| Description | ApplicationIt is used in the research and development of enzymatic glycosylated albumin reagents and mass formulation.Enzymatic propertiesSource: MicroorganismEnzymology Committee Number: EC1.5.3Molecular weight: 55kDa (SDS-PAGE)Isoelectric point: 6Km value: 5.0×10 ⁻⁴ M (Fructosyl-ApplicationIt is used in the research and development of enzymatic glycosylated albumin reagents and mass formulation.Enzymatic propertiesSource: MicroorganismEnzymology Committee Number: EC1.5.3Molecular weight: 55kDa (SDS-PAGE)Isoelectric point: 6Km value: 5.0×10 ⁻⁴ M (Fructosyl-Ala)Inhibitors: Hg ²⁺, Pb ²⁺ Optimal pH: 7.7 Figure 1Optimum temperature: 42℃ Figure 2pH stability: 5.0-9.5 (25℃, 16h) Figure 3Thermal stability: Stable below 40℃ (pH8.0, 30min) Figure 4Stability: -25 ~ -15℃ standing store for 12 monthsMore than 90% activity Figure 5Protective agent: glycerin, trehaloseAssay method for activity1. Principle 2. Definition of enzyme activityUnit enzyme activity is defined as the amount of enzyme required to catalyze the production of 1µmol H2O2 per minute under the following conditions.3. Reagent preparationReagent I: 1M potassium phosphate buffer, pH8.0Reagent II: 1kU/mL PODReagent III: 50mM TOOS solutionReagent IV: 50mM 4-AA solutionReagent V: 200mM Glycated alanineEnzyme diluent: 20mM Tris-HCl, pH8.0Prepare the reaction mixture as follows:Reagent I: 10mLReagent II: 0.1mLReagent III: 1mLReagent IV: 1mLReagent V: 10mLDouble steam water set volume to 100mL4. Operation procedure4.1 Add 980µL reaction mixture into 1mL colorimetric dish.4.2 Incubate at 37°C for 5 minutes.4.3 Add 20 µL of enzyme solution to be tested to the reaction mixture.4.4 Reaction at 37°C, the absorbance change (∆As) of the sample within 1min is detected by spectrophotometer at 555nm.* Blank control measurement method: Use 20 µL of enzyme dilution solution instead of the enzyme solution to be tested, and measure the absorbance change (ΔAb) of the sample within 1 minute.∆A=∆As-∆Ab5. Vitality computingVt: Total volume of reaction liquid (1.0 mL);Vs: Enzyme liquid volume (0.02 mL);t: Reaction time (1 min);df: Dilution ratio;C: Enzyme concentration (mg/mL);1.0: Optical path length (cm);1/2: 1 mole hydrogen peroxide to generate 1/2 mole quinone imide dye;39.2: Under standard reaction conditions, the millimolar absorption coefficient of the color group at 555nm (cm² /µmol)... Read More | Inquire | Apatinib(YN-968D1) is an orally bioavailable, selective VEGFR2 inhibitor with IC50 of 1 nM | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：HSPD1, also known as HSP60, is a member of the chaperonin family. HSPD1 may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：HSPD1, also known as HSP60, is a member of the chaperonin family. HSPD1 may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. It may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSPD1 gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. Defects in HSPD1 are a cause of spastic paraplegia autosomal dominant type 13 (SPG13). Spastic paraplegia is a degenerative spinal cord disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Defects in HSPD1 are the cause of leukodystrophy hypomyelinating type 4 (HLD4); also called mitochondrial HSP60 chaperonopathy or MitCHAP-60 disease. HLD4 is a severe autosomal recessive hypomyelinating leukodystrophy. HSPD1 is clinically characterized by infantile-onset rotary nystagmus, progressive spastic paraplegia, neurologic regression, motor impairment, profound mental retardation. Death usually occurs within the first two decades of life... Read More | Purity>95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose Purity>95% SDS-PAGE.FunctionImportant adipokine involved in the control of fat metabolism and insulin sensitivity, with direct anti-diabetic, anti-atherogenic and anti-inflammatory activities. Stimulates AMPK phosphorylation and activation in the liver and the skeletal muscle, enhancing glucose utilization and fatty-acid combustion. Antagonizes TNF-alpha by negatively regulating its expression in various tissues such as liver and macrophages, and also by counteracting its effects. Inhibits endothelial NF-kappa-B signaling through a cAMP-dependent pathway. May play a role in cell growth, angiogenesis and tissue remodeling by binding and sequestering various growth factors with distinct binding affinities, depending on the type of complex, LMW, MMW or HMW.Post-translationalHydroxylated Lys-33 was not identified in PubMed:16497731, probably due to poor representation of the N-terminal peptide in mass fingerprinting. HMW complexes are more extensively glycosylated than smaller oligomers. Hydroxylation and glycosylation of the lysine residues within the collagene-like domain of adiponectin seem to be critically involved in regulating the formation and/or secretion of HMW complexes and consequently contribute to the insulin-sensitizing activity of adiponectin in hepatocytes. O-glycosylated. Not N-glycosylated. O-linked glycans on hydroxylysines consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. Sialylated to varying degrees depending on tissue. Thr-22 appears to be the major site of sialylation. Higher sialylation found in SGBS adipocytes than in HEK fibroblasts. Sialylation is not required neither for heterodimerization nor for secretion. Not sialylated on the glycosylated hydroxylysines. Desialylated forms are rapidly cleared from the circulation... Read More |