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Lipoprotein lipase hydrolyzes triglycerides in plasma lipoproteins causing release of fatty acids for metabolic purposes in muscles and adipose tissue.
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Thrombin is an endolytic serine protease that selectively cleaves the Arg-Gly bonds of fibrinogen to form fibrin and release fibrinopeptides A and B.1 2The optimal cleavage sites for thrombin are as follows1. A-B-Pro-Arg--X-Y where A and B are hydrophobic amino acids and X and Y are nonacidic amino acids.2. Gly-Arg--GlyRecombinant human thrombin protease is expressed in human HEK 293 cells as a glycoprotein heterodimer. The DTT-reduced protein migrates as two bands of 31 kDa (heavy chain) and 6 kDa (light chain) on SDS-PAGE. This protein is manufactured in human cells with no serum. The human cells expression system allows human-like glycosylation and folding and often supports higher activity of the protein. This thrombin protease is useful for cleaving recombinant proteins that are expressed as fusion proteins with this sequence between the carrier domain and the protein of interest.
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Plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. Required for normal branching morphogenesis. May play a role in wound healing.