70923
BugBuster® (primary amine-free) Extraction Reagent
Synonym(s):
Protein Extraction Reagent
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About This Item
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
Related Categories
General description
Features and Benefits
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
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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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