N(), N() bis-(Carboxymethyl)-L-Lysine

Disodium salt monohydrate

Product Number C 9609
Storage at Room Temperature

Preparation Instructions
Soluble in water to 10 mg/ml. Prepare solutions fresh.

Synonyms: AB-NTA; Aminobutyl-NTA; N-(5-Amino-1carboxypentyl)iminodiacetic acid

Precautions and Disclaimer

This product is for laboratory use only. Please
consult the Material Data Safety Sheet for information
regarding hazards and safe handling practices

Product Description
Molecular Formula: C10H16 N2O6Na2 H2O
Molecular Weight: 324.2
Aminobutyl-NTA was originally used for the purification
of recombinant proteins. The applications for this
compound have been expanded to include protein
immobilization. Proteins can be bound to a solid
surface such a glass or gold (AU) electrodes via
Aminobutyl-NTA chelated to nickel ions or by utilizing
1,2
column chromatography.
The Aminobutyl-NTA is adsorbed onto a given surface.
2+
The NTA group forms a tetravalent chelate with Ni
creating a self-assembled monolayer (SAM) that will
then be capable of binding histidine containing proteins.
Bound proteins can be typically desorbed by treatment
with imidazole; however, researchers have reported
successful desorption using EDTA and a competitive
chelator. Aminobutyl-NTA has also been used in
surface plasmon resonance (SPR) studies. A histidine
derivative of a viral polymerase subunit has been
successfully reversibly immobilized to Aminobutyl-NTA
2+
(Ni chelated) covalently bound to carboxymethylated
dextran surface of a flow cell in the SPR sensor.
Proteins isolated using the NTA-SAM method retained
a greater degree of binding capacity compared to
2,3
proteins immobilized on dextran by covalent coupling.

Storage/Stability
Store at room temperature. Protect from light and
moisture. The compound is susceptible to degradation
by light and moisture and has been packaged under
argon.
References
1. Hochuli, E., et al., New metal chelate adsorbent
selective for proteins and peptides containing
neighbouring histidine residues. J. Chromatogr.
411, 177-184 (1987).
2. Sigal, G.B., et al., A self-assembled monolayer for
the binding and study of histidine-tagged proteins
by surface prasmon resonance. Anal. Chem, 68,
490-497 (1996)
3. Gershon, P.D. and Khilko, S., Stable chelating
linkage for reversible immobilization of
oligohistidine tagged proteins in the BIAcore
surface plasmon resonance detector. J. Immunol.
Meth., 183, 65-76 (1995).

LCM/ARO 1/02

Purity: >97% by HPLC

Sigma brand products are sold through Sigma-Aldrich, Inc.

Sigma-Aldrich, Inc. warrants that its products conform to the information contained in this and other Sigma-Aldrich publications. Purchaser
must determine the suitability of the product(s) for their particular use. Additional terms and conditions may apply. Please see reverse side of
the invoice or packing slip.