G/GS Linker-digesting Enzyme
CAT#: VS-0724-CJ10
This G/GS linker-digesting enzyme can digest the G/GS-rich linkers of fusion proteins. These linkers consisting of glycine (G), or glycine and serine (GS) can be digested within 1 hour without reducing conditions. The enzyme was cloned from Phage K and produced in E. coli with His-tag for easy purification.
Specifications
- Cleavage Site
- Mutiple sites in G or GS-rich linkers
- Species Reactivity
- No species dependent
- Specificity
- G or GS-rich linkers
- Reaction Condition
- 1-hour reaction
- Format
- Lyophilized; Immobilized
- Original Source
- Phage K
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Fast And Efficient Digestion
This enzyme is a game changer for our fusion protein analysis. It completely digested the glycine-rich linker within one hour as promised, allowing us to separate the domains for individual structural characterization without using harsh reducing agents.
Easy Removal Via His Tag
We really appreciated that this enzyme comes with a His-tag. After the digestion reaction was complete, we were able to easily remove the enzyme from our sample using a simple nickel column, leaving our target protein pure and ready for downstream applications.
Q&As
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What are the reaction conditions required for this linker-digesting enzyme?
A: This enzyme is highly efficient and can digest G or GS-rich linkers within just 1 hour. Importantly, the reaction can proceed without reducing conditions, which is beneficial if you need to maintain the disulfide bonds or the native conformation of your fusion protein domains during the cleavage process.
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Does this enzyme have a tag to facilitate its removal after digestion?
A: Yes, the enzyme is produced in E. coli and contains a His-tag. This design feature allows for easy purification and subsequent removal of the enzyme from your reaction mixture using immobilized metal affinity chromatography (IMAC), ensuring your digested sample remains pure.
View the frequently asked questions answered by Creative Biolabs Support.
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