CLPS Protein (His tag)
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- Target Alle CLPS Proteine anzeigen
- CLPS (Colipase, Pancreatic (CLPS))
- Protein-Typ
- Recombinant
- Biologische Aktivität
- Active
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Spezies
- Human
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Quelle
- Baculovirus infected Insect Cells
- Aufreinigungstag / Konjugat
- Dieses CLPS Protein ist gelabelt mit His tag.
- Verwendungszweck
- Recombinant Human CLPS/Colipase Protein (His Tag)(Active)
- Sequenz
- Met 1-Gln 112
- Produktmerkmale
- A DNA sequence encoding the human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus.
- Reinheit
- > 90 % as determined by reducing SDS-PAGE.
- Endotoxin-Niveau
- < 1.0 EU per μg as determined by the LAL method.
- Biological Activity Comment
- Measured by its binding ability in a functional ELISA. Immobilized human CLPS-His at 10μg/mL(100μL/well) can bind biotinylated human PNLIP-His.The EC50 of biotinylated human PNLIP-His is 0.57-1.33μg/mL.
- Top Product
- Discover our top product CLPS Protein
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- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Lyophilized
- Rekonstitution
- Please refer to the printed manual for detailed information.
- Buffer
- Lyophilized from sterile PBS, 500 mM NaCl, pH 7.0, 10 % gly
- Lagerung
- 4 °C,-20 °C,-80 °C
- Informationen zur Lagerung
- Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
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- Target
- CLPS (Colipase, Pancreatic (CLPS))
- Andere Bezeichnung
- CLPS/Colipase (CLPS Produkte)
- Synonyme
- CLPS Protein, 2200003J09Rik Protein, COLQ Protein, colipase Protein, colipase, pancreatic Protein, CLPS Protein, Clps Protein
- Hintergrund
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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.
Synonym: CLPS
- Molekulargewicht
- 11.5 kDa
- UniProt
- P04118
- Pathways
- Lipid Metabolism
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