Recombinant CLPS Protein, Human (His Tag) Recombinant Proteins The human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus The recombinant human CLPS consists of 105a.a and predicts a molecular weight of 11.5 kDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.
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Formulation: The recombinant human CLPS consists of 105a.a and predicts a molecular weight of 11.5 kDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.
Source: Baculovirus-Insect Cells
Usage: Our products are for research use only. This product is not intended or approved for human, diagnostics or veterinary use

Recombinant CLPS Protein, Human (His Tag)

The product is for non-human research only. Not for therapeutic or veterinary use.

Catalog No: bt-203542

Molecular Weight: The recombinant human CLPS consists of 105a.a and predicts a molecular weight of 11.5 kDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.

Formulation: Recombinant CLPS Protein was lyophilized from sterile PBS, 500mM NaCl, pH 7.0, 10% gly1

Source: Baculovirus-Insect Cells

Product Name Recombinant CLPS Protein, Human (His Tag)
AA Sequence Met 1-Gln 112
Bioactivity 1. Measured by its binding ability in a functional ELISA.2. Immobilized human CLPS-His at 10ug/mL(100uL/well) can bind biotinylated human PNLIP-His.The EC50 of biotinylated human PNLIP-His is 0.57-1.33ug/mL.
Description The human CLPS (P04118) (Met 1-Gln 112) was fused with a polyhistidine tag at the C-terminus
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant CLPS Protein was lyophilized from sterile PBS, 500mM NaCl, pH 7.0, 10% gly1
Host Species Homo sapiens (Human)
Molecular Weight The recombinant human CLPS consists of 105a.a and predicts a molecular weight of 11.5 kDa. It migrates as an approximately 12 KDa band in SDS-PAGE under reducing conditions.
Product 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.
Product Type Recombinant Protein
Purity Greater than 90% as determined by SDS-PAGE
Source Baculovirus-Insect Cells
Storage Store recombinant protein under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Terminal Ala 18
Uniprot No P04118
Usage Our products are for research use only. This product is not intended or approved for human, diagnostics or veterinary use