Examples of 'ni-nta' in a sentence

Meaning of "ni-nta"

Ni-nta stands for amino-terminal (Ni) and affinity (nta) as in Ni-NTA agarose used in protein purification techniques

How to use "ni-nta" in a sentence

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ni-nta
The obtained Ni-NTA was packed in the column.
The original construct still bound to Ni-NTA plates.
The resulting Ni-NTA was packed into a column.
The secreted proteins were purified using Ni-NTA agarose beads.
Equilibrate Ni-NTA resin column overnight with sonication buffer.
Added an appropriate amount of Ni-NTA resin to a tube.
In addition to the Ni-NTA column, an affinity resin was prepared with immobilized FSH.
Protein was purified by Ni-NTA chromatography.
The harvested supernatant was flowed through a column packed with a Ni-NTA resin.
Immobilisation of luciferase on Ni-NTA coated beads ; activity measured by luminometry.
In addition, protein can be purified using immunoaffinity columns or Ni-NTA columns.
Binding of bacteriophage particles to Ni-NTA plates was determined as briefly outlined.
Alternatively, the protein can be successfully refolded while immobilized on the Ni-NTA column.
Affinity purification was performed by Ni-NTA chromatography following the supplier 's recommendations.
The protein was purified using sequential chromatography on Ni-NTA and HiTrapQ / HiTrapS.

See also

Lysate was added to equilibrated Ni-NTA agarose beads for affinity purification on a column.
The fusión polypeptide contained six histidine residues to enable purification using Ni-NTA agarose.
The lysate was mixed with Ni-NTA and loaded into a column.
The Btk protein is then purified to homogeneity using Ni-NTA column.
After enrichment over the Ni-NTA column, the proteins were purified by gel filtration.
His-tag protein was purified by affinity chromatography to a Ni-NTA Superflow column.
Following Ni-NTA chromatography, the protein was immediately subjected to further purification through CM silica resin.
The subsequent affinity purification was completed by Ni-NTA chromatography following the supplier 's recommendations.
The protein peaks from the Q-sepharose column were pooled and loaded onto a Ni-NTA agarose column.
Ni-NTA agarose resin from Qiagen was used according to the manufacturer 's instructions.
These results demonstrate that purification by affinity chromatography on a Ni-NTA column yielded a homogenous protein fraction.
Acid pH protonates the histidine, causing dissociation from the Ni-NTA.
The receptor protein was then purified vía Ni-NTA and HPC4 affinity purifications.
Fig 3C shows that the fusion protein of lane B can be further purified using Ni-NTA resin.
The supernatant was deposited on a Ni-NTA agarose column ( QIAgen ).
After expression and osmotic shock, the resulting extract was purified on 1 ml of Ni-NTA resin.
The conditions for purification on Ni-NTA gel are described in table 7.
The supernatant was applied to an HBSS-equilibrated Ni-NTA column.
Small scale purification over Ni-NTA columns was then performed, for each clone.
Cleaved MBP was separated from the 8xHis tagged nanobodies by an additional Ni-NTA purification step.
Ni-NTA elutions are shown on the gels.
The proteins were induced with IPTG and purified on Ni-NTA agarose using standard methods.
Five mls of Ni-NTA resin was added into the medium and kept stirring at 4 °C overnight.
The protein peaks from the Q-sepharose column are pooled and loaded onto a Ni-NTA agarose column.
For histidine tagged proteins, Ni-NTA agarose ( Qiagen ) is used for protein purification.
Purification was performed with the Qiagen protocol using Qiagen Ni-NTA and columns.
This recombinant protein was purified using Ni-NTA agarose ( Qiagen ) having affinity for 6 x histidine.
Supernatants, containing the LbpB protein, were combined and added to Ni-NTA agarose.
The supernatant was recovered and applied to Ni-NTA ( manufactured by Invitrogen Corporation ).
Approximately 0.6 mg of pentameric complex per liter of media could be purified by Ni-NTA purification.
Incubate the supernatant with 5 mL of Ni-NTA metal affinity resin ( Qiagen ) for three hours.
Purification of the enzymes was performed using his-tag and Ni-NTA columns.
This suspension was bound to Ni-NTA agarose ( QIAGEN ) that was pre-equilibrated in the same buffer.
Following centrifugation, the cleared supernatant is chromatographed using a Ni-NTA Superflow column Qiagen Catalogue No.
Ni-NTA agarose beads + scFv were then washed 4X as previously described.

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