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.
Tag
His tag
Description
A DNA sequence encoding the human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus.
Regulatory
RUO
Host
Baculovirus-Insect Cells
Endotoxin Level
< 1.0 EU per μg of the protein as determined by the LAL method
Nature
Recombinant
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Buffer
Lyophilized from sterile PBS, 500mM NaCl, pH 7.0, 10% gly
Description
Please refer to the printed manual for detailed information.
Purity
> 90 % as determined by SDS-PAGE
Expiry Date
Samples are stable for up to twelve months from date of receipt at -70℃
Immunogen Species
Homo Sapiens (Human)
Attachment
Reviews of Recombinant Human CLPS/Colipase Protein (His Tag)(Active)