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Nitrilotriacetic Acid

Nitrilotriacetic Acid (NTA) is a versatile chemical compound with a wide range of applications in research and industry.
It is a chelating agent, capable of forming stable complexes with various metal ions, making it useful in metal ion extraction, water treatment, and analytical chemistry.
NTA is also employed in biochemical and molecular biology applications, such as protein purification and metal ion sensing.
This MeSH term provides a concise overview of the key properties and uses of Nitrilotriacetic Acid, helping researchers quickly understand its importance and potential within their studies.
PubCompare.ai's AI-driven insights can optimize your NTA research protocols, enabling you to quickly locate the best procedures from literature, pre-prints, and patents, and leverage AI-powered comparisons to identify the most effective products and methods.
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Most cited protocols related to «Nitrilotriacetic Acid»

1
Purification of SOSIP.664-His and gp41ECTO-His Proteins
Cited 24 times
Supernatants from cells transiently expressing SOSIP.664-His gp140 or gp41ECTO-His proteins were diluted 1∶2 in TBS/10% FCS and incubated for 2 h with Ni2+-nitrilotriacetic acid (Ni-NTA) coated Hissorb 96-well plates (Qiagen, Venlo, The Netherlands) [32] (link), [33] (link), [72] (link), [73] (link). The subsequent procedures were exactly as described above for the D7324-capture ELISA.
Sanders R.W., Derking R., Cupo A., Julien J.P., Yasmeen A., de Val N., Kim H.J., Blattner C., de la Peña A.T., Korzun J., Golabek M., de los Reyes K., Ketas T.J., van Gils M.J., King C.R., Wilson I.A., Ward A.B., Klasse P.J, & Moore J.P. (2013). A Next-Generation Cleaved, Soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, Expresses Multiple Epitopes for Broadly Neutralizing but Not Non-Neutralizing Antibodies. PLoS Pathogens, 9(9), e1003618.
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Publication 2013
Cells Enzyme-Linked Immunosorbent Assay GP 140 Nitrilotriacetic Acid Proteins
2
Validating Antibodies for Sur1 and Trpm4
Cited 14 times
The anti-Sur1 and anti-Trpm4 antibodies used in this study are listed in Table 2. Anti-Myc and anti-HSC70 antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA). Anti-FLAG antibody and anti-calmodulin antibody were purchased from Cell Signaling Technology (Beverly, MA). Two different sources of both anti-Sur1 and anti-Trpm4 antibodies were developed for this study (Table 2). To construct a bacterial expression vector encoding the intracellular nucleotide-binding domain 1 of Sur1 fused with hexahistidine, the corresponding region of the rat Sur1 cDNA sequence (amino acids 598–965 of NP_037171) was cloned into pQE30 (Qiagen, Gaithersburg, MD). The recombinant protein was purified by using a Ni+-nitrilotriacetic acid-agarose column and used to raise antibodies in rabbit and in goat, which was performed by a commercial service (Covance, Princeton, NJ). Using the same method, anti-Trpm4 antibodies targeting the N-terminal intracellular domain of mouse Trpm4, corresponding to amino acids 1–612 (NP_780339), were developed in rabbit and in chicken.
The specificity of the antibodies described above was validated using lysates from the appropriate Sur1 or Trpm4 expression systems and spinal cord tissues from wild-type, Trpm4−/−, and Abcc8−/− mice. Anti-Sur1-b antibody and anti-Trpm4-b antibody were used to immunoisolate Sur1 and Trpm4, respectively, from the various lysates. Subsequently, in one experiment, immunoblots of the immunoisolated proteins were performed using anti-Sur1-a antibody and anti-Trpm4-a antibody, respectively (see Fig. 9). In a parallel experiment, electrophoresis gels of the immunoisolated proteins were developed with Coomassie Blue stain, the protein bands at the appropriate molecular masses were isolated, and peptide fragments were analyzed by mass spectrometry (Taplin Mass Spectrometry Facility, Harvard Medical School, Boston, MA), which confirmed the identity of Sur1 and Trpm4.
Woo S.K., Kwon M.S., Ivanov A., Gerzanich V, & Simard J.M. (2012). The Sulfonylurea Receptor 1 (Sur1)-Transient Receptor Potential Melastatin 4 (Trpm4) Channel. The Journal of Biological Chemistry, 288(5), 3655-3667.
Publication 2012
Amino Acids Anti-Antibodies Antibodies Antibodies, Anti-Idiotypic Antibody Specificity Bacteria Calmodulin Chickens Cloning Vectors Coomassie blue DNA, Complementary Electrophoresis Gels Goat His-His-His-His-His-His Histocompatibility Testing Immunoblotting Immunoglobulins Mass Spectrometry Mus Nitrilotriacetic Acid Nucleotides Peptide Fragments Proteins Protoplasm Rabbits Recombinant Proteins Sepharose Spinal Cord Stains
3
Iron Saturation of Lactoferrin
Cited 7 times
Lactoferrin supplied by the manufacturers was used without further purification. For apolactoferrin, preparation containing 50 mg/mL protein was dissolved in water and dialyzed extensively against 100 mM citrate buffer for 24 h, followed by dialysis against distilled water for 24 h [37 (link)]. Temperature (4 and 20 °C) and buffer pH (2.0–5.0) were modified in order to monitor their impact on iron desaturation. Iron saturation was calculated based on the A280/A466 ratio according to the calibration curve presented in “Results and discussion.” We define the iron saturation level of lactoferrin as the percentage of iron-binding sites occupied by ferric ions assuming that 2 mol of iron(III) ions is bound per 1 mol of protein. Thus, the given values refer to the percentage of differic lactoferrin. For some of these samples, the ICP-MS and ELISA tests were carried out and were used to prepare a calibration curve.
Hololactoferrin was prepared by the reaction of 50 mg/mL lactoferrin solution in 50 mM Tris–HCl, 150 mM NaCl (pH 7.4) with ferric nitrate salt in the presence of nitrilotriacetic acid (NTA) as well as different concentrations of sodium bicarbonate [24 (link)]. After incubation, excess iron was removed by dialysis against the same buffer solution without ferric salts for 24 h and against water for another 24 h. Various incubation times, temperatures, as well as ratios of Lf/Fe/NTA were employed to examine their effect on iron saturation efficiency; detailed conditions are depicted in the captions of figures.
Majka G., Śpiewak K., Kurpiewska K., Heczko P., Stochel G., Strus M, & Brindell M. (2013). A high-throughput method for the quantification of iron saturation in lactoferrin preparations. Analytical and Bioanalytical Chemistry, 405(15), 5191-5200.
Publication 2013
apolactoferrin Bicarbonate, Sodium Binding Sites Buffers Citrates Dialysis Enzyme-Linked Immunosorbent Assay ferric nitrate Ions Iron Iron Overload Lactoferrin Mol-Iron Nitrilotriacetic Acid PER1 protein, human Proteins Salts Sodium Chloride Tromethamine
4
Optimizing Affinity-Based Protein Labeling
Cited 7 times
Constructs were transformed into the BL12-derived Rosetta2 BL21(DE3) line (EMD Millipore). 50mL starter cultures were grown overnight in LB-Ampicillin. These were added to 450mL of LB and grown to an OD600 of 0.8–1 before induction with 0.5mM Isopropyl β-D-1-thiogalactopyranoside (IPTG). Cultures were allowed to express for 24hrs at 25°C. Cells were then harvested by centrifugation (6000 RPM, 15min) and resuspended in 10mL of lysis buffer (50mM NaH2PO4, 300mM NaCl, 1mg/mL Lysozyme, 1 EDTA-free cOmplete Mini protease inhibitor tablet (Roche), pH 7.5). Lysates were incubated at room temperature for 30min under gentle agitation before freezing overnight at −80°C. Samples were then thawed and incubated for 30min with DNAse I (Roche) under gentle agitation. Lysates were then sonicated and separated by centrifugation (10,000 rpm, 30min).
For optimization experiments, 8mL of clarified lysate for each condition was incubated for 1 hr with 0.6mL Talon resin (Clontech, equilibrated in lysis buffer). The lysate and beads were then added to a column and beads were washed with 6mL STEPL buffer (20mM Tris-base, 50mM NaCl, pH 7.5). Washed beads were resuspended in a total of 1.2mL of STEPL buffer containing the indicated amounts of CaCl2 and triglycine (Sigma-Aldrich) and aliquoted into three 1.5mL microcentrifuge tubes. Samples were shaken at 1,000 rpm, the indicated temperature, and protected from light. At each timepoint, samples were spun down at 3,000 rpm for 5min. Absorbance spectra were taken of the supernatants from 400 – 600nm using a Cary 100 Bio UV-Visible Spectrophotometer (Varian) and the sample was returned to shaking. At the end of the timecourse, beads were washed three times with 1mL STEPL buffer and incubated for 30 min in 100mM EDTA. Stripped beads were spun down as before and the absorbance spectra were taken of the supernatants from 400 – 600nm.
For bioconjugation experiments, 8mL of clarified lysate was incubated for 1hr with 0.5mL Talon resin (equilibrated in lysis buffer). The lysate and beads were added to a column and beads were washed with 5mL STEPL buffer. 400μL of STEPL buffer containing 150μM synthetic peptide (Table 2) or 5mM triglycine (for labeled and unlabeled preparations, respectively) and 100μM CaCl2 was flowed over the beads until it replaced the wash buffer. Columns were protected from light and reacted for 6hrs at 37°C. 1mL of STEPL buffer was added to the column and the flow through collected. To remove unreacted peptide, flowthrough was dialyzed three times against 4L of STEPL buffer at 4°C while protected from light (Slide-A-Lyzer2 cassettes, 3.5K cutoff, Thermo Scientific).
Warden-Rothman R., Caturegli I., Popik V, & Tsourkas A. (2013). Sortase-Tag Expressed Protein Ligation (STEPL): combining protein purification and site-specific bioconjugation into a single step. Analytical chemistry, 85(22), 10.1021/ac402871k.
Publication 2013
Ampicillin Buffers Cells Centrifugation Claw Deoxyribonuclease I Edetic Acid Light Muramidase Nitrilotriacetic Acid Peptides Protease Inhibitors Resins, Plant Sodium Chloride Tablet Tromethamine
5
Producing Folded Recombinant Proteins
Cited 6 times
All proteins were produced by transient transfection using human embryonic kidney HEK293E cells as described (11 (link)) to ensure posttranslational modifications such as disulfide bonds and glycans were added. Proteins were purified using their His6 tag using a bespoke supernatant loading rig and 96-well Ni2+-nitrilotriacetic acid filter plates (15 (link)). Heat-labile immunoreactivity to demonstrate folding was confirmed by heat-denaturing the proteins for 10 min at 90 °C before capture on a streptavidin-coated plate via their biotin tag and determination of immunoreactivity by ELISA as described (19 (link)).
Sun Y., Vandenbriele C., Kauskot A., Verhamme P., Hoylaerts M.F, & Wright G.J. (2015). A Human Platelet Receptor Protein Microarray Identifies the High Affinity Immunoglobulin E Receptor Subunit α (FcεR1α) as an Activating Platelet Endothelium Aggregation Receptor 1 (PEAR1) Ligand. Molecular & Cellular Proteomics : MCP, 14(5), 1265-1274.
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Publication 2015
Biotin Cells Disulfides Embryo Enzyme-Linked Immunosorbent Assay his6 tag Homo sapiens Kidney Nitrilotriacetic Acid Polysaccharides Post-Translational Protein Processing Proteins Streptavidin Transfection Transients

Most recents protocols related to «Nitrilotriacetic Acid»

1
Recombinant TcbZIP60 Protein Production and DNA-Binding Assay
The ORF without the TcbZIP60 terminator codon was used to generate the pET6×HN-C vector protein, which was fused into the N-terminal frame of 6×His, and the vector pET6×HN-C-TcbZIP60 was then transformed into E. coli strain Rosetta (DE3). For the induced recombinant protein, 0.5 mM IPTG was used, and the cultures were incubated at 18°C for 16 h. Then, Ni2+–nitrilotriacetic acid was used to purify the recombinant proteins. For the electrophoretic mobility shift assay (EMSA), the promoter fragments of TcCHS and TcAOC containing E-box or G-box cis-regulatory elements labeled with fluorescein amidite (FAM) as probes, the same but unlabeled DNA fragments, and cis-element mutant DNA fragments were used as competitors in the assay. After performing the EMSA assays, FAM-labeled DNA was detected from the chemiluminescent signal.
Xu Z., Zeng T., Li J., Zhou L., Li J., Luo J., Zheng R., Wang Y., Hu H, & Wang C. (2023). TcbZIP60 positively regulates pyrethrins biosynthesis in Tanacetum cinerariifolium. Frontiers in Plant Science, 14, 1133912.
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Publication 2023
Biological Assay Cloning Vectors Codon, Terminator Electrophoresis Electrophoretic Mobility Shift Assay Escherichia coli Fluorescein HN Protein Isopropyl Thiogalactoside Nitrilotriacetic Acid Reading Frames Recombinant Proteins Regulatory Sequences, Nucleic Acid Strains
2
Expression and Purification of DENV-2 RdRP Domain
The pET28a+-DEN2-Pol plasmid containing the NS5 RNA-dependent RNA polymerase (RdRP) domain (sequence from residue 272 to residue 900 of DENV-2 NGC) (GenBank accession number KM204118.1) was obtained by PCR amplification using primers D2_NS5(262-900) FOR and REV (see Table S2B in the supplemental material) and cloning into pET28a+ plasmid (Merck) at BamHI/SalI sites. The fusion construct was verified by sequencing. To obtain the 6×His-NS5(272-900) protein, a procedure described in reference 52 (link) was followed with modifications. pET28a+-DEN2-Pol plasmid was transformed into Escherichia coli strain BL21(DE3)pLysS (StrataGene). Three liters of cells were grown in Luria Bertani (LB) medium containing 100 μg/mL ampicillin until the optical density at 600 nm (OD600) was 0.5. Then, cells were cooled at 16°C, and protein expression was induced by the addition of 0.5 mM isopropyl-β-d-thiogalactopyranoside (IPTG, ICN) overnight (O/N) at 16°C. Cells were pelleted, resuspended in resuspension buffer (20 mM Tris-HCl pH 8.0, 500 mM NaCl, 10 mM β-mercaptoethanol, 10% glycerol) added with 1 mg/mL lysozyme and complete protease inhibitors (Roche Molecular Biochemicals), and then lysed by two freeze/thaw cycles and by sonication. The lysate was centrifuged at 16,000 × g for 30 min, applied to a 0.5 mL-Ni-nitrilotriacetic acid (Ni-NTA) agarose resin column (Qiagen) that had been equilibrated in resuspension buffer. The column was washed with resuspension buffer added with 15 mM imidazole, and then protein was eluted with 20 mM Tris-HCl pH 8.0, 500 mM NaCl, 10 mM β-mercaptoethanol, and 125 mM imidazole.
Celegato M., Sturlese M., Vasconcelos Costa V., Trevisan M., Lallo Dias A.S., Souza Passos I.B., Queiroz-Junior C.M., Messa L., Favaro A., Moro S., Teixeira M.M., Loregian A, & Mercorelli B. (2023). Small-Molecule Inhibitor of Flaviviral NS3-NS5 Interaction with Broad-Spectrum Activity and Efficacy In Vivo. mBio, 14(1), e03097-22.
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Publication 2023
2-Mercaptoethanol Ampicillin Buffers Cells Escherichia coli Freezing Glycerin imidazole Muramidase Nitrilotriacetic Acid Oligonucleotide Primers Plasmids Protease Inhibitors Proteins Resins, Plant RNA-Directed RNA Polymerase Sepharose Sodium Chloride Strains Tromethamine Vision
3
Genetic Manipulation of E. coli Strains
RAW264.2 cells were purchased from ATCC. All plasmids and bacterial strains used in this study are shown in Tables 2to4. E. coli K-12 BW25113 (wild type [WT]) and single gene-deleted mutant strains (ΔompA: opmA::kan for JW0940-KC, ΔfepA: fepA::kan for JW5086-KC, ΔcirA: cirA::kan for JW2142-KC, ΔdegP: degP::kan for JW0157-KC, and ΔompC: ompC::kan for JW2203-KC) were provided by National BioResource Project (NIG, Japan). The competent cell BL21(DE3) strain and DH5α strain were purchased from TaKaRa (Shiga, Japan). LB broth was purchased from Sigma/Merck (Tokyo, Japan). The plasmid pET22b(+) was purchased from Novagen/Merck (Tokyo, Japan). pTV118N vector was gifted by Ishijima (Kyoto Prefectural University). Ex Taq, Mighty TA-cloning kit containing pMD T vector, DNA ligation kit Mighty Mix, in-fusion HD cloning kit, isopropyl β-d-1-thiogalactopyranoside (IPTG), and TB Green premix Ex Taq II were purchased from TaKaRa (Shiga, Japan). Ni-nitrilotriacetic acid (NTA) agarose was purchased from Qiagen (Hilden, Germany). cOmplete Mini protease inhibitor was purchased from Roche/Nippon Gene (Tokyo, Japan). Anti-OmpC antibody was purchased from MyBioSource (Vancouver, Canada). Isogen II was purchased from Nippon Gene (Tokyo, Japan). Can Get Signal and ReverTra Ace quantitative PCR (qPCR) reverse transcription (RT) kit were purchased from Toyobo (Osaka, Japan).
Imamiya R., Shinohara A., Yakura D., Yamaguchi T., Ueda K., Oguro A., Minamiyama Y., Ichikawa H., Horiguchi Y, & Osada-Oka M. (2023). Escherichia coli-Derived Outer Membrane Vesicles Relay Inflammatory Responses to Macrophage-Derived Exosomes. mBio, 14(1), e03051-22.
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Publication 2023
Antibodies, Anti-Idiotypic Bacteria Cells Cloning Vectors Escherichia coli Genes Ligation Nitrilotriacetic Acid OmpC protein Plasmids Protease Inhibitors Reverse Transcription Sepharose Strains
4
Recombinant Protein Expression and Purification from E. coli
The full-length gene for TafE was amplified from A. baumannii genomic DNA using the appropriate primers (Table S1), and the PCR product was digested with BamHI/SalI and inserted into pETSumo (Thermo Fisher) to produce sumo-His6-tagged fusion proteins. The gene coding for TaeI, an immunity protein that antagonizes the activity of TafE, was cloned into pGEX-6P-1 to express GST-TaeI. When needed, substitution mutations were introduced using the QuikChange kit (Agilent) and fusion PCR. E. coli strain BL21(DE3) was used as the host for expression and purification of recombinant proteins.
Amounts of 20 mL of overnight cultures were transferred to 500 mL LB broth supplemented with 100 μg/mL of ampicillin or 30 μg/mL of kanamycin. Cultures were grown to an optical density at 600 nm (OD600) of 0.6 in a shaker (200 rpm) at 37°C. The expression of the fusion protein was induced at 16°C by adding 0.2 mM IPTG (isopropyl-β-d-thiogalactopyranoside) for 18 h. The harvested cell pellets were resuspended in lysis buffer (50 mM NaH2PO4, 300 mM NaCl, 10 mM imidazole) and were lysed by using a cell homogenizer (JN-mini; JNBio, Guangzhou, China). The supernatant of lysed cells was mixed with Ni2+-nitrilotriacetic acid (NTA) or glutathione beads at 4°C for 1 h. Ni2+-NTA resin was extensively washed with washing buffer (50 mM NaH2PO4, 300 mM NaCl, 20 mM imidazole) following protein binding. Glutathione beads were washed with 20× the column volume of phosphate-buffered saline (PBS). Bound His6-sumo-tagged proteins were eluted five times with the same buffer containing 250 mM imidazole. GST-tagged proteins were eluted with 10 mM glutathione. His6-Hcp and His6-TafE fusion proteins were similarly purified with Ni2+-NTA beads. The purity of the proteins was evaluated by SDS-PAGE followed by Coomassie brilliant blue staining, and only proteins purer than 95% were used in subsequent experiments. Proteins were dialyzed in a storage buffer (50 mM Tris·HCl, 150 mM NaCl, 10% glycerol) at 4°C. Protein concentration was determined by the Bradford method.
Luo J., Chu X., Jie J., Sun Y., Guan Q., Li D., Luo Z.Q, & Song L. (2023). Acinetobacter baumannii Kills Fungi via a Type VI DNase Effector. mBio, 14(1), e03420-22.
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Publication 2023
Ampicillin brilliant blue G Buffers Escherichia coli Genes Genome Glutathione Glycerin imidazole Isopropyl Thiogalactoside Kanamycin Missense Mutation Nitrilotriacetic Acid Oligonucleotide Primers Pellets, Drug Phosphates Proteins Recombinant Proteins Resins, Plant Response, Immune Saline Solution SDS-PAGE Small Ubiquitin-Related Modifier Proteins Sodium Chloride Strains Tromethamine Vision
5
Recombinant Expression of Mycobacterium tuberculosis Antigens
DNA sequences encoding ESAT6, CFP10 (fragment 1–41 and fragment 45–80), TB9.8, TB10.4, MPT64 (25–228), MPT83 (58–220), and MPT51 (33–299) were amplified from Mtb genomic DNA (H37Rv strain) (a kind gift of Robert Husson, Boston Children’s Hospital) by conventional PCR and cloned into the pET21b vector for recombinant expression in E. coli as described previously (32 (link)). For rhavi fusion proteins, seven constructs, each of which contained up to three Mtb antigens, were prepared by inserting Mtb DNA sequence(s) at the 3′ end of the rhavi gene (see Table S1 in the supplemental material) and then cloned into the pET21b vector. Lipidated rhavi was constructed by adding a lipidation box at the 5′ end of the rhavi gene as described previously (32 (link)). All Mtb proteins (nonfusion) and lipidated rhavi were expressed in E. coli BL21(DE3) cells, and all rhavi-Mtb fusion antigens were expressed in T7 shuffle express cells. The recombinant His-tagged proteins were then purified using nitrilotriacetic acid (NTA) resin followed by size exclusion chromatography as described previously (32 (link)). The purified proteins were then concentrated, filtered via 0.2-μm filters, aliquoted, and stored at −80°C until use.
O’Hara J.M., Wakabayashi S., Siddiqi N., Cheung E., Babunovic G.H., Thompson C.M., Lu Y.J., Rubin E.J., Malley R, & Zhang F. (2023). A MAPS Vaccine Induces Multipronged Systemic and Tissue-Resident Cellular Responses and Protects Mice against Mycobacterium tuberculosis. mBio, 14(1), e03611-22.
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Publication 2023
Antigens Cells Cloning Vectors DNA Sequence Escherichia coli Genes Genes, vif Genome Molecular Sieve Chromatography Nitrilotriacetic Acid Proteins Resins, Plant

Top products related to «Nitrilotriacetic Acid»

1
Ni nitrilotriacetic acid nta agarose by Qiagen
Sourced in Germany, United States
Ni-nitrilotriacetic acid (NTA) agarose is a chromatography resin used for the purification of histidine-tagged recombinant proteins. The agarose beads are functionalized with the chelating agent NTA, which binds to nickel ions. This allows for the efficient capture and purification of histidine-tagged proteins from complex samples.
2
Superdex 200 column by GE Healthcare
Sourced in United States, Sweden, United Kingdom, Germany, Japan
The Superdex 200 column is a size-exclusion chromatography media used for the separation and purification of proteins, peptides, and other biomolecules. It is designed to provide efficient separation and high resolution across a wide range of molecular weights. The column is suitable for a variety of applications, including protein analysis, desalting, and buffer exchange.
3
Ni nitrilotriacetic acid agarose by Qiagen
Sourced in Germany
Ni–nitrilotriacetic acid agarose is a resin used for the purification of recombinant proteins with a histidine-tag. It utilizes the specific interaction between nickel ions and the histidine residues to capture and isolate the target protein.
4
Nitrilotriacetic acid by Merck Group
Sourced in United States
Nitrilotriacetic acid is a chemical compound commonly used in laboratory equipment. It functions as a chelating agent, capable of forming stable complexes with metal ions. This property makes it useful in various analytical and purification applications within a laboratory setting.
5
Ni nta by Qiagen
Sourced in Germany, United States, United Kingdom
Ni-NTA is a nickel-nitrilotriacetic acid (Ni-NTA) resin used for the purification of histidine-tagged recombinant proteins. It utilizes the high affinity between nickel ions and histidine residues to capture and purify target proteins from complex samples.
6
Ni nta agarose by Qiagen
Sourced in Germany, United States, United Kingdom, Netherlands, China, Switzerland, Italy, Canada, Spain, India
Ni-NTA agarose is a solid-phase affinity chromatography resin designed for the purification of recombinant proteins containing a histidine-tag. It consists of nickel-nitrilotriacetic acid (Ni-NTA) coupled to agarose beads, which selectively bind to the histidine-tagged proteins.
7
Ni nitrilotriacetic acid column by Qiagen
Sourced in Germany
The Ni-nitrilotriacetic acid (Ni-NTA) column is a chromatography column designed for the purification of proteins containing a histidine-tag. The column utilizes the high affinity between the nickel ions on the resin and the histidine residues on the target protein, allowing for efficient capture and separation of the desired protein from a complex mixture.
8
Ni nitrilotriacetic acid nta column by Qiagen
Sourced in Germany
The Ni-nitrilotriacetic acid (NTA) column is a type of chromatography column used for the purification of proteins. It contains Ni-NTA, a nickel-charged resin that can bind to proteins containing a histidine tag, allowing for selective capture and separation of the target protein from complex mixtures.
9
Isopropyl β d thiogalactopyranoside iptg by Merck Group
Sourced in United States, China, Germany
Isopropyl-β-D-thiogalactopyranoside (IPTG) is a synthetic chemical compound commonly used in molecular biology and biotechnology laboratories. It is a lactose analog that functions as an inducer, stimulating the expression of genes under the control of the lac operon or other lac-based promoter systems.
10
Ni2 nitrilotriacetic acid resin by Qiagen
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Ni2+-nitrilotriacetic acid resin is a chromatography resin used for the purification of recombinant proteins containing a polyhistidine tag. The resin utilizes the high affinity interaction between the nickel ions (Ni2+) and the polyhistidine tag to selectively bind and capture the target protein from complex mixtures.

More about "Nitrilotriacetic Acid"

Nitrilotriacetic acid (NTA) is a versatile chemical compound with a wide range of applications in research and industry.
As a chelating agent, it can form stable complexes with various metal ions, making it useful in metal ion extraction, water treatment, and analytical chemistry.
NTA is also employed in biochemical and molecular biology applications, such as protein purification and metal ion sensing.
One of the key uses of NTA is in affinity chromatography, where it is commonly used in the form of Ni-nitrilotriacetic acid (Ni-NTA) agarose or Ni-NTA resin.
These materials are used to purify recombinant proteins that contain a histidine (His) tag, which has a high affinity for the Ni2+ ions bound to the NTA.
This Ni-NTA affinity chromatography is a popular technique for the purification of His-tagged proteins, allowing for efficient and selective capture of the target protein from complex mixtures.
Additionally, NTA has been used in conjunction with other chromatographic media, such as Superdex 200 columns, to further refine protein purification protocols.
These combined techniques enable researchers to isolate and purify proteins with a high degree of purity and specificity.
Beyond protein purification, NTA has found applications in metal ion sensing, where it can be used to detect and quantify the presence of various metal ions in samples.
This is particularly useful in environmental and analytical chemistry applications, where the precise measurement of metal ion concentrations is crucial.
PubCompare.ai's AI-driven insights can help optimize your NTA research protocols by quickly locating the best procedures from literature, pre-prints, and patents, and providing AI-powered comparisons to identify the most effective products and methods.
Streamline your Nitrilotriacetic Acid research with PubCompare.ai - your ultimate tool for protocol optimization.