Recombinant Thermobifida fusca Cutinase Protein (His Tag)

Cutinase;cut2

E5BBQ3

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.

29.5 kDa

< 1.0 EU per ug of the protein as determined by the LAL method.

E.coli

Supplied as a 0.2 um filtered solution of PBS,50% Glycerol,pH7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.

C-His

28-30 kDa

> 95 % as determined by reducing SDS-PAGE.

Ala1-Phe261

Cutinase

E5BBQ3