HIS Lite™ iFluor® 647 Tris NTA Chelator

HIS Lite™ iFluor® 647 Tris NTA Chelator is a red fluorescent probe for selective, noncovalent labeling and detection of polyhistidine-tagged proteins in cells, solutions, and on solid surfaces.

Selective Labeling: Enables site-specific labeling of polyhistidine-tagged proteins with added Ni²⁺ ions.
Spectral Properties: Excitation at 655 nm and emission at 670 nm.
Stable Binding: Multivalent tris-NTA interactions provide greater binding stability than mono-NTA.
Multicolor Compatibility: Supports multicolor protein analysis when combined with OG488-tris-NTA.
Applications: Suitable for protein detection, interaction studies, and live-cell surface labeling.

iFluor® 647 Tris-NTA Chelator is used as a sensitive red fluorescent probe for detecting polyhistidine-labeled proteins in combination with the addition of a heavy metal ion such as Ni2+ in cells, solution and solid surfaces.

Datasheet

SDS

COA

Catalog	Size	Price	Quantity
12658	100 ug	Price

Overview

iFluor® 647 Tris-NTA Chelator is used as a sensitive red fluorescent probe for detecting polyhistidine-labeled proteins in combination with the addition of a heavy metal ion such as Ni2+ in cells, solution and solid surfaces. Fluorescent tris-NTA compounds provide an efficient method for site-specific and stable noncovalent fluorescence labeling of polyhistidine-tagged proteins. In contrast to the transient binding of conventional mono-NTA, the multivalent interaction of tris-NTA conjugated fluorophores form a much more stable complex with polyhistidine-tagged proteins. The high selectivity of tris-NTA compounds toward cumulated histidines enables the selective labeling of proteins in cell lysates and on the surface of live cells. Fluorescent tris-NTA conjugates can be applied for the analysis of a ternary protein complex in solution and on surfaces. In combination with OG488-tris-NTA compound iFluor® 647 Tris-NTA can be used for multicolor analysis of polyhistidine-tagged proteins. AAT Bioquest also offers HIS Lite™ iFluor® 647 Tris NTA-Ni Complex that can be directly used for the specific and highly sensitive detection of His-tagged fusion proteins without the addition of a heavy metal ion. The transition metal ions (e.g., Ni ion)-mediated complexation of polyhistidine-labeled proteins with fluorescent tris-NTA conjugates provides a sensitive reporter for detecting and monitoring protein-protein interactions in real time.

Calculators

Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of HIS Lite™ iFluor® 647 Tris NTA Chelator to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

	0.1 mg	0.5 mg	1 mg	5 mg	10 mg
1 mM	49.845 µL	249.224 µL	498.447 µL	2.492 mL	4.984 mL
5 mM	9.969 µL	49.845 µL	99.689 µL	498.447 µL	996.895 µL
10 mM	4.984 µL	24.922 µL	49.845 µL	249.224 µL	498.447 µL

Molarity calculator

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

Mass (Calculate)		Molecular weight		Volume (Calculate)		Concentration (Calculate)		Moles
mg	÷	2006.23 g/mol	=	mL	x	mM	=	mmol

References

View all 50 references: Citation Explorer

Correction: Diamond nanowires modified with poly[3-(pyrrolyl)carboxylic acid] for the immobilization of histidine-tagged peptides.

Authors:

Subramanian, Palaniappan and Mazurenko, Ievgen and Zaitsev, Vladimir and Coffinier, Yannick and Boukherroub, Rabah and Szunerits, Sabine

Journal:

The Analyst (2024)

Analysis of histidine-tagged recombinant proteins from nickel and copper coated surfaces by direct electrospray ionization and desorption electrospray ionization mass spectrometry.

Authors:

Javanshad, Roshan and Taylor, Christopher James and Delavari, Niusha and Barkman, Todd J and Stull, Frederick and Venter, Andre R

Journal:

Rapid communications in mass spectrometry : RCM (2023): e9516

Chromatographic purification of histidine-tagged proteins using zirconia particles modified with phosphate groups.

Authors:

Kanoh, Shogo and Shiraki, Kentaro and Wada, Momoyo and Tanaka, Takeshi and Kitamura, Masahiro and Kato, Katsuya and Hirano, Atsushi

Journal:

Journal of chromatography. A (2023): 464112

Synthesis of micron-sized magnetic agarose beads chelated with nickel ions towards the affinity-based separation of histidine-tagged/rich proteins.

Authors:

Zhao, Ya-Qi and Yu, Shi-Song and Chen, Meng-Ying and Wang, Yuan and Shi, Yu-Jun and Wang, Xin-Yu and Zhao, Jia-Meng and Dong, Lin-Yi and Zhao, Zhen-Yu and Wang, Xian-Hua

Journal:

Journal of chromatography. A (2023): 464365

Cation affinity purification of histidine-tagged proteins.

Authors:

Sun, Hongxu and Wang, Hongrui and Chen, Qiwei and Dong, Wenge and Gao, Chao and Song, Haiyan and Peng, Hui and Li, Ren and Wu, Hao and Hou, Liangyu and Chang, Yanhong and Luo, Hui

Journal:

Applied microbiology and biotechnology (2023): 2639-2651

Physical properties

Molecular weight	2006.23
Solvent	DMSO

Spectral properties

Correction factor (260 nm)	0.03
Correction factor (280 nm)	0.03
Correction factor (656 nm)	0.0793
Extinction coefficient (cm ^-1 M ^-1)	220000 ¹
Excitation (nm)	655
Emission (nm)	670
Quantum yield	0.25 ¹

Usage and storage

Intended use	Research Use Only (RUO)
Storage	Freeze (< -15 °C); Minimize light exposure

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Page updated on October 26, 2026