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BugBuster® Ni-NTA His•Bind® Purification Kit

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storage condition

OK to freeze

shipped in

wet ice

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Ni-NTA Buffer Kit



Ni-NTA Reagent Kit

shipped in

wet ice

shipped in


shipped in


shipped in

wet ice

storage condition

OK to freeze

storage condition

OK to freeze

storage condition

OK to freeze

storage condition


General description

BugBuster®Ni-NTA HIS-BIND® Purification Kit is used for protein purification. Ni-NTA HIS-BIND® Resin is high-performance Ni2+-charged agarose used for rapid, one-step purification of proteins containing a polyhistidine tag sequence.


BugBuster®Ni-NTA HIS-BIND® Purification Kit has been used for the purification of His tagged proteins such as trehalose-6-phosphate phosphatase (TPP) , Ras(WT) proteins and CsgA (major curlin subunit) proteins.


•2 × 100 mlBugBuster Protein Extraction Reagent

•10,000 UBenzonase Nuclease, purity >90%

•10 mlNi-NTA His•Bind Resin

•pkg/4Chromatography Columns


Toxicity: Multiple Toxicity Values, refer to MSDS (O)

Other Notes

Due to the nature of the Hazardous Materials in this shipment, additional shipping charges may be applied to your order. Certain sizes may be exempt from the additional hazardous materials shipping charges. Please contact your local sales office for more information regarding these charges.

Legal Information

BUGBUSTER is a registered trademark of Merck KGaA, Darmstadt, Germany
HIS-BIND is a registered trademark of Merck KGaA, Darmstadt, Germany
NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany






Hazard Classifications

Flam. Liq. 2

Storage Class

3 - Flammable liquids



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Sagar Lahiri et al.
Journal of cellular physiology, 229(9), 1245-1255 (2014-01-22)
Trehalose-6-phosphate phosphatase (TPP) catalyzes the final step in the biosynthesis of the anti-stress sugar trehalose. An 82 kDa TPP enzyme was isolated from Candida utilis with 61% yield and 43-fold purification. The protein sequence, determined by N-terminal sequencing and MALDI-TOF analysis
Chae-Seok Lim et al.
Small (Weinheim an der Bergstrasse, Germany), 13(40) (2017-08-16)
Intermolecular interactions dominate the behavior of signal transduction in various physiological and pathological cell processes, yet assessing these interactions remains a challenging task. Here, this study reports a single-molecule force spectroscopic method that enables functional delineation of two interaction sites
Sarah A Tursi et al.
PLoS pathogens, 13(4), e1006315-e1006315 (2017-04-15)
Bacterial biofilms are associated with numerous human infections. The predominant protein expressed in enteric biofilms is the amyloid curli, which forms highly immunogenic complexes with DNA. Infection with curli-expressing bacteria or systemic exposure to purified curli-DNA complexes triggers autoimmunity via


This article shows the use of BugBuster® and Benzonase® as protein purification tools to extract recombinant proteins from E. coli and to reduce the viscosity of the extract.

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

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