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Literature summary for 3.4.19.12 extracted from

  • Jin, F.L.; Xu, X.X.; Yu, X.Q.; Ren, S.X.
    High-level expression of active recombinant ubiquitin carboxyl-terminal hydrolase of Drosophila melanogaster in Pichia pastoris (2009), Protein Expr. Purif., 65, 115-121.
    View publication on PubMed
Search for more literature for 3.4.19.12

Application

Application Comment Organism
molecular biology Pichia pastoris is a robust system to express the secreted form of Drosophila melanogaster UCH Drosophila melanogaster

Cloned(Commentary)

Cloned (Comment) Organism
active C-terminal His-tagged UCH expressed in Pichia pastoris Drosophila melanogaster

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 1 * 29000, SDS-PAGE or calculated from the deduced amino acid sequence Drosophila melanogaster

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant UCH purified to homogeneity by gel filtration, fusion protein purified by Ni-NTA chromatography Drosophila melanogaster

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ubiquitin-magainin + H2O is efficiently cleaved at the carboxyl terminus of ubquitin, yielding recombinant magainin with high antimicrobial activity Drosophila melanogaster magainin + ubiquitin
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 29000, SDS-PAGE or calculated from the deduced amino acid sequence Drosophila melanogaster

Synonyms

Synonyms Comment Organism
ubiquitin carboxyl-terminal hydrolase
-
 Drosophila melanogaster
UCH
-
 Drosophila melanogaster

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
-
 Drosophila melanogaster