Lipoprotein Lipase , human, recombinant

Life Sciences / Peptides and Biochemicals / Research Peptides

-20 C

LPL is a lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. LPL acts as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Type I hyperlipoproteinemia is a result of severe mutations which cause LPL deficiency, whereas less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. Lipoprotein lipase (LPL) is a fundamental enzyme in plasma triglyceride hydrolysis and is secreted by macrophages in the subendothelial space. LPL also promotes the development of atherosclerosis through facilitation of monocyte adhesion to endothelial cells, stimulation of tumor necrosis factor alpha (TNF) secretion and induction of vascular smooth muscle cell proliferation.Description: The Recombinant Human LPL produced in E.coli has a molecular mass of 51.61kDa containing 458 amino acid residues of the human LPL and fused to a 10 a.a. His tag at N-terminus.Formulation: LPL was filtered (0.4 µ m) and lyophilized from 0.5 mg/ml in 50mM Acetate buffer, pH=4Solubility: It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µ g/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.Stability: Store lyophilized protein at -20° C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4° C for a limited period of time; it does not show any change after two weeks at 4° C.