| Description | ApplicationFor the detection of lactic acid content.Enzymatic propertiesSource: MicroorganismEnzymology Committee Number: EC 1.1.3.2Molecular weight: 42 kDa (SDS-PAGE)Isoelectric point: pH 4.6Km value: 7.5 × 10-4 M (L-Lactate)Inhibitors: Hg²⁺, Pb²⁺ Optimum pH: 6.0-7.0 ApplicationFor the detection of lactic acid content.Enzymatic propertiesSource: MicroorganismEnzymology Committee Number: EC 1.1.3.2Molecular weight: 42 kDa (SDS-PAGE)Isoelectric point: pH 4.6Km value: 7.5 × 10-4 M (L-Lactate)Inhibitors: Hg²⁺, Pb²⁺ Optimum pH: 6.0-7.0 Figure 1 Optimum temperature: 50℃ Figure 2pH stability: 6.0-8.5 (25℃,16h) Figure 3 Thermal stability: Stable below 50℃ (pH7.0, 30min) Figure 4Stability: -25 ~ -15℃ standing store for 12 monthsMore than 90% activity Figure 5 Enzyme activity definitionUnit enzyme activity is defined as the amount of enzyme required to catalyze the production of 1µmol H2O2 per minute under the following conditions.Assay method for activity1. PrincipleThe amount of Quinoneimine dye produced by the reaction can be measured by spectrophotometer at 555 nm.2. Definition of enzyme activityUnit enzyme activity is defined as the amount of enzyme required to catalyze the production of 1 µmol H2O2 per minute under the following conditions.3. Reagent preparationReagent I: 0.2 MpH 6.5 potassium phosphate buffer.Reagent II: 1kU/mL peroxidase (POD) solution.Reagent III: 50 mM4-AA solution.Reagent IV: 0.5 MDL- lactic acid solution, pH6.5.Reagent V: 50 mMTOOS solution.Enzyme diluent: 10 mMpH7.0 potassium phosphate buffer containing 10 µM FAD.Sample: Dilute the enzyme with enzyme diluent to 0.05-0.2U/mL.Prepare the reaction mixture as follows:Reagent I is 10 mlReagent II 0.25 mLReagent III 1.5 mLReagent IV is 5 mLReagent V 1.5 mLDouble steam water to 50 ml4. Operation procedure4.1 Add 1mL reaction mixture into 1mL colorimetric dish.4.2 Preheat the reaction mixture at 37 °C for 5min.4.3 Add 20µL of enzyme liquid to be measured and mix well.4.4 The reaction is measured at 37 °C at 555 nm and the absorbance change (∆As) within 1min is recorded.* Replace enzyme liquid with enzyme diluent, other steps are the same, the absorbance of the resulting solution is blank absorbance (∆Ab)∆A=∆As-∆Ab5. Vitality computing1.020: total volume of reaction liquid (mL);0.020: enzyme liquid volume (mL);1: optical path length (cm);1/2:1 mole of hydrogen peroxide to generate 1/2 mole of quinone imide dye;df: dilution ratio;C: Enzyme concentration (mg/mL);39.2: Under standard reaction conditions, the millimolar absorption coefficient of the color group at 555 nm (cm2/µmol)... Read More | Inquire | H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application：H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application：H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo fibroblasts (REF52) cells and acts as a kinase inhibitor... Read More | TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification.TEV Protease is the 241 amino acid (aa), 27 kDa catalytic domain of the nuclear inclusion a (NIa) protein encoded by the potyvirus, tobacco etch virus (TEV). It may be used in biotechnology to cleave affinity tags from recombinant proteins, either co-translationally orin vitrofollowing purification. Its high specificity and activity at a wide range of pH and ionic strength make TEV Protease more versatile than many other proteases used for the same purpose. Unlike factor Xa, enteropeptidase or thrombin, TEV Protease has not been found to cleave at unintended sites, even when present at a high concentration. TEV Protease is a 3C-type protease that cleaves substrates with a consensus sequence of ENLYFQG. Cleavage occurs between Q and G. Since the final aa remains on the cleaved protein where it could potentially affect structure or function, substitution of a variety of aa have been tested. In order of efficiency, S, A, M, Y, D, N, E, K or L may be effectively used in place of G. Several of the remaining aa may also vary, giving a final consensus sequence of ExxYF(M)Q(E)/G(S, A or others) where aa in parenthesis are alternatives and x is any aa. The autocatalytic site of NIa at S2256 has been mutated to an N for improved stability of the protease.Tobacco Etch Virus Protease is a highly site-specific cysteine protease that is found in the tags from fusion proteins. The optimal temperature for cleavage is 30°C. It is recommended that the cleavage for each fusion protein be optimized by varying the amount of recombinant viral TEV protease, reaction time, or incubation temperature. It can be removed by Ni2+ affinity resin... Read More | Purity>97% SDS-PAGE.FunctionReceptor for interleukin-2 |