| Description | Cardiolipin (CL) is a complex lipid with a dimeric structure. It has four acyl chains and two phosphatidyl moieties. Its phosphatidyl moieties are linked to the glycerol backbone. Around 15-20 percent of the inner mitochondrial membrane accounts for cardiolipin.Cardiolipin is a unique phospholipid Cardiolipin (CL) is a complex lipid with a dimeric structure. It has four acyl chains and two phosphatidyl moieties. Its phosphatidyl moieties are linked to the glycerol backbone. Around 15-20 percent of the inner mitochondrial membrane accounts for cardiolipin.Cardiolipin is a unique phospholipid found exclusively within the mitochondrial inner membrane. This specific localization allows Cardiolipin to exert crucial influence on mitochondrial structure and function. Deviations in Cardiolipin content, structure, or localization can lead to impaired mitochondrial activity, contributing to various diseases like cancer, neurological disorders, cardiovascular conditions, and metabolic diseases. As Cardiolipin plays a crucial role in mitochondrial function, it holds immense potential for biomarker development and finds application in cardiovascular, neuroscience, cancer, diabetes, and metabolomics research.Application：Cardiolipin solution from bovine heart has been used:for coating Corning 96-well enzyme immunoassay/radioimmunoassay (EIA/RIA) plate to perform enzyme-linked immunosorbent assay (ELISA)-based cardiolipin binding assayin lipid analysis along with phosphatidylglycerol (PG) to comigrate the radiolabeled lipids to identify PG and cardiolipin (CL)in coating ELISA plates for antiphospholipid antibodies (aPL) assaysCharacteristics and advantages：High-quality molecule suitable for mulitple research applicationsCommonly employed in Metabolomics and Biochemical studies... Read More | Inquire | Inquire | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.ApplicationUseful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.Reported useful for the isolation of hepatic, yeast, and mung bean mitochondriaDetermination of enzyme localization on membranesTreatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research... Read More | Purity>95% (SDS-PAGE&HPLC) Endotoxin level<0.1 EU/µgFunctionMay regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn Purity>95% (SDS-PAGE&HPLC) Endotoxin level<0.1 EU/µgFunctionMay regulate apoptosis, cell proliferation and cell differentiation. Binds beta-galactoside and a wide array of complex carbohydrates. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase.Gal-1 is also engaged in many protein-protein interactions. Gal-1 plays a number of crucial roles in neuronal cell differentiation and survival in both the central and the peripheral nervous systems, and the establishment and maintenance of T-cell tolerance and homeostasis in vivo... Read More |