PIERCE 15160/Immobilized Glutathione
產(chǎn)品名稱：Immobilized Glutathione
產(chǎn)品貨號：PIERCE 15160
產(chǎn)品規(guī)格：10 ML
產(chǎn)品價格：2395
產(chǎn)品說明書地址：http://www.piercenet.com/
銷售直線：021-31322337、（何）
Thermo Scientific Immobilized Glutathione is 4% beaded agarose resin to which glutathione has been covalently attached for use in affinity purification of glutathione-S-transferase （GST） and GST fusion proteins from cell lysates of various kinds.
Upon incubation of a sample with the glutathione agarose beads, GST-tagged proteins bind to the immobilized glutathione ligand, allowing undesired components of the sample to be washing away. Addition of reduced glutathione or an acid buffer recovers the GST fusion protein in purified form.
Highlights:
- High binding capacity – binds approximay 15mg of GST per milliliter of settled resin
- Low nonspecific binding – 4% beaded agarose and highly purified glutathione result in an affinity resin that is free of contaminants that could be a source of nonspecific binding
- Low steric hindrance – glutathione is immobilized through its central sulhydryl group by a 12-atom spacer arm, ensuring that the ligand is not sterically hindered from binding GST tags
- Compatible – use with Thermo Scientific B-PER Protein Extraction Reagents or other nondenaturing and nonreducing cell lysis reagents
- Convenient – offered as stand-alone resin or prepacked column for use in gravity-flow or centrifuge methods
Product Details:
The bound GST-tagged proteins can be eluted from the glutathione beads by any one of three alternative methods. The most common elution method is to add a buffer containing free Reduced Glutathione （Part No. 78259）, which mildly and competitively displaces the GST from the immobilized glutathione. GST can also be dissociated from glutathione using low pH buffer （e.g., 0.1M glycine, pH 2.8）. One other method is to cleave the fusion protein from the bound GST tag using a protease such as Factor Xa （Part No. 32521）; this method allows recovery of the protein without the GST fusion tag.
