)

Spelling variants of this product

Ni-NTA resin (665 citations) Ni-NTA (356 citations) Ni-NTA chromatography (19 citations) Ni-NTA affinity chromatography resin (5 citations) NTA)-resin chromatography (2 citations) NTA) resins (2 citations) Ni-NTA agarose resin affinity chromatography (2 citations)

2 protocols using ni nta chromatography resin

1

Extraction and Purification of Mtb DNA

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The genomic DNA of Mtb H37Rv was purchased from ATCC. Phusion DNA polymerase and the restriction enzymes used for cloning were purchased from Thermo Scientific (Massachusetts, USA) and New England Biolabs. The Ni–NTA chromatography resin was obtained from Qiagen (Hilden, Germany).
Asthana P., Singh D., Pedersen J.S., Hynönen M.J., Sulu R., Murthy A.V., Laitaoja M., Jänis J., Riley L.W, & Venkatesan R. (2021). Structural insights into the substrate-binding proteins Mce1A and Mce4A from Mycobacterium tuberculosis. IUCrJ, 8(Pt 5), 757-774.
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2

Purification of Pfu DNA Polymerase

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Pfu DNA polymerase was purchased from Thermo Scientific (Massachusetts, USA) and Ni-NTA chromatography resin was obtained from Qiagen (Hilden, Germany). Enzymatic digestion was performed using restriction enzymes from New England BioLabs. Chemicals from Bio-Rad (California, USA) were used for SDS-PAGE. All other chemicals of analytical grade were obtained from Biomol (Hamburg, Germany), Merck (Darmstadt, Germany), Sigma, or Serva (Heidelberg, Germany).
Singh D., Singh D, & Grüber G. (2018). Crystallographic and enzymatic insights into the mechanisms of Mg-ADP inhibition in the A1 complex of the A1AO ATP synthase. Journal of structural biology, 201(1).
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