71456
BugBuster® Master Mix
Synonym(s):
BugBuster® Protein Extraction Reagent with Benzonase® Nuclease and rLysozyme solution, Cell Lysis Master Mix
Select a Size
About This Item
form
liquid
Quality Level
manufacturer/tradename
Novagen®
storage condition
OK to freeze
shipped in
wet ice
storage temp.
2-8°C
Related Categories
General description
Application
- 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
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
Disclaimer
Storage Class
10 - Combustible liquids
wgk_germany
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’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Articles
Citation Spotlight: BugBuster® Protein Extraction Reagent for Efficient Protein Extraction from Bacterial Pathogens
Related Content
Cell lysis and protein extraction methods overview various techniques, from detergent solubilization to mechanical disruption, supporting research needs.
Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.
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.
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.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service