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A propos de cet article
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Matériaux
self-standing
Caractéristiques
binder
Fabricant/nom de marque
PureProteome
Technique(s)
RNA purification: suitable (with magnetic beads)
protein purification: suitable
Conditions d'expédition
ambient
Catégories apparentées
1 of 4
Cet article | LSKMAGL10 | LSKMAGS08 | LSKMAGG |
|---|---|---|---|
| feature binder | feature - | feature binder | feature - |
| manufacturer/tradename PureProteome | manufacturer/tradename PureProteome | manufacturer/tradename PureProteome | manufacturer/tradename PureProteome |
| material self-standing | material - | material self-standing | material - |
| technique(s) RNA purification: suitable (with magnetic beads) | technique(s) depletion: suitable (serum), protein purification: suitable | technique(s) RNA purification: suitable (with magnetic beads), protein purification: suitable | technique(s) depletion: suitable (serum), immunoprecipitation (IP): suitable, protein purification: suitable |
| shipped in ambient | shipped in wet ice | shipped in ambient | shipped in wet ice |
Description générale
Application
- purification à l'aide de billes magnétiques
- purification des protéines
- purification du complexe protéique impliquant la protéine de choc thermique 90 (Hsp90)/Cdc37 (cycle de division cellulaire 37)/kinase dépendante des cyclines 4 (Cdk4), pour incuber et laver les billes avec 10 volumes de tampon de lyse[1]
Autres remarques
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Contenu apparenté
Read an automated protocol for protein purification using PureProteome™ nickel magnetic beads on the AAW™ automated assay workstation and see results comparing manual vs automated runs.
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.
Purification of recombinant proteins expressed in E.coli requires many time-consuming steps. To liberate the protein of interest, traditional bacterial lysis relies on the addition of lysozyme and a combination of sonication and repeated freeze/thaw cycles to break the bacterial cell wall. Disruption of the cell is accompanied by an increase in the viscosity of the suspension, due to the release of DNA. An endonuclease is added to digest the DNA, thus reducing the viscosity of the lysate. Finally, to render the lysate compatible with traditional purification methods, insoluble cell debris must be removed by centrifugation.
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