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Human CLPS / Colipase Protein (His Tag)

DatasheetSpecific ReferencesReviewsRelated ProductsProtocols
Human CLPS Protein Product Information
Protein Construction:A DNA sequence encoding the human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus.
Expressed Host:Baculovirus-Insect Cells
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.
Human CLPS Protein QC Testing
Purity:> 90 % as determined by SDS-PAGE
Bio-Activity: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.
Endotoxin:< 1.0 EU per μg of the protein as determined by the LAL method
Stability:Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N Terminal:Ala 18
Molecule Mass: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.
Formulation: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.
Human CLPS Protein Usage Guide
Storage: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.
Reconstitution:A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
Human CLPS Protein SDS-PAGE
Human CLPS / Colipase Protein (His Tag) SDS-PAGE
Other CLPS Recombinant Protein Products
CLPS / Colipase 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.

Human CLPS / Colipase References
  • Davis RC, et al. (1991) Assignment of the human pancreatic colipase gene to chromosome 6p21.1 to pter. Genomics. 10(1):262-5.
  • Lowe ME. (1997) Structure and function of pancreatic lipase and colipase. Annu Rev Nutr. 17: 141-58.
  • Verger R, et al. (1999) Colipase: structure and interaction with pancreatic lipase. Biochim Biophys Acta. 1441(2-3):173-84.
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    Size / Price
    Catalog: 13631-H08B-50
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    All information of our products is subject to change without notice. Please refer to COA enclosed in shipped package for the newest information.