HIS Lite™ OG488-Tris NTA-Ni Complex

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 enable 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. 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. This OG488-tris-NTA compound has been reported to be an sensitive fluorescent probe for detecting polyhistidine-labeled proteins in cells, solution and solid surfaces.

Protocol

SDS

COA

Catalog	Size	Price	Quantity
12615	100 ug	Price

Calculators

Common stock solution preparation

Table 1. Volume of Water needed to reconstitute specific mass of HIS Lite™ OG488-Tris NTA-Ni Complex 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	54.405 µL	272.023 µL	544.046 µL	2.72 mL	5.44 mL
5 mM	10.881 µL	54.405 µL	108.809 µL	544.046 µL	1.088 mL
10 mM	5.44 µL	27.202 µL	54.405 µL	272.023 µL	544.046 µL

Molarity calculator

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

Mass (Calculate)		Molecular weight		Volume (Calculate)		Concentration (Calculate)		Moles
mg	÷	1838.08 g/mol	=	mL	x	mM	=	mmol

Citations

View all 25 citations: Citation Explorer

Escherichia coli tRNA 2-selenouridine synthase SelU selects its prenyl substrate to accomplish its enzymatic function

Authors:

Szczupak, Patrycja and Radzikowska-Cieciura, Ewa and Kulik, Katarzyna and Madaj, Rafa{\l} and Sierant, Ma{\l}gorzata and Krakowiak, Agnieszka and Nawrot, Barbara

Journal:

Bioorganic Chemistry (2022): 105739

Selective binding, magnetic separation and purification of histidine-tagged protein using biopolymer magnetic core-shell nanoparticles

Authors:

Zhou, Y., Yan, D., Yuan, S., Chen, Y., Fletcher, E. E., Shi, H., Han, B.

Journal:

Protein Expr Purif (2018): 5-11

Quantification of Histidine-Rich Protein 3 of Plasmodium falciparum

Authors:

Palani, B.

Journal:

Monoclon Antib Immunodiagn Immunother (2018): 87-90

A novel reverse micellar purification strategy for histidine tagged human interferon gamma (hIFN-gamma) protein from Pichia pastoris

Authors:

Prabhu, A. A., Purkayastha, A., M and al, B., Kumar, J. P., M and al, B. B., Veeranki, V. D.

Journal:

Int J Biol Macromol (2018): 2512-2524

Label-Free Direct Electrical Detection of a Histidine-Rich Protein with Sub-Femtomolar Sensitivity using an Organic Field-Effect Transistor

Authors:

Minamiki, T., Sasaki, Y., Tokito, S., Minami, T.

Journal:

ChemistryOpen (2017): 472-475

Physical properties

Molecular weight	1838.08
Solvent	Water

Spectral properties

Correction factor (260 nm)	0.31
Correction factor (280 nm)	0.12
Extinction coefficient (cm ^-1 M ^-1)	76000
Excitation (nm)	498
Emission (nm)	526

Storage, safety and handling

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

Instrument settings

Gel Imager
Excitation	Blue laser
Emission	Long path green filter (SYBR filter)

Documents

Protocol
Safety Data Sheet
Certificate of Analysis

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Page updated on November 3, 2025