CLPS / Colipase Protein (His Tag)

Colipase, pancreatic Protein Datasheet

CLPS / Colipase Protein Product Information

• Synonym: CLPS
• Protein Construction: A DNA sequence encoding the human CLPS (P04118) （Met 1-Gln 112）was fused with a polyhistidine tag at the C-terminus.
• Source: Human
• Expression Host: Baculovirus-Insect cells

CLPS / Colipase Protein QC Testing

• Purity: > 90 % as determined by SDS-PAGE
• 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
• Molecular 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.
• SDS-PAGE: CLPS / Colipase protein

CLPS / Colipase Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. 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.

CLPS / Colipase Protein Description

Colipase is a member of the colipase family. It is only expressed in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Colipase 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 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. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture. It 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.

References

1. Davis RC. et al., 1991, Genomics. 10 (1): 262-5.
2. Lowe ME. 1997, Annu Rev Nutr. 17: 141-58.
3. Verger R. et al., 1999, Biochim Biophys Acta. 1441 (2-3): 173-84.