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Merck

71456

BugBuster® Master Mix

Synonym(s):

BugBuster® Protein Extraction Reagent with Benzonase® Nuclease and rLysozyme solution, Cell Lysis Master Mix

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About This Item

UNSPSC Code:
41106511
NACRES:
NA.32

Key Documents

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form

liquid

Quality Level

200

manufacturer/tradename

Novagen®

storage condition

OK to freeze

shipped in

wet ice

storage temp.

2-8°C

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General description

The BugBuster® Master Mix enables efficient protein purification and other related applications. It replaces the need for mechanical methods like the French press or sonication. The two available package sizes contain sufficient reagents for extracting proteins from either 20 grams or 100 grams of cell paste.

Application

BugBuster® Master Mix has been used:
  • to resuspend and lyse the cell pellets during protein purification
  • to extract proteins for immunoblotting
  • as a bacterial lysis buffer for the preparation of inclusion bodies


    

Biochem/physiol Actions

BugBuster® Protein Extraction Reagent is specifically designed to gently disrupt the cell wall of E. coli, allowing the release of soluble proteins. This unique formulation utilizes a detergent mix that can effectively perforate the cell wall without denaturing the soluble proteins. By combining BugBuster Reagent, rLysozyme solution, and Benzonase Nuclease, our BugBuster Master Mix enhances protein extraction efficiency and simplifies downstream processing of protein extracts.

Features and Benefits

  • Efficient lysis of Gram-positive and Gram-negative bacteria
  • Maximum recovery of active, soluble protein
  • Capable of cell wall perforation without denaturing soluble protein
  • Useful for the preparation of high purity inclusion bodies
  • Compatible with protease and phosphatase inhibitor cocktail

  • Offers a convenient, fast, and cost-effective solution for releasing the expressed target protein.
  • The Master Mix eliminates the need to dilute or perform separate addition steps.

Legal Information

BUGBUSTER is a registered trademark of Merck KGaA, Darmstadt, Germany
Benzonase is a registered trademark of Merck KGaA, Darmstadt, Germany
NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany

Disclaimer

Toxicity: Standard Handling (A)

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

71456-25ML:
71456-3:
71456-EA:
71456-ML:
71456-4:
71456-1L:
71456-100ML:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Matthew Thomas Doyle et al.
Molecular cell, 81(9), 2000-2012 (2021-03-12)
The β-barrel assembly machine (BAM) integrates β-barrel proteins into the outer membrane (OM) of Gram-negative bacteria. An essential BAM subunit (BamA) catalyzes integration by promoting the formation of a hybrid-barrel intermediate state between its own β-barrel domain and that of
Daniel G Isom et al.
Proteins, 79(4), 1034-1047 (2011-03-10)
Protein thermodynamic stability is a fundamental physical characteristic that determines biological function. Furthermore, alteration of thermodynamic stability by macromolecular interactions or biochemical modifications is a powerful tool for assessing the relationship between protein structure, stability, and biological function. High-throughput approaches
Yong Y Peng et al.
Bioengineered, 5(6), 378-385 (2014-12-09)
The collagen like domain Scl2 from Streptococcus pyogenes has been proposed as a potential biomedical material. It is non-cytotoxic and non-immunogenic and can be prepared in good yield in fermentation. The Scl2 collagen domain is about a quarter of the
Nicolas Broguiere et al.
Acta biomaterialia, 77, 182-190 (2018-07-15)
The bacterial ligase Sortase A (SA) and its mutated variants have become increasingly popular over the last years for post-translational protein modifications due to their unparalleled specificity and efficiency. The aim of this work was to study SA as a
Shmuel Gleizer et al.
Cell, 179(6), 1255-1263 (2019-11-30)
The living world is largely divided into autotrophs that convert CO2 into biomass and heterotrophs that consume organic compounds. In spite of widespread interest in renewable energy storage and more sustainable food production, the engineering of industrially relevant heterotrophic model

Articles

Citation Spotlight: BugBuster® Protein Extraction Reagent for Efficient Protein Extraction from Bacterial Pathogens

Citation Spotlight: BugBuster® Protein Extraction Reagent for Efficient Protein Extraction from Bacterial Pathogens

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Global Trade Item Number

SKUGTIN
71456-3CN07790788053260
71456-4CN04055977270150

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