GlySERIAS®
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GlySERIAS is a unique enzyme that digests flexible glycine-rich fusion protein linkers such as Gly4Ser and GlyxSery (GS), and polyglycine (G) linkers.

SmartEnzymes™
GlySERIAS enables separation of the individual domains of multi-functional fusion proteins to facilitate characterization and increase the understanding of these molecules. Middle-level analysis of fusion proteins serves to both reduce the overall sample complexity and allows for domain-specific identification and monitoring of post-translational modifications.
For improved linker removal, we recommend GlySERIAS Immobilized.
For linker characterization, we recommend GlySERIAS Lyophilized.
Fusion proteins with flexible GS or G linkers
1 hour reaction (optimization for individual proteins may be required)
No need for reducing agents or co-factors
Flexible linkers consisting of repetitive sequences of Gly or Gly and Ser residues

Immobilized enzyme for digestion of fusion proteins in spin columns
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GlySERIAS is a unique enzyme for digestion of fusion proteins designed with flexible linkers consisting of repetitive sequences of glycine, or glycine and serine, residues. The enzyme is active under native reaction conditions and enables middle-level characterization of complex fusion proteins.
The linker regions are digested at several sites simultaneously, leading to separation of the previously linked components. Optimal activity occurs at pH 7.6 and the length of the incubation can be varied depending on the desired end-products. For improved linker removal we recommend GlySERIAS Immobilized, for linker characterization we recommend GlySERIAS Lyophilized.
GlySERIAS is cloned from phage K and is expressed in E. coli. The enzyme contains a His-tag and has a molecular weight of 18 kDa.
GlySERIAS Immobilized delivers a more complete digestion of linkers for precise characterization of fusion protein quality attributes.
Efficient digestion of multi-domain BiTE molecules, separating the domains for high-quality LC-MS analysis and precise localization of protein modifications
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