Recombinant Thermobifida fusca Cutinase Protein (His Tag) | PKSQ050088

Recombinant Thermobifida fusca Cutinase Protein (His Tag) | PKSQ050088 | Gentaur US, UK & Europe Disrtribition

Synonyms: Cutinase

Active Protein: N/A

Activity: Recombinant Thermobifida fusca Cutinase is produced by our E.coli expression system and the target gene encoding Ala1-Phe261 is expressed with a 6His tag at the C-terminus.

Protein Construction: Recombinant Thermobifida fusca Cutinase is produced by our E.coli expression system and the target gene encoding Ala1-Phe261 is expressed with a 6His tag at the C-terminus.

Fusion Tag: C-His

Species: Thermobifida fusca

Expressed Host: E.coli

Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg as determined by the LAL method.

Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

Molecular Mass: 29.5 kDa

Formulation: Supplied as a 0.2 μm filtered solution of PBS, 50% Glycerol, pH7.4.

Reconstitution: Not Applicable

Background: Cutinase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is cutin hydrolase. Cutinase is a serine esterase containing the classical Ser, His, Asp triad of serine hydrolases. The protein belongs to the alpha-beta class, with a central beta-sheet of 5 parallel strands covered by 5 helices on either side of the sheet. Cutin monomers released from the cuticle by small amounts of cutinase on fungal spore surfaces can greatly increase the amount of cutinase secreted by the spore. The active site cleft is partly covered by 2 thin bridges formed by amino acid side chains, by contrast with the hydrophobic lid possessed by other lipases. The protein also contains 2 disulfide bridges, which are essential for activity, their cleavage resulting in complete loss of enzymatic activity.

Research Area: N/A