LSKMAGS08
PureProteome Magnetic Stand
The PureProteome Magnetic Stand is designed to rapidly & easily isolate magnetic particles from up to eight 1. 5 mL or 2. 0 mL tubes.
Synonym(s):
Magnetic Bead Stand, Magnetic Separation Stand
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$1,030.00
$1,030.00
About This Item
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material
self-standing
feature
binder
manufacturer/tradename
PureProteome
technique(s)
RNA purification: suitable (with magnetic beads)
protein purification: suitable
shipped in
ambient
Related Categories
1 of 4
This Item | LSKMAGS15 | LSKMAG03CBX | LSKMAG1CBX |
|---|---|---|---|
| feature binder | feature binder | feature - | feature - |
| manufacturer/tradename PureProteome | manufacturer/tradename PureProteome | manufacturer/tradename PureProteome | manufacturer/tradename PureProteome |
| material self-standing | material self-standing | material - | material - |
| technique(s) RNA purification: suitable (with magnetic beads) | technique(s) RNA purification: suitable (with magnetic beads), protein purification: suitable | technique(s) protein purification: suitable | technique(s) protein purification: suitable |
| shipped in ambient | shipped in ambient | shipped in wet ice | shipped in wet ice |
General description
Application
Cell Culture
Features and Benefits
- Enables reproducible process
- Comparable results with standard protocols
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Certificates of Analysis (COA)
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Articles
Comparison of elution techniques for small-scale protein purification of FLAG® tag proteins using anti-FLAG® M2 magnetic beads.
PureProteome™ Protein A and G Magnetic beads provide a rapid and reproducible means to purify immunoglobulins (IgG) using the KingFisher Duo particle processor.
Related Content
Immunoprecipitation (IP) is a powerful technique for proteomic screening, biomarker discovery, and signaling network elucidation. It is frequently used to enrich target proteins from complex samples such as cell lysates or extracts. Traditional IP protocols use Protein A, Protein G or a mixture of Protein A and G coupled to a solid support resin, such as agarose beads, to capture an antigen/antibody complex in solution. As the number of samples increase, the traditional, manual IP method can be time-consuming. Processing of multiple IP reactions in parallel can introduce complexity, variability and pipetting errors, which may affect reproducibility.
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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