Recombinant Human CLPS/Colipase Protein (His Tag)(Active)

CLPS;Colipase

P04118

Immobilized human CLPS-His at 10ug/mL(100uL/well) can bind biotinylated human PNLIP-His. The EC50 of biotinylated human PNLIP-His is 0.57-1. 33ug/mL.

Colipase belongs to the colipase family. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture. It is a small protein with five conserved disulphide bonds. Structural analogies have been recognised between a developmental protein, the pancreatic lipase C-terminal domain, the N-terminal domains of lipoxygenases and the C-terminal domain of alpha-toxin. Colipase can only be detected in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Colipase allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase. Colipase is a cofactor needed by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilising as active conformation and considerably increasing the overall hydrophobic binding site.

11.5 kDa

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

Baculovirus-Insect Cells

Lyophilized from sterile PBS, 500mM NaCl, pH 7.0, 10% glycerol
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

12 kDa

> 90 % as determined by reducing SDS-PAGE.

Met 1-Gln 112

CLPS

P04118