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Literature summary for 4.2.2.7 extracted from

  • Huang, J.; Cao, L.; Guo, W.; Yuan, R.; Jia, Z.; Huang, K.
    Enhanced soluble expression of recombinant Flavobacterium heparinum heparinase I in Escherichia coli by fusing it with various soluble partners (2012), Protein Expr. Purif., 83, 169-176.
    View publication on PubMed

Application

Application Comment Organism
synthesis expression as fusion protein, fused to the C-terminus of soluble partners translation initiation factor 2 domain I, glutathione S-transferase, maltose-binding protein, small ubiquitin modifying protein and N-utilization substance A, and purification of hybrid proteins. Except for NusA, the fusion partners dramatically improve the soluble expression of recombinant HepA, with translation initiation factor 2 domain I-HepA and small ubiquitin modifying protein-HepA creating almost completely soluble HepA where 98% and 94% of expressed HepA fusions are soluble, respectively Pedobacter heparinus

Cloned(Commentary)

Cloned (Comment) Organism
expression as fusion protein, fused to the C-terminus of soluble partners Pedobacter heparinus

Organism

Organism UniProt Comment Textmining
Pedobacter heparinus
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-
-

Synonyms

Synonyms Comment Organism
HepA
-
Pedobacter heparinus