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Low CLPS expression is associated with pancreatic cancer.
humans with the Arg92Cys substitution will secrete less functional colipase
found no evidence for an association of pancreatic colipase(CLPS) single nucleotide polymorphisms rs2766597, rs41270082, rs3748050, and rs3748051 with obesity or percentage of dietary fat intake
evidence in two German Caucasian study populations that the variant of the rare colipase Arg109Cys polymorphism might contribute to increased susceptibility of type 2 diabetes
Our findings demonstrate that the Arg92Cys polymorphism decreases the function of Cys92 colipase. This change may contribute to the development of type 2 diabetes.
CLPS genetic variability associates with insulin secretory function in non-diabetic humans and may represent a novel candidate gene for development of type 2 diabetes
Data suggest that the conditional expression of mPlrp2 and mClps is involved in the hydrolysis of retinyl esters in the mouse liver.
colipase (-/-)mice develop diet-induced obesity, as do colipase (+/+) mice, and have normal responses to a two-macronutrient choice diet and to a switch from a high-fat to a low-fat diet
We conclude that, in addition to its critical role in fat digestion, procolipase has essential functions in postnatal development and in regulating body weight set point.
isotropic orientation of colipase which could explain its incapacity to reverse the inhibitory effects of these lipids on the lipase activity
Analysis of structures of NMR colipase models and simulations of their interactions with various lipid aggregates, lipid droplet, and bile salt micelle, were carried out to determine and to map the lipid binding sites on colipase.
The protein encoded by this gene is a cofactor needed by pancreatic lipase for efficient dietary lipid hydrolysis. It binds to the C-terminal, non-catalytic domain of lipase, thereby stabilizing an active conformation and considerably increasing the overall hydrophobic binding site. The gene product allows lipase to anchor noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts. This cofactor is only expressed in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Three transcript variants encoding different isoforms have been found for this gene.
, pancreatic colipase preproprotein
, pancreatic colipase
, procolipase II