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Recombinant human apolipoprotein C-II with a C-terminal 6xHis tag, expressed in E. coli and supplied as a purified protein (5 μg). The protein (~13 kDa) is >95% pure by reducing SDS-PAGE and is intended for in vitro studies of triglyceride metabolism and lipoprotein lipase activation. Store at -20°C and aliquot for extended stability.
Expressed in E. coli with C-terminal 6xHis tag.
Approximately 13 kDa molecular weight.
Purity greater than 95% by reducing SDS-PAGE.
Supplied as 5 μg of purified protein for biochemical assays.
Store at -20°C and aliquot to maintain activity.
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Lipoprotein Lipase (LPL) is majorly secreted by myocytes and adipocytes in humans and is crucial for triglyceride homeostatis. Mutations in the catalytic domain of LPL impairs its interaction with glycosylphosphatidylinositol anchored high density lipoprotein binding protein 1 (GPIHBP1). The N-terminal catalytic domain is essential for lipolysis. The C-terminal is crucial for binding lipoproteins. Altered LPL levels may play role in the pathogenesis of atherosclerosis coronary heart disease and chronic lymphocytic leukemia.
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Recombinant human thrombospondin-1 is expressed in HEK293 cells as a glycoprotein with a calculated moleculaer mass of 127.5 kDa. This protein is manufactured in human cells using an all-human production system with no serum. The human cells expression system allows human-like glycosylation and folding and often supports better stability of the protein in culture.
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Recombinant human Clusterin (ApoJ) expressed in HEK293 cells, supplied as an Fc-His tagged fusion protein in lyophilized form. The product is formulated for stability and supplied with storage and handling recommendations for research use in biochemical and cell-based assays.
Recombinant expression in HEK293 cells.
C-terminal Fc and His tag.
Lyophilized formulation with trehalose and mannitol.
Recommended storage at -20°C; freeze aliquots at -80°C for long-term.
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The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene.
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