| Description | Product introductionFirefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics Product introductionFirefly luciferase is an enzyme that catalyzes production of light from luciferin in the presence of Mg2+-ATP and oxygen. The reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase activity can be inhibited by general anesthetics including isoflurane and ketamine/medetomidine thereby affecting the sensitivity of bioluminescence imaging.ApplicationThe reaction of this enzyme with luciferin, ATP, and O2 results in the emission of light. Luciferase can be used to detect trace amounts of ATP. Firefly luciferase is also one of the most commonly utilized reporter genes for the study of gene expression. The bioluminescent reaction catalyzed by luciferase is one of the most sensitive analytical tools for measuring gene expression. < or equal to one femtomole of ATP can be detected using 0.2 µg of luciferase... Read More | Cardiolipin is a unique phospholipid present in the inner mitochondrial membrane, which makes up to 20% of total lipids. It is a non-bilayer anionic phospholipid, which has four acyl chains and small headgroupHeart CA has been used as a standard stock solution for its quantitative analysis using Cardiolipin is a unique phospholipid present in the inner mitochondrial membrane, which makes up to 20% of total lipids. It is a non-bilayer anionic phospholipid, which has four acyl chains and small headgroupHeart CA has been used as a standard stock solution for its quantitative analysis using liquid chromatography?mass spectrometry (LC-MS)/MS. It has also been used for liposome preparation... Read More | Source: Microorganism Isoelectric point: 6.5 Michaelis constant: 9.2×10^-3 M (D-Glucose); 8.6×10^-3 M (NAD) Optimum pH: 9.0~9.5 Fig. 1Optimum temperature: 55℃ Fig. 3pH Stability: 6.0-10.0 (25℃, 24hr) Fig. 2Thermal stability: <50℃ (pH 8.0, Source: Microorganism Isoelectric point: 6.5 Michaelis constant: 9.2×10^-3 M (D-Glucose); 8.6×10^-3 M (NAD) Optimum pH: 9.0~9.5 Fig. 1Optimum temperature: 55℃ Fig. 3pH Stability: 6.0-10.0 (25℃, 24hr) Fig. 2Thermal stability: <50℃ (pH 8.0, 30min) Fig. 4Inhibitors: NEM,SDS Effect of various chemicals: Table 1Reaction:... Read More | Inquire | Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a Purity＞97% by SDS-PAGE and HPLC analyses.FunctionPigment epithelium-derived factor (PEDF) is encoded by the SERPINF1 gene in humans and found in verebrates. It is a secreted phosphoglycoprotein that belongs to the clade F subfamily, serpin superfamily of proteinase inhibitors. The PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. It is synthesized as a 418 a.a. about 50kDa precursor that contains a 19 a.a. signal sequence and a 399 a.a. mature region that shows a pyroglutamate at Gln20. Like other serpins, it contains three β-sheets, 810 α-helices, and a C-terminal RCL (reactive center loop). Unlike other serpins with Ser protease inhibiting activity. PEDF has functions of inducing extensive neuronal differentiation in retinoblastoma cells, inhibiting of angiogenesis. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity. PEDF is researched as a therapeutic candidate for treatment of such conditions as choroidal neovascularization, heart disease, and cancer... Read More |