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Tris-NTA Amine


  • A complex of three Ni-NTA groups ensures high-affinity binding of His-tags
  • Binding affinity is approximately four orders of magnitude higher than monovalent metal ion chelators
  • Protein binding is stoichiometric


  • Reversible labeling of proteins or cell surfaces
  • Detection and analysis of target molecules
  • Immobilization of proteins, lipids and cells on surfaces
  • Purification and sample preparation of proteins
  • Coupling with microscopic or spectroscopic probes

Purchase Tris-NTA Amine

Availability: In stock Bulk requests please inquire at

Catalog # Size Package Content Price* Qty
BR1001101 100 µg 100 µl Tris-NTA Amine
BR1001102 1 mg 1 ml Tris-NTA Amine

*Does not include applicable tax, shipping & handling, or other charges.


biotechrabbit™ Tris-NTA Amine for high-affinity His-tag binding.

His-tags are one of the most commonly used tags for protein expression analysis. Conventional metal ion chelators, such as nitrilotriacetic acid (NTA) and iminodiacetic acid (IDA), bind His-tags with low affinities in the range of 10 µM. The biotechrabbit Tris-NTA complexes three NTA groups that together bind a 6×His-tag with an affinity that is four orders of magnitude higher (1 nM) than is possible with conventional chelators (10 µM). The binding of His-tags is stoichiometric and single-molecule detection is possible. Binding is reversible: bound His-tags can be released with imidazole or ethylenediaminetetraacetic acid (EDTA).

biotechrabbit™ Tris-NTA is available with a free amine group or conjugated to biotin. It can be used in a large range of applications, including protein detection and labeling, coupling proteins, lipids or cells to surfaces, protein purification and reversible protein modification.

The use of this product for research purposes is covered by a license from QIAGEN Group. No rights to use this product to perform or offer diagnostic, companion diagnostic, commercial testing or other commercial services for money or money’s worth are granted by the supply of this product expressly, by implication or by estoppel.
Should you wish to use this product for any other purpose not covered by this license, please contact QIAGEN Corporate Business Development at




Tris-NTA Amine

Tris-NTA Amine (1 mg/ml) in PBS



4°C (until expiry date – see product label)



Tris-NTA (trifluoracetic acid salt)


24 months


store at 4°C


HPLC, Mass spec


free base: 862778-60-7


free base: C43H68N8O22


free base: 1049.04




>95% (HPLC)


1 mg/ml PBS solution



Quality Control

Identity of the substance was determined by MS analysis. The identity was consistent with the reference substance.


The purity of Tris-NTA Amine was determined by HPLC. Purity was >95%.

Tris-NTA is not pre-loaded with a metal ion.

Please, choose the metal ion (i.e. Nickel or Cobalt) and loading method that fit best to your application.

As an example, please, refer to Figure 5 in "Reichel et al., Anal Chem., 2007, 79, 8590–600":
Ni2+ loading by injection of 10 mM NiCl2 when using Tris-NTA with a biosensor surface. 

Application examples

High-Affinity Adaptors for Switchable Recognition of Histidine-Tagged Proteins.
Lata et al., J. Am. Chem. Soc., 2005, 127, 10205–10215

Specific and Stable Fluorescence Labeling of Histidine-Tagged Proteins for Dissecting Multi-Protein Complex Formation.
Lata et. al., J. Am. Chem. Soc., 2006, 128, 2365–2372

Noncovalent, Site-Specific Biotinylation ofHistidine-Tagged Proteins.
Reichel et al., Anal Chem., 2007, 79, 8590–600

Identifying Modulators of Protein-Protein Interactions Using Photonic Crystal Biosensors.
Heeres et al., J Am Chem Soc. 2009, 131: 18202–18203

Tris-Nitrilotriacetic Acids of Sub-nanomolar Affinity Toward Hexahistidine Tagged Molecules.
Huang et al., Bioconjug Chem., 2009, 20: 1667–1672

Four-color single-molecule fluorescence with noncovalent dye labeling to monitor dynamic multimolecular complexes.
DeRocco et al., BioTechniques 2010, 49: 807-816

Co- and distinct existence of Tris-NTA and biotin functionalities on individual and adjacent micropatterned surfaces generated by photo-destruction.
Biswas et al., Soft Matter, 2014, 10, 2341–2345

High-affinity gold nanoparticle pin to label and localize histidine tagged protein in macromolecular assemblies.
Anthony et al., Structure, 2014, 22: 628–635


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