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BugBuster® 10X Protein Extraction Reagent
BugBuster 10X is a concentrated formulation of the protein extraction reagent, using proprietary detergents employed in BugBuster without the addition of salts or buffer components.
Synonym(s):
BugBuster Reagent
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About This Item
Quality Level
form
liquid
manufacturer/tradename
Novagen®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
technique(s)
protein purification: suitable
suitability
suitable for column chromatography
application(s)
life science and biopharma
shipped in
ambient
storage temp.
10-30°C
General description
Features and Benefits
Proprietary detergents: The proprietary detergents used in BugBuster 10X provide all the benefits of the standard BugBuster reagent, such as efficient lysis of bacterial and yeast cells. The absence of salts and buffer components ensures that the extracted protein is of high purity and free from contaminants.
User-defined control: With BugBuster 10X, users have complete control over the pH, reagent concentration, and buffer additives necessary for optimal protein extraction and activity. This level of customization makes it an ideal solution for working on protein research with unique requirements.
Pain points addressed: BugBuster 10X addresses the pain points including but not limited to: low yields, inefficient extraction, and protein degradation. Its concentrated formulation and user-defined control offer a flexible and efficient solution to protein extraction, resulting in high-quality protein samples for downstream applications.
Legal Information
Disclaimer
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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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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