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70751

Millipore

BugBuster® Ni-NTA His•Bind® Purification Kit

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About This Item

Code UNSPSC :
41106500
Nomenclature NACRES :
NA.56

Fabricant/nom de marque

Novagen®

Conditions de stockage

OK to freeze

Conditions d'expédition

wet ice

Description générale

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) , Ras(WT) proteins and CsgA (major curlin subunit) proteins.

Composants

•2 × 100 mlBugBuster Protein Extraction Reagent

•10,000 UBenzonase Nuclease, purity >90%

•10 mlNi-NTA His•Bind Resin

•pkg/4Chromatography Columns

Avertissement

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

Autres remarques

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.

Informations légales

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

Pictogrammes

Flame
GHS02

Mention d'avertissement

Danger

Mentions de danger

H225

Classification des risques

Flam. Liq. 2

Code de la classe de stockage

3 - Flammable liquids

Classe de danger pour l'eau (WGK)

WGK 3

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Consulter la Bibliothèque de documents

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

Articles

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.

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.

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.

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.

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