CLPS Human
Description
CLPS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Colipase is a small protein that plays a crucial role in the digestion of dietary fats. It is a cofactor for pancreatic lipase, an enzyme responsible for breaking down triglycerides into free fatty acids and monoglycerides. Without colipase, pancreatic lipase cannot effectively anchor to the lipid-water interface, which is essential for its activity. Colipase is produced in the pancreas and is secreted into the small intestine, where it facilitates the digestion of fats by stabilizing the active conformation of pancreatic lipase.
Colipase belongs to the colipase family and has a molecular mass of approximately 11.5 kDa . It is characterized by five conserved disulfide bonds that contribute to its stability and functionality. The protein structure of colipase allows it to bind noncovalently to the surface of lipid micelles, counteracting the destabilizing influence of intestinal bile salts . This binding is essential for the proper functioning of pancreatic lipase, as bile salts can inhibit the enzyme by washing it off the lipid surface.
Recombinant human colipase can be produced using various expression systems, including Escherichia coli (E. coli) and baculovirus-insect cells. The process typically involves the following steps:
- Gene Cloning: The gene encoding human colipase is cloned into an appropriate expression vector.
- Transformation: The vector is introduced into the host cells (e.g., E. coli or insect cells).
- Expression: The host cells are cultured under conditions that induce the expression of the recombinant protein.
- Purification: The recombinant colipase is purified using techniques such as affinity chromatography, which may involve tags like His-tag for easier purification .
For example, in one study, recombinant human pancreatic lipase (recHPL) was successfully prepared from E. coli using a short Strep-tag II (ST II). The recHPL-ST II was solubilized using 8 M urea from the E. coli lysate and purified on a Strep-Tactin-Sepharose column .
Recombinant human colipase is used in various research and clinical applications. It is essential for studying the mechanisms of lipid digestion and the role of pancreatic lipase in metabolic processes. Additionally, recombinant colipase can be used in enzyme replacement therapies for individuals with pancreatic insufficiency, where the pancreas does not produce enough digestive enzymes.
