CLPS
CLPS (colipase) is a secreted protein that acts as an essential cofactor for pancreatic lipase in the hydrolysis of dietary lipid. It belongs to the colipase family, and the older HGNC name for the gene was colipase, pancreatic. Browse Assay Genie's current range of CLPS research reagents below, or read on for the biology behind the target.
CLPS encodes colipase, a cofactor that pancreatic lipase needs for efficient hydrolysis of dietary lipid. Colipase binds the C-terminal, non-catalytic domain of lipase. This stabilises an active conformation of the enzyme and considerably enlarges its overall hydrophobic binding site. The cofactor also allows lipase to anchor noncovalently to the surface of lipid micelles, which counteracts the destabilising influence of intestinal bile salts.
The colipase protein is secreted and belongs to the colipase family. According to the NCBI Gene summary, expression is restricted to pancreatic acinar cells, which suggests that tissue-specific regulatory elements control the CLPS gene. Three transcript variants encoding different isoforms have been described. Orthologues are present in mouse and rat, both named Clps, which makes rodent models a practical route for studying the protein.
UniProt also records a second activity linked to this precursor: enterostatin, a peptide with biological activity as a satiety signal. CLPS is therefore of interest both in lipid digestion and in the study of feeding behaviour. The HGNC gene name is colipase, and the previous name was colipase, pancreatic. Researchers studying CLPS, whether through a CLPS antibody, a CLPS ELISA kit or recombinant CLPS protein, are typically working on dietary fat handling in the pancreas and gut.
Colipase is required by pancreatic lipase for efficient hydrolysis of dietary lipid, making it central to studies of fat digestion.
Colipase binds the non-catalytic C-terminal domain of lipase and stabilises its active conformation, a useful model of cofactor-assisted enzyme activation.
Colipase anchors lipase to lipid micelles and counteracts the destabilising effect of intestinal bile salts.
Enterostatin, linked to this precursor in UniProt, has biological activity as a satiety signal, connecting CLPS to feeding studies.
CLPS encodes colipase, a cofactor for pancreatic lipase. It binds the lipase C-terminal domain, stabilises an active conformation and anchors the enzyme to lipid micelles, counteracting destabilisation by intestinal bile salts so that dietary lipid is hydrolysed efficiently.
Yes. The NCBI Gene summary reports three transcript variants encoding different isoforms. The gene was previously named colipase, pancreatic. UniProt also describes enterostatin, a satiety signal, in connection with this protein. Check the datasheet of any product for its validated reactivity.
CLPS expression is reported only in pancreatic acinar cells, and the protein is secreted. Mouse and rat both have an orthologous gene named Clps. Check the datasheet of any product for its validated reactivity.
Pancreatic lipase, related digestive enzymes and other acinar cell proteins that may be studied alongside colipase.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P04118; product specifications from Assay Genie datasheets.