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BugBuster® Ni-NTA His•Bind® Purification Kit

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NACRES:
NA.56
UNSPSC Code:
41106500
Shipped in:
wet ice
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manufacturer/tradename

Novagen®

storage condition

OK to freeze

shipped in

wet ice

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.

Application

BugBuster®Ni-NTA HIS-BIND® Purification Kit has been used for the purification of His tagged proteins such as trehalose-6-phosphate phosphatase (TPP) [1], Ras(WT) proteins[2] and CsgA (major curlin subunit) proteins.[3]

Other Notes

•2 × 100 mlBugBuster Protein Extraction Reagent

•10,000 UBenzonase Nuclease, purity >90%

•10 mlNi-NTA His•Bind Resin

•pkg/4Chromatography Columns
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

Disclaimer

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

pictograms

Flame
GHS02

signalword

Warning

hcodes

H226

Clase de almacenamiento

3 - Flammable liquids

wgk

WGK 3

Hazard Classifications

Flam. Liq. 3

Certificados de análisis (COA)

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Artículos

BugBuster® and Benzonase® Reagents are the Clear Solutions to Simple, Efficient Extraction of E. coli Proteins

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.

Contenido relacionado

Ni-NTA HisﾕBind® Resins
Simultaneous cell lysis and capture using the Amicon®Pro device

E. coli transformation with poly-histidine tagged constructs represents a common vehicle for protein production. Initial screening of small-scale cultures is routinely performed to identify clones producing the highest amounts of protein with the desired form and function. As the demand for greater throughput at this level has increased, so has the need for process simplification and greater reproducibility. To meet this need, we have developed a condensed workflow that can be performed in a single device.

Protein Purification and Detection Tools
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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
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
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

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SKUGTIN
369071-5G04061837008450

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