Rat CLPS / Colipase Protein (His Tag)
CLPS, Colipase
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| Catalog Number | P80729-R08H |
|---|---|
| Organism Species | Rat |
| Host | Human Cells |
| Synonyms | CLPS, Colipase |
| Molecular Weight | The recombinant rat Clps consists 106 amino acids and predicts a molecular mass of 11.9 kDa. |
| predicted N | Ala 18 |
| SDS-PAGE |  |
| Purity | > 95 % as determined by SDS-PAGE. |
| Protein Construction | A DNA sequence encoding the rat Clps (NP_037271.1) (Met1-Gln112) was expressed with a polyhistidine tag at the C-terminus. |
| Bio-activity | |
| Research Area | Cardiovascular |Lipids / Lipoproteins |Lipid Metabolism |
| Formulation | Lyophilized from sterile PBS, pH 7.4. 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | 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. |
| Reference |