| Description | FAD-dependent glucose dehydrogenase is an enzyme used as a regeneration cofactor to convert glucose and NAD(P) into NAD(P)H and gluconic acid.ORIGIN: Aspergillus oryzae CATALYSIS: SPECIFICATIONSActivity≥100 U/mg powderAppearanceYellow powder, lyophilizedStabilityStable for 36 months at -20 &#FAD-dependent glucose dehydrogenase is an enzyme used as a regeneration cofactor to convert glucose and NAD(P) into NAD(P)H and gluconic acid.ORIGIN: Aspergillus oryzae CATALYSIS: SPECIFICATIONSActivity≥100 U/mg powderAppearanceYellow powder, lyophilizedStabilityStable for 36 months at -20 ℃AdditivesNot AddedCHARACTERISTICSMolecular weight180,000 (Gel filtration)Isoelectric point6.5 Km (Glucose)15.0 × 10⁻³ M InhibitorsAg⁺, Hg²⁺ ActivatorTriton X-100 Opt. pH7.0Fig.1Opt. temperature55 ℃Fig.2Stable pH range4.0-7.0Fig.3Stable temp. rangebelow 40 ℃Fig.4Substrate specificity Table 1Mediator Preference Fig.5APPLICATIONS This enzyme is used for enzymatic determination of glucose in blood or urine by glucose sensor etc.Assay Method of Glucose Dehydrogenase (GDH-FAD)Principle1* phenadine methosulfate, 2* Nitorotetrazorium blueThe appearance of diformazan is measured at 570nm by spectrophotometry.Unit Definition One unit is defined as the enzyme quantity which produces 0.5 µmol of diformazan per minute under the conditions described below.ReagentsA. Triton X-100 Solution (5% Triton X-100 solution)Weigh 5.0 g of Triton X-100 and dissolve in 30 mL of deionized water with heating. After cooling, fill up to 100 mL with deionized water. (Expires after 1 month at room temperature)B. Working Solution (50 mmol/L PIPES-NaOH (pH 6.5) containing 0.5 % Triton X-100)Weigh 1.51 g of PIPES and dissolve in approx. 70mL of deionized water. Add 10 mL of Triton X-100 solution (A), then adjust the pH to 6.5 with 4N NaOH. Fill up to 100 mL with deionized water. (Expires after 1 month at 2~8℃)C. NTB Solution (6.6 mmol/L)Weigh 54 mg of Nitorotetrazorium blue and dissolve in 10 mL of deionized water. This solution should be kept in a light-proof tube to avoid exposure to light. (Expires after 14 days at 2~8℃)D. PMS Solution (3.0 mmol/L)Weigh 9 mg of phenazine methosulfate and dissolve in 10 mL of deionized water. This solution should be kept in a light-proof tube to avoid exposure to light. (Expires after 14 days at 2~8℃)E. Substrate Solution (1.0 mol/L Glucose)Weigh 3.6 g of D-glucose and dissolve in deionized water. Fill up to 20 mL with deionized water. (Expires after 14 days at room temperature)F. Enzyme DiluentWeigh 3.02 g of PIPES and 0.2 g of bovine serum albumin and 29.4 mg of CaCl₂·2H₂O in approx. 160 mL of deionized water. Add 4 mL of Triton X-100 solution (A), then adjust the pH to 6.5 with 4N NaOH. Fill up to 200 mL with deionized water. (Expires after 1 month at 2~8℃)G. Enzyme SolutionWeigh 25 mg of Glucose Dehydrogenase (GDH-FAD) and dissolve in chilled Enzyme Diluent (F). Enzyme Solution should be prepared so that the value of ΔOD/2minutes becomes in the range of 0.058±0.026.H. Mix SolutionMix 26 mL of Working Solution (B), 1 mL of NTB Solution (C), 2 mL of PMS Solution (D) and 1 mL of Substrate Solution (E). This solution should be kept in a light-proof tube to avoid exposure to light. (Expires 6 hours at 2~8℃)ProcedurePipette 3 mL of Mix Solution (H) into a disposable plastics cuvette (d=10 ~mm) and keep at 37±0.5 ℃ for 10 minutes. Then, pipette 0.1 mL of Enzyme Solution (E) into the cuvette and mix well immediately. Keep the reaction mixture at 37±0.5 ℃. Exactly at 3 minutes and 5 minutes after the addition of Enzyme Solution (E), measure the absorbances of the reaction mixture at 570 nm. (A3 and A5) As a blank, pipette Enzyme Diluent (F) into another disposable plastics cuvette (d=10 ~mm) instead of Enzyme Solution (E), and take the same procedure described above. (Ab3 and Ab5)Calculation2: Reaction time20.1: Half of millimolar extinction coefficient of diformazan at 570 nm3.1: Final volume of the reaction mixture0.1: Volume of Enzyme SolutionDm: Dilution multiple of Enzyme Solution... Read More | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: DCX (doublecortin, N-GST chimera)contains 2 doublecortin domains and belongs to the doublecortin family. It is highly expressed in neuronal cells of fetal brain, but not expressed in other fetal tissues. In the Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description: DCX (doublecortin, N-GST chimera)contains 2 doublecortin domains and belongs to the doublecortin family. It is highly expressed in neuronal cells of fetal brain, but not expressed in other fetal tissues. In the adult, it is highly expressed in the brain frontal lobe, but very low expression in other regions of brain, and not detected in heart, placenta, lung, liver, skeletal muscles, kidney and pancreas. DCX is a microtubule-associated protein required for initial steps of neuronal dispersion and cortex lamination during cerebral cortex development. It may act by competing with the putative neuronal protein kinase DCAMKL1 in binding to a target protein. DCX may in that way participate in a signaling pathway that is crucial for neuronal interaction before and during migration, possibly as part of a calcium ion-dependent signal transduction pathway. It may be part with LIS-1 of a overlapping, but distinct, signaling pathways that promote neuronal migration. Defects in DCX are the cause of lissencephaly X-linked type 1 and subcortical band heterotopia X-linked... Read More | Purity>95% SDS-PAGEFunctionHas hepatocyte mitogenic activity | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Histones are a complex family of highly conserved basic proteins responsible for packaging chromosomal DNA into nucleosomes. Histone proteins exhibit two levels of diversity: 1. evolutionary diversity Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Histones are a complex family of highly conserved basic proteins responsible for packaging chromosomal DNA into nucleosomes. Histone proteins exhibit two levels of diversity: 1. evolutionary diversity between species and 2. subtype diversity in a class(H1, H2A, H2B, H3 or H4) within a species. It has become more and more evident that histone modifications are key players in the regulation of chromatin states and dynamics as well as in gene expression. Therefore, histone modifications and the enzymatic machinery that set them are crucial regulators that can control cellular proliferation, differentiation, plasticity, and malignancy processes. However, extracellular histones are a double-edged sword because they also damage host tissue and may cause death. Histones bound to platelets, induced calcium influx, and recruited plasma adhesion proteins such as fibrinogen to induce platelet aggregation. Histone H2B proteins have been studied in a variety of species and are easily detected in most species. The reversible ubiquitylation of histone H2B has long been implicated in transcriptional activation and gene silencing. Phosphorylation of H2B serine 32 occurs in normal cycling and mitogen-stimulated cells. Notably, this phosphorylation is elevated in skin cancer cell lines and tissues compared with normal counterparts. HIST2H2BE is a member of the histone H2B family and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif... Read More | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: Major histocompatibility complex, class II, DR alpha (HLA-DRA) belongs to the MHC class II family. HLA-DRA binds peptides derived from antigens which access the endocytic route of antigen presenting cells (APC) Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description: Major histocompatibility complex, class II, DR alpha (HLA-DRA) belongs to the MHC class II family. HLA-DRA binds peptides derived from antigens which access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for identification by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mainly by degradation of proteins which access the endocytic route, where they are processed by lysosomal proteases and other hydrolases... Read More |