|Datasheet||Specific References||Reviews||Related Products||Protocols|
|A DNA sequence encoding the human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus.|
|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.
|> 90 % as determined by SDS-PAGE|
|1. Measured by its binding ability in a functional ELISA.|
2. Immobilized human CLPS-His at 10μg/mL(100μL/well) can bind biotinylated human PNLIP-His (Cat:13564-H08H).
The EC50 of biotinylated human PNLIP-His (Cat:13564-H08H) is 0.57-1.33μg/mL.
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The recombinant human CLPS consists of 105 amino acids and predicts a molecular mass of 11.5 kDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.|
|Lyophilized from sterile PBS, 500mM NaCl, pH 7.0, 10% gly|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
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.