Recombinant Rat CLPS/Colipase Protein (His Tag) | PKSR030146

Recombinant Rat CLPS/Colipase Protein (His Tag) | PKSR030146 | Gentaur US, UK & Europe Disrtribition

Synonyms: CLPS;Colipase

Active Protein: N/A

Activity: A DNA sequence encoding the rat Clps (NP_037271.1) (Met1-Gln112) was expressed with a polyhistidine tag at the C-terminus.

Protein Construction: A DNA sequence encoding the rat Clps (NP_037271.1) (Met1-Gln112) was expressed with a polyhistidine tag at the C-terminus.

Fusion Tag: C-His

Species: Rat

Expressed Host: HEK293 Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per μg protein as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 11.9 kDa

Formulation: Lyophilized from sterile PBS, pH 7.4

Reconstitution: Please refer to the printed manual for detailed information.

Background: 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.

Research Area: N/A