AAT Bioquest

NTA maleimide

Product Image
Product Image
Gallery Image 1
Ordering information
Catalog Number
Unit Size
Add to cart
Additional ordering information
InternationalSee distributors
Bulk requestInquire
Custom sizeInquire
ShippingStandard overnight for United States, inquire for international
Request quotation
Physical properties
Molecular weight413.38
Storage, safety and handling
Certificate of OriginDownload PDF
H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
Alternative formats
NTA succinimidyl ester


Molecular weight
NTA maleimide is used to attach NTA groups to a biological substrate or a surface that has thiol groups. Through the NTA moiety attached to the substrate or surface, genetically expressed proteins bearing the hexahistidine extension (HIS Tag) can be detected or immobilized via Ni-mediated His-Tag method. The NTA maleimide is an excellent building block for developing the HIS tag detection probes.


Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of NTA maleimide to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM241.908 µL1.21 mL2.419 mL12.095 mL24.191 mL
5 mM48.382 µL241.908 µL483.816 µL2.419 mL4.838 mL
10 mM24.191 µL120.954 µL241.908 µL1.21 mL2.419 mL

Molarity calculator

Enter any two values (mass, volume, concentration) to calculate the third.

Mass (Calculate)Molecular weightVolume (Calculate)Concentration (Calculate)Moles



View all 2 citations: Citation Explorer
Transition Metal Ion FRET-Based Probe to Study Cu (II)-Mediated Amyloid-$\beta$ Ligand Binding
Authors: Wu, Ri and Svingou, Despoina and Metternich, Jonas B and Benzenberg, Lukas R and Zenobi, Renato
Journal: Journal of the American Chemical Society (2024)
Protein Engineering of Microbial Ferritins
Authors: Gyamfi, Hawa
Journal: (2019)


View all 14 references: Citation Explorer
Purification of a Recombinant Polyhistidine-Tagged Glucosyltransferase Using Immobilized Metal-Affinity Chromatography (IMAC)
Authors: de Costa F, Barber CJ, Pujara PT, Reed DW, Covello PS.
Journal: Methods Mol Biol (2016): 91
Cellular uptake and in vivo distribution of polyhistidine peptides
Authors: Iwasaki T, Tokuda Y, Kotake A, Okada H, Takeda S, Kawano T, Nakayama Y.
Journal: J Control Release (2015): 115
Characterization of soluble RNA-dependent RNA polymerase from dengue virus serotype 2: The polyhistidine tag compromises the polymerase activity
Authors: Kamkaew M, Chimnaronk S.
Journal: Protein Expr Purif (2015): 43
New shuttle vector-based expression system to generate polyhistidine-tagged fusion proteins in Staphylococcus aureus and Escherichia coli
Authors: Schwendener S, Perreten V.
Journal: Appl Environ Microbiol (2015): 3243
Effects of the polyhistidine tag on kinetics and other properties of trehalose synthase from Deinococcus geothermalis
Authors: Panek A, Pietrow O, Filipkowski P, Synowiecki J.
Journal: Acta Biochim Pol (2013): 163
Electrodeposition of polymer nanodots with controlled density and their reversible functionalization by polyhistidine-tag proteins
Authors: Bazin D, Chevalier S, Saadaoui H, Santarelli X, Larpent C, Feracci H, Faure C.
Journal: Langmuir (2012): 13968
Surface-attached polyhistidine-tag proteins characterized by FTIR difference spectroscopy
Authors: Pinkerneil P, Guldenhaupt J, Gerwert K, Kotting C.
Journal: Chemphyschem (2012): 2649
A pair of ligation-independent Escherichia coli expression vectors for rapid addition of a polyhistidine affinity tag to the N- or C-termini of recombinant proteins
Authors: Dan H, Balach and ran A, Lin M.
Journal: J Biomol Tech (2009): 241
A facile method for reversibly linking a recombinant protein to DNA
Authors: Goodman RP, Erben CM, Malo J, Ho WM, McKee ML, Kapanidis AN, Turberfield AJ.
Journal: Chembiochem (2009): 1551
RNA aptamer binding to polyhistidine-tag
Authors: Tsuji S, Tanaka T, Hirabayashi N, Kato S, Akitomi J, Egashira H, Waga I, Ohtsu T.
Journal: Biochem Biophys Res Commun (2009): 227