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CLPS Protein (His tag)

CLPS Origin: Human Host: Baculovirus infected Insect Cells Recombinant > 90 % as determined by reducing SDS-PAGE. Active
Catalog No. ABIN7317222
  • Target See all CLPS Proteins
    CLPS (Colipase, Pancreatic (CLPS))
    Protein Type
    Recombinant
    Biological Activity
    Active
    Origin
    • 6
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Human
    Source
    • 6
    • 3
    • 2
    • 2
    • 1
    Baculovirus infected Insect Cells
    Purification tag / Conjugate
    This CLPS protein is labelled with His tag.
    Purpose
    Recombinant Human CLPS/Colipase Protein (His Tag)(Active)
    Sequence
    Met 1-Gln 112
    Characteristics
    A DNA sequence encoding the human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus.
    Purity
    > 90 % as determined by reducing SDS-PAGE.
    Endotoxin Level
    < 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.
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    Discover our top product CLPS Protein
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Reconstitution
    Please refer to the printed manual for detailed information.
    Buffer
    Lyophilized from sterile PBS, 500 mM NaCl, pH 7.0, 10 % gly
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    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.
  • Target
    CLPS (Colipase, Pancreatic (CLPS))
    Alternative Name
    CLPS/Colipase (CLPS Products)
    Synonyms
    CLPS Protein, 2200003J09Rik Protein, COLQ Protein, colipase Protein, colipase, pancreatic Protein, CLPS Protein, Clps Protein
    Background

    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

    Molecular Weight
    11.5 kDa
    UniProt
    P04118
    Pathways
    Lipid Metabolism
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