CLPS Protein, Human (sf9, His)

CLPS or colipase is an important cofactor for pancreatic lipase that helps anchor it at the lipid-water interface. In the absence of colipase, pancreatic lipase is easily washed away by bile salts, which inhibit the enzyme. CLPS Protein, Human (sf9, His) is the recombinant human-derived CLPS protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of CLPS Protein, Human (sf9, His) is 95 a.a., with molecular weight of ~12 kDa.

Colipase (CLPS) is a vital cofactor for pancreatic lipase, facilitating its anchoring to the lipid-water interface. This interaction is crucial for the enzyme's stability and effectiveness in lipid digestion. In the absence of colipase, pancreatic lipase is prone to being washed away by bile salts, which exert an inhibitory effect on the lipase. Colipase's role in enhancing lipase activity underscores its significance in efficient lipid hydrolysis within the digestive system. Furthermore, the biological activity of enterostatin as a satiety signal suggests a potential role for colipase in the regulation of appetite and food intake, further highlighting its multifaceted functions in digestive processes and metabolic regulation (

Human

Sf9 insect cells

C-His

P04118 (A18-Q112)

1208  [NCBI]

APGPRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSITNTNFGICHDAGRSKQ

Approximately 12 kDa

Greater than 90% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.