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Merck

70923

BugBuster® (primary amine-free) Extraction Reagent

Synonym(s):

Protein Extraction Reagent

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100 ML

€152.00

500 ML

€597.00

€152.00


Estimated to ship onDecember 09, 2025Details



About This Item

UNSPSC Code:
41106511
NACRES:
NA.77

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form

liquid

Quality Level

manufacturer/tradename

Novagen®

storage condition

OK to freeze
avoid repeated freeze/thaw cycles

shipped in

ambient

storage temp.

10-30°C

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This Item
7092270584-M71186
form

liquid

form

liquid

form

liquid

form

liquid

manufacturer/tradename

Novagen®

manufacturer/tradename

Novagen®

manufacturer/tradename

Novagen®

manufacturer/tradename

Novagen®

storage condition

OK to freeze

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze, avoid repeated freeze/thaw cycles

storage condition

OK to freeze

shipped in

ambient

shipped in

wet ice

shipped in

-

shipped in

wet ice

storage temp.

10-30°C

storage temp.

2-8°C

storage temp.

10-30°C

storage temp.

-

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

-

General description

BugBuster (primary amine-free) Protein Extraction Reagent is a special formulation of BugBuster designed for applications where primary amines would interfere if present in the protein extract, such as protein immobilization or cross-linking. The PIPPS buffer used in BugBuster (primary amine-free) has a similar buffer capacity and pH range as the original Tris-buffered BugBuster, but will not complex metal ions, also making it ideally suited for extraction of metal dependent proteins.

Features and Benefits

Primary Amine-Free Formulation: BugBuster® (primary amine-free) Extraction Reagent is specially designed for applications where primary amines would interfere with protein extract. This means that academic researchers can purify metal-dependent proteins or proteins to be used for immobilization or crosslinking without worrying about the presence of primary amines, which could cause interference.

Enhanced Extraction: The extraction process can be further enhanced by the addition of rLysozyme Solution and Benzonase Nuclease, which helps to efficiently extract and purify proteins from the sample.

Metal Ion Compatibility: The PIPPS buffer used in the primary amine-free formulation of BugBuster® has a similar buffer capacity and pH range as the original Tris-buffered BugBuster® but will not complex metal ions. This makes it an ideal choice for extraction of metal-dependent proteins

Legal Information

BUGBUSTER 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


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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Articles

The combination of BugBuster® and Lysonase™ reagents greatly enhances the release of soluble proteins from Gram-positive bacteria.

Cell lysis and nucleic acid removal for Gram-negative and Gram-positive bacteria using the BugBuster Plus Lysonase™ Kit

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

Related Content

Traditionally, protein purification from E. coli consists of four distinct phases: harvest, bacterial cell lysis, lysate clarification and protein purification. Bacterial lysis typically requires several time-consuming, hands-on steps, such as freeze/thaw cycles and sonication. These harsh lysis techniques may negatively impact protein quality and contribute to sample-to-sample variability. To maintain protein activity and integrity, detergent-based lysis buffers are routinely used to avoid mechanical protein extraction methods. Regardless of the lysis method used, centrifugation is traditionally required to pellet unwanted cell debris and permit recovery of the clarified lysate. The final step, purification, is frequently performed using affinity media specific for expressed epitope tags. Agarose-based media have typically been used, either as a slurry in microcentrifuge tubes or packed into gravity-driven or spin columns. While easier to manipulate, columns are greatly affected by lysate consistency and carryover of cell debris, which can lead to clogging of the column frits.

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