Anti-CLPS Antibody (Rabbit Polyclonal antibody) General Information
Reacts with: Human
Recombinant Human CLPS / Colipase protein (Catalog#13631-H08B)
Produced in rabbits immunized with purified, recombinant Human CLPS / Colipase (rh CLPS / Colipase; Catalog#13631-H08B; P04118; Met1-Gln112). CLPS / Colipase specific IgG was purified by Human CLPS / Colipase affinity chromatography.
Polyclonal Rabbit IgG
Protein A & Antigen Affinity
0.2 μm filtered solution in PBS with 5% trehalose
This antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Immunochemical staining of human CLPS in human pancreas with rabbit polyclonal antibody (1:1000, formalin-fixed paraffin embedded sections). Positive staining was localized to pancreatic acinus.
CLPS Background Information
Colipase belongs to the colipase family. Structural studies of the complex and of colipase alone have revealed the functionality of its architecture. It 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 can only be detected in pancreatic acinar cells, suggesting regulation of expression by tissue-specific elements. Colipase 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. 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.